|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-231 |
1.94e-120 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 342.45 E-value: 1.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTFPI 81
Cdd:COG1121 13 TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVDWDFPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:COG1121 93 TVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 162 VSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLVASGSVESTFVTKNIQAAYGDTMGEI 231
Cdd:COG1121 173 ATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPVALL 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-209 |
1.05e-103 |
|
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: 299.06 E-value: 1.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTFPI 81
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:cd03235 86 SVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 162 VSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLVASG 209
Cdd:cd03235 166 KTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-225 |
1.97e-78 |
|
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: 236.48 E-value: 1.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR-----KKIAYVEQRSaiD 76
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSrrelaRRIAYVPQEP--P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:COG1120 86 APFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 157 VGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDL-HKTReYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLnLAAR-YADRLVLLKDgRIVAQGPPEEVLTPELLEEVYG 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-200 |
5.41e-69 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 210.17 E-value: 5.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirKKIAYVEQRSAIDLTFPIKVDEVVLL 89
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG------ARVAYVPQRSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 GTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVD 169
Cdd:NF040873 81 GRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|.
gi 2282925441 170 LLKELRNQGKTIVIVHHDLHKTREYFDNLII 200
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-238 |
1.10e-65 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 204.73 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQH-KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK--IAYVEQRSAIDL 77
Cdd:PRK15056 12 VTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK15056 92 SFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLVASGSVESTFVTKNIQAAYGDTMGEIVIKGVN 237
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHVALNGSE 251
|
.
gi 2282925441 238 D 238
Cdd:PRK15056 252 E 252
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-212 |
2.49e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.20 E-value: 2.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV----IRKKIAYVEQRSAIDL 77
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpaeVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKvDEVVLLGtfpnlGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:COG1131 87 DLTVR-ENLRFFA-----RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPD 216
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
16-209 |
2.89e-59 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 186.60 E-value: 2.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 16 VSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTFPIKVDEVVLLGTFPNL 95
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 96 GLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELR 175
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190
....*....|....*....|....*....|....
gi 2282925441 176 NQGKTIVIVHHDLHKTREYFDNLIIMNKQLVASG 209
Cdd:TIGR03771 161 GAGTAILMTTHDLAQAMATCDRVVLLNGRVIADG 194
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
1.68e-58 |
|
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: 184.84 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQ-HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG-----KSLDVIRKKIAYVEQRSAI 75
Cdd:COG1122 7 SFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkKNLRELRRKVGLVFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFPIkVDEVVLLGtfP-NLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG1122 87 QLFAPT-VEEDVAFG--PeNLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPREVF 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-209 |
4.02e-58 |
|
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: 182.25 E-value: 4.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQrsaid 76
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlspkeLARKIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 ltfpikvdevvllgtfpnlglfrrpkkaqkekvveCLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 157 VGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASG 209
Cdd:cd03214 126 SHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLkDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-203 |
2.64e-56 |
|
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: 178.43 E-value: 2.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQRSAiDLTFP 80
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkeLRRKVGLVFQNPD-DQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGtFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:cd03225 91 PTVEEEVAFG-LENLGL---PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-212 |
5.05e-55 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 176.74 E-value: 5.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQRsai 75
Cdd:PRK11231 8 LTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssRQLARRLALLPQH--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 dLTFP--IKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:PRK11231 85 -HLTPegITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANgHVMAQGTPE 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-203 |
3.22e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 171.78 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQ-HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV--------SGKSLDVIRKKIAYVEQ- 71
Cdd:COG3638 9 SKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdgqdvtalRGRALRRLRRRIGMIFQq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 ------RSAIdltfpikvdEVVLLGTFPNLG----LFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIAR 141
Cdd:COG3638 89 fnlvprLSVL---------TNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 142 ALAQEADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
2-225 |
1.42e-52 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 170.26 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQrsAID 76
Cdd:COG4604 8 SKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsRELAKRLAILRQ--ENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVVLLGTFP-NLGlfrRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:COG4604 86 INSRLTVRELVAFGRFPySKG---RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 156 FVGIDMvseKVIVDLLKELRN----QGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVESTFVTKNIQAAYG 225
Cdd:COG4604 163 LNNLDM---KHSVQMMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEIITPEVLSDIYD 234
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-225 |
1.98e-51 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 167.60 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR-----KKIAYVEQRSAid 76
Cdd:COG4559 8 SVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelaRRRAVLPQHSS-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVVLLGTFPNlglfRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQ-------EADI 149
Cdd:COG4559 86 LAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdgGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEVLTDELLERVYG 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-202 |
3.62e-51 |
|
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: 166.20 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG--------KSLDVIRKKIAYVEQRSAidLTF 79
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgKALRQLRRQIGMIFQQFN--LIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLGTFPNL----GLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:cd03256 92 RLSVLENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 156 FVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMN 202
Cdd:cd03256 172 VASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLK 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-224 |
1.09e-50 |
|
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: 165.42 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG----KSLDVIRKKIAYVEQRSAIDL 77
Cdd:COG4555 8 SKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrKEPREARRQIGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKvDEVVLLGTfpnlgLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:COG4555 88 RLTVR-ENIRYFAE-----LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVE---STFVTKNIQAAY 224
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILhKGKVVAQGSLDelrEEIGEENLEDAF 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-225 |
1.27e-48 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 160.32 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR-----KKIAYVEQRSAid 76
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelaRRRAVLPQHSS-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVVLLGTFPNlglfRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEAD------II 150
Cdd:PRK13548 87 LSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpprWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEVLTPETLRRVYG 239
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
11-225 |
2.09e-48 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 159.98 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK-----IAYVEQRSAIDLtfPIKVDE 85
Cdd:TIGR03873 17 VDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRararrVALVEQDSDTAV--PLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:TIGR03873 95 VVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 166 VIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:TIGR03873 175 ETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGgRVVAAGPPREVLTPALIRAVYG 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-212 |
3.39e-48 |
|
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: 158.60 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV--------SGKSLDVIRKKIAYVEQRS 73
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqditglSEKELYELRRRIGMLFQGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AI--DLTfpikVDEVVLlgtFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:COG1127 92 ALfdSLT----VFENVA---FPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVE 212
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPE 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-225 |
2.38e-47 |
|
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: 156.78 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLI-KTESGEVTVSGKSL---DV--IRKKIAYVEQRSAI 75
Cdd:COG1119 10 TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRggeDVweLRKRIGLVSPALQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:COG1119 90 RFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQG-KTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDgRVVAAGPKEEVLTSENLSEAFG 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-212 |
4.43e-47 |
|
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: 163.39 E-value: 4.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAY-QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI-----RKKIAYVEQRSAI 75
Cdd:COG4988 343 SFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpaswRRQIAWVPQNPYL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 dltFPIKVDEVVLLGtfpnlglfrRPKkAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALA 144
Cdd:COG4988 423 ---FAGTIRENLRLG---------RPD-ASDEELEAALEAAGLDEFVAAlpdgldtPLGeggrGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHkTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA-LLAQADRILVLDDgRIVEQGTHE 556
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-189 |
8.26e-47 |
|
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: 154.55 E-value: 8.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRsaiDLTFPIK-VDEV 86
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQ---DALLPWLtVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 87 VLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS-EK 165
Cdd:cd03293 94 VALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTrEQ 169
|
170 180
....*....|....*....|....
gi 2282925441 166 VIVDLLKELRNQGKTIVIVHHDLH 189
Cdd:cd03293 170 LQEELLDIWRETGKTVLLVTHDID 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-224 |
1.05e-46 |
|
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: 161.61 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV--------IRKKIAYVEQ--RSAI 75
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrslreLRRRVQMVFQdpYSSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFPIKvDEVvllgTFPNLGLFRRPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG1123 356 NPRMTVG-DII----AEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFvtKNIQAAY 224
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDgRIVEDGPTEEVF--ANPQHPY 500
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-203 |
1.26e-46 |
|
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: 152.55 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL----DVIRKKIAYVEQRSAIdl 77
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkepEEVKRRIGYLPEEPSL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 tfpikvdevvllgtFPNLglfrrpkkaqkeKVVECLKqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:cd03230 85 --------------YENL------------TVRENLK--------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-212 |
3.65e-46 |
|
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: 153.43 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS--------LDVIRKKIAYVEQRS 73
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaeLYRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AI--DLTfpikVDEVVllgTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:cd03261 87 ALfdSLT----VFENV---AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVE 212
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPE 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-209 |
3.79e-46 |
|
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: 153.05 E-value: 3.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL--------DVIRKKIAYVEQ--RSAID 76
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrlrKIRRKEIQMVFQdpMSSLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIK--VDEVVLLGTFPnlglfrRPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:cd03257 97 PRMTIGeqIAEPLRIHGKL------SKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03257 171 EPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAgKIVEEG 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-212 |
3.81e-46 |
|
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: 153.36 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYVEQRSAI--DLTfp 80
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglpphEIARLGIGRTFQIPRLfpELT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikVDEVVLLG------TFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:cd03219 92 --VLENVMVAaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPD 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-202 |
2.75e-45 |
|
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: 151.30 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG--------KSLDVIRKKIAYVEQRsaIDLTF 79
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgKKLRKLRRRIGMIFQH--YNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVL---LGTFPNL-GLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:TIGR02315 93 RLTVLENVLhgrLGYKPTWrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 156 FVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMN 202
Cdd:TIGR02315 173 IASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-187 |
1.02e-44 |
|
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: 149.18 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL---------DVIRKKIAYVEQRSAI- 75
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekelaAFRRRHIGFVFQSFNLl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 -DLTfpikVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:cd03255 95 pDLT----ALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190
....*....|....*....|....*....|....
gi 2282925441 155 PFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHD 187
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD 200
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-203 |
1.51e-44 |
|
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: 148.44 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK---SLDVIRKKIAYVEQRSAIdlt 78
Cdd:cd03259 7 SKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtGVPPERRNIGMVFQDYAL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FP-IKVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:cd03259 84 FPhLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2282925441 158 GIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-187 |
3.87e-44 |
|
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: 147.24 E-value: 3.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL----DVIRKKIAYVEQRSAI-- 75
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdarEDYRRRLAYLGHADGLkp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTfpikVDEvvllgtfpNLGLFRR--PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:COG4133 89 ELT----VRE--------NLRFWAAlyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-215 |
2.53e-43 |
|
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: 152.75 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQH--KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE---SGEVTVSGKSL-----DVIRKKIAYVEQ 71
Cdd:COG1123 11 SVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelseALRGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 RSAIDLtFPIKVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:COG1123 91 DPMTQL-NPVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEIL 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-215 |
2.93e-43 |
|
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: 147.21 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG--------KSLDVIRKKIAYVEQrsaidltF 79
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditakkkKKLKDLRKKVGLVFQ-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIK------VDEVVLLGtfP-NLGLfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:TIGR04521 91 PEHqlfeetVYKDIAFG--PkNLGL---SEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPREVF 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-188 |
3.53e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.39 E-value: 3.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRsaiDLTFPIK-VDEVVL 88
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQE---PALLPWLtVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 89 LGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS-EKVI 167
Cdd:COG1116 103 LG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrERLQ 178
|
170 180
....*....|....*....|.
gi 2282925441 168 VDLLKELRNQGKTIVIVHHDL 188
Cdd:COG1116 179 DELLRLWQETGKTVLFVTHDV 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-212 |
1.25e-42 |
|
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: 144.56 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-----VIRKKIAYVEQ--RSAID 76
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrrrrkAFRRRVQMVFQdpYASLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 ltfPIK-VDEVVLLGtfpnLGLFRRPkkAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG1124 94 ---PRHtVDRILAEP----LRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG1124 165 PTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNgRIVEELTVA 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-225 |
7.33e-42 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 146.91 E-value: 7.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQRSAidLTFPIKVDE 85
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealSARAASRRVASVPQDTS--LSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 166 VIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVESTFVTKNIQAAYG 225
Cdd:PRK09536 177 RTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFD 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-235 |
8.94e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.71 E-value: 8.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-VIRKKIAYV-EQRSaidLtFP-I 81
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpEDRRRIGYLpEERG---L-YPkM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVL-LGTFPNLglfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRV-FIArALAQEADIIFLDEPFVGI 159
Cdd:COG4152 87 KVGEQLVyLARLKGL-----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIA-ALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVEStfvtknIQAAYGDTMGEIVIKG 235
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKgRKVLSGSVDE------IRRQFGRNTLRLEADG 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-203 |
1.65e-41 |
|
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: 138.92 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI-----RKKIAYVEQrsaid 76
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpleelRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 ltfpikvdevvllgtfpnlglfrrpkkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-210 |
1.70e-41 |
|
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: 149.98 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsaidltfp 80
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqiDPASLRRQIGVVLQ--------- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikvdEVVLL-GT-FPNLGLFRrpKKAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEA 147
Cdd:COG2274 557 ----DVFLFsGTiRENITLGD--PDATDEEIIEAARLAGLHDFIEAlpmgydtVVGeggsNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHkTREYFDNLIIMNK-QLVASGS 210
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLS-TIRLADRIIVLDKgRIVEDGT 692
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-212 |
1.85e-41 |
|
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: 140.65 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYVEQRSAI 75
Cdd:cd03224 7 NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglpphERARAGIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 --DLTfpikVDEVVLLGTFPnlgLFRRPKKAQKEKVVEC---LKQvkmedFSNRQIGNLSGGQLQRVFIARALAQEADII 150
Cdd:cd03224 87 fpELT----VEENLLLGAYA---RRRAKRKARLERVYELfprLKE-----RRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 151 FLDEPFVGI--DMVSEkvIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:cd03224 155 LLDEPSEGLapKIVEE--IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERgRVVLEGTAA 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-215 |
2.74e-41 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 140.79 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV--------SGKSLDVIRKKIAYVEQ-------RS 73
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdgtdltllSGKELRKARRRIGMIFQhfnllssRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AID-LTFPIKVDEVvllgtfpnlglfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:cd03258 99 VFEnVALPLEIAGV--------------PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKgEVVEEGTVEEVF 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-210 |
3.57e-41 |
|
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: 147.61 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAY--QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQRSA 74
Cdd:COG4987 340 SFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdldeDDLRRRIAVVPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 IdltFPIKVDEVVLLGtfpnlglfrRPKkAQKEKVVECLKQVKMEDFSNRQ-------IG----NLSGGQLQRVFIARAL 143
Cdd:COG4987 420 L---FDTTLRENLRLA---------RPD-ATDEELWAALERVGLGDWLAALpdgldtwLGeggrRLSGGERRRLALARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHkTREYFDNLIIM-NKQLVASGS 210
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLA-GLERMDRILVLeDGRIVEQGT 552
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-224 |
3.76e-41 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 140.94 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD------VIRKKIAYVEQRSAI--DLTfp 80
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphrIARLGIARTFQNPRLfpELT-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikVDEVVLLG-----------TFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:COG0411 96 --VLENVLVAaharlgrgllaALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 150 IFLDEPFVGIDmVSEKV-IVDLLKELR-NQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVEStfVTKN--IQAAY 224
Cdd:COG0411 174 LLLDEPAAGLN-PEETEeLAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTPAE--VRADprVIEAY 250
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-203 |
2.78e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.25 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-----VIRKKIAYVEQRSAI- 75
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSampppEWRRQVAYVPQEPALw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 ------DLTFPIKVdevvllgtfpnlglfrRPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEAD 148
Cdd:COG4619 87 ggtvrdNLPFPFQL----------------RERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 149 IIFLDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-215 |
3.42e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 139.10 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG------KSLDVIRKKIAYVEQR------S 73
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWEIRKKVGMVFQNpdnqfvG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AIdltfpikVDEVVLLGtfP-NLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:TIGR04520 93 AT-------VEDDVAFG--LeNLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRN-QGKTIVIVHHDLHKTREYfDNLIIMNK-QLVASGSVESTF 215
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLA-DRVIVMNKgKIVAEGTPREIF 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-202 |
7.32e-40 |
|
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: 135.39 E-value: 7.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-------VIRKKIAYVEQRSAIdl 77
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledelpPLRRRIGMVFQDFAL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 tfpikvdevvllgtFPNlglfrrpkkaqkekvveclkqvkMEDFSNRQIGnLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:cd03229 88 --------------FPH-----------------------LTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 158 GIDMVSEKVIVDLLKELR-NQGKTIVIVHHDLHKTREYFDNLIIMN 202
Cdd:cd03229 130 ALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-224 |
9.74e-40 |
|
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: 136.65 E-value: 9.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYVEQRSAI 75
Cdd:COG0410 10 HAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpphRIARLGIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 --DLTfpikVDEvvllgtfpNL--GLFRRPKKAQKEKVVEclkQV-----KMEDFSNRQIGNLSGGQLQRVFIARALAQE 146
Cdd:COG0410 90 fpSLT----VEE--------NLllGAYARRDRAEVRADLE---RVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 147 ADIIFLDEPFVGI--DMVSEkvIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAA 223
Cdd:COG0410 155 PKLLLLDEPSLGLapLIVEE--IFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERgRIVLEGTAAELLADPEVREA 232
|
.
gi 2282925441 224 Y 224
Cdd:COG0410 233 Y 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-225 |
1.61e-39 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 137.43 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-VIRKKIAYVEQRSAIDLTF 79
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 P--IKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK10253 93 PgdITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 158 GIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPKEIVTAELIERIYG 242
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-212 |
1.68e-39 |
|
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: 136.16 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKA---MIGLIKTE--SGEVTVSGK-----SLDVI--RKKIAYV 69
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPGApdEGEVLLDGKdiydlDVDVLelRRRVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 70 EQRSAIdltFPIKVDEVVLLGtfPNLGLfRRPKKAQKEKVVECLKQVKM-EDFSNRQIG-NLSGGQLQRVFIARALAQEA 147
Cdd:cd03260 87 FQKPNP---FPGSIYDNVAYG--LRLHG-IKLKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNgRLVEFGPTE 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
11-157 |
6.91e-39 |
|
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: 132.00 E-value: 6.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI-----RKKIAYVEQRSAIDLTfpIKVDE 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerkslRKEIGYVFQDPQLFPR--LTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 86 VVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGN----LSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:pfam00005 79 NLRLG----LLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-203 |
1.51e-38 |
|
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: 131.74 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAY--QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQRSA 74
Cdd:cd03228 7 SFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdlDLESLRKNIAYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 IdltFPikvdevvllGT-FPNLglfrrpkkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:cd03228 87 L---FS---------GTiRENI---------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHkTREYFDNLIIMNK 203
Cdd:cd03228 122 EATSALDPETEALILEALRALA-KGKTVIVIAHRLS-TIRDADRIIVLDD 169
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-209 |
1.96e-38 |
|
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: 132.79 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-IRKKIAYV-EQRSaidLTF 79
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIaARNRIGYLpEERG---LYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKV-DEVVLLGTFPNLglfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:cd03269 84 KMKViDQLVYLAQLKGL-----KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 159 IDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKgRAVLYG 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-212 |
2.07e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK----SLDVIRKKIAYVEQRSAIdltfpikvd 84
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRERRVGFVFQHYAL--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 evvllgtFPNL--------GL--FRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG1118 87 -------FPHMtvaeniafGLrvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 155 PFVGIDmvsEKVIVDLLKELRN----QGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG1118 160 PFGALD---AKVRKELRRWLRRlhdeLGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPD 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-210 |
2.86e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 2.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---RKKIAYVEQRSAIdlt 78
Cdd:COG3842 12 SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRNVGMVFQDYAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 fpikvdevvllgtFPNL--------GL-FRR-PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEAD 148
Cdd:COG3842 89 -------------FPHLtvaenvafGLrMRGvPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 149 IIFLDEPFVGID------MVSEkvIVDLLKELrnqGKTIVIVHHDLHktrEYF---DNLIIMNK-QLVASGS 210
Cdd:COG3842 156 VLLLDEPLSALDaklreeMREE--LRRLQREL---GITFIYVTHDQE---EALalaDRIAVMNDgRIEQVGT 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-211 |
3.84e-38 |
|
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: 132.24 E-value: 3.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL----DVIRKKIAYVEQRSAIDLTFpiKV 83
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrKAARQSLGYCPQFDALFDEL--TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLgtfpnLGLFR-RPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMV 162
Cdd:cd03263 93 REHLRF-----YARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 163 SEKVIVDLLKELRnQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSV 211
Cdd:cd03263 168 SRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDgKLRCIGSP 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-201 |
4.03e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.47 E-value: 4.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS--------LDVIR-KKIAYVEQRSAI--DL 77
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslsereLARLRrRHIGFVFQFFNLlpEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TfpikVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:COG1136 102 T----ALENVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2282925441 158 GIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHkTREYFDNLIIM 201
Cdd:COG1136 174 NLDSKTGEEVLELLRELnRELGTTIVMVTHDPE-LAARADRVIRL 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-215 |
1.05e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 131.65 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-------IRKKIAYVEQ----- 71
Cdd:COG1126 10 SFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdinkLRRKVGMVFQqfnlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 --RSAID-LTF-PIKVdevvllgtfpnlglFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEA 147
Cdd:COG1126 90 phLTVLEnVTLaPIKV--------------KKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 148 DIIFLDEPFVGID--MVSEkvIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG1126 156 KVMLFDEPTSALDpeLVGE--VLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGgRIVEEGPPEEFF 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-209 |
4.53e-37 |
|
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: 129.41 E-value: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVIRKKIAyVEQR----SAIDLTFP-I 81
Cdd:cd03266 17 TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAE-ARRRlgfvSDSTGLYDrL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLgtFPNL-GLFRRPKKAQKEKVVEclkQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:cd03266 94 TARENLEY--FAGLyGLKGDELTARLEELAD---RLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRgRVVYEG 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
2-188 |
9.38e-37 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 128.12 E-value: 9.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---------KSLDVIRKKIAYVEQR 72
Cdd:TIGR03608 5 SKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetpplnskKASKFRREKLGYLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 SAI--DLTfpikVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADII 150
Cdd:TIGR03608 85 FALieNET----VEENLDLG----LKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-209 |
1.10e-36 |
|
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: 128.10 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDvirKKIAYVEQRSAIdLTFPIKVD 84
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ---KNIEALRRIGAL-IEAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EvvlLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSE 164
Cdd:cd03268 86 N---LTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 165 KVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKgKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-209 |
1.75e-36 |
|
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: 127.69 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGkITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG----KSLDVIRKKIAYVEQrsaiDL 77
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlKQPQKLRRRIGYLPQ----EF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFP--IKVDEVV-LLGTfpnlgLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:cd03264 82 GVYpnFTVREFLdYIAW-----LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELrNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKgKLVFEG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-189 |
2.03e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.86 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI--------RKKIAYVEQ-------R 72
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreipylRRRIGVVFQdfrllpdR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 SAID-LTFPIKVdevvlLGtfpnlglfrRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:COG2884 95 TVYEnVALPLRV-----TG---------KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLH 189
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
5.02e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 128.27 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG-------KSLDVIRKKIAYVEQRSAiDLTFPIK 82
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkKSLLEVRKTVGIVFQNPD-DQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMV 162
Cdd:PRK13639 96 VEEDVAFGPL-NLGL---SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 163 SEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNI 220
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDgKIIKEGTPKEVFSDIET 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-213 |
5.76e-36 |
|
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: 126.87 E-value: 5.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV------IRKKIAYVEQRSAI 75
Cdd:TIGR03410 7 NVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlppherARAGIAYVPQGREI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 dltFP-IKVDEVVLLGtfpnLGLFRRPKKAQKEKVVEcLKQVkMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:TIGR03410 87 ---FPrLTVEENLLTG----LAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGK-TIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVES 213
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERgRVVASGAGDE 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-203 |
6.14e-36 |
|
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: 126.49 E-value: 6.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-------IRKKIAYVEQ----- 71
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknineLRQKVGMVFQqfnlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 --RSAID-LTF-PIKVdevvllgtfpnlglFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEA 147
Cdd:cd03262 89 phLTVLEnITLaPIKV--------------KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 148 DIIFLDEPFVGID--MVSEkvIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03262 155 KVMLFDEPTSALDpeLVGE--VLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-212 |
6.82e-36 |
|
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: 126.33 E-value: 6.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG----KSLDVIRKKIAYVEQRSAIDltfpikvDE 85
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQDLSVD-------DE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vvlLGTFPNLGLFRR----PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:cd03265 88 ---LTGWENLYIHARlygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 162 VSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:cd03265 165 QTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEGTPE 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-203 |
3.53e-35 |
|
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: 125.04 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS---LDVIRKKIAYVEQRSAIdltFP 80
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHKRPVNTVFQNYAL---FP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 -IKVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:cd03300 86 hLTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2282925441 160 DMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03300 162 DLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-210 |
4.73e-35 |
|
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: 125.11 E-value: 4.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKaMIG-LIKTESGEVTVSGK---SLDVI--RKKIAYVEQRsaIDLtFP- 80
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINrLIEPTSGEIFIDGEdirEQDPVelRRKIGYVIQQ--IGL-FPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVllGTFPNLGLFRRPKKaqKEKVVECLKQVKMED--FSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:cd03295 90 MTVEENI--ALVPKLLKWPKEKI--RERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 159 IDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGS 210
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNgEIVQVGT 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-210 |
5.57e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.67 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsaidltfpik 82
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdlTLESLRRQIGVVPQ----------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 vdEVVLL-GT-FPNLGLFRrpKKAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEADI 149
Cdd:COG1132 422 --DTFLFsGTiRENIRYGR--PDATDEEVEEAAKAAQAHEFIEAlpdgydtVVGergvNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHkTREYFDNLIIMNK-QLVASGS 210
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLS-TIRNADRILVLDDgRIVEQGT 557
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-189 |
7.41e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 7.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKA---MIGLI---KTEsGEVTVSG-----KSLDVI--RKKIAY 68
Cdd:COG1117 18 NVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIpgaRVE-GEILLDGediydPDVDVVelRRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 69 VEQRSAIdltFPIKVDEVVLLGtfPNL-GLfrRPKKAQKEKVVECLKQ------VKmeDFSNRQIGNLSGGQLQRVFIAR 141
Cdd:COG1117 97 VFQKPNP---FPKSIYDNVAYG--LRLhGI--KSKSELDEIVEESLRKaalwdeVK--DRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 142 ALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLH 189
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQ 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
9.61e-35 |
|
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: 129.71 E-value: 9.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHK-KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQRSAI 75
Cdd:TIGR02857 328 SVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadaDSWRDQIAWVPQHPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 dltFPIKVDEVVLLGTfpnlglfrrpKKAQKEKVVECLKQVKMEDFS-------NRQIGN----LSGGQLQRVFIARALA 144
Cdd:TIGR02857 408 ---FAGTIAENIRLAR----------PDASDAEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHKTREYfDNLIIM 201
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-202 |
1.36e-34 |
|
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: 122.75 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK--SLDVIRKKIAYVEQRSAIDLtFPIKVDE 85
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQDVDYQL-FTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTfpnlglfrRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:cd03226 92 ELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 2282925441 166 VIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMN 202
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-215 |
2.06e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQRSaiDLTF- 79
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvwdVRRQVGMVFQNP--DNQFv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLGtFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK13635 96 GATVQDDVAFG-LENIGV---PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVI-VHHDLHKTREYfDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13635 172 DPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQA-DRVIVMNKgEILEEGTPEEIF 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
14-225 |
2.32e-34 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 123.41 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIkTESGEVTVSGKSLD--------VIRkkiAYVEQRSaiDLTFPIKVde 85
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdwsaaelaRHR---AYLSQQQ--SPPFAMPV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vvllgtFPNLGLFRRPK--KAQKEKVVECL-KQVKMEDFSNRQIGNLSGGQLQRVFIARALAQ-------EADIIFLDEP 155
Cdd:COG4138 87 ------FQYLALHQPAGasSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 156 FVGIDmVSEKVIVD-LLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:COG4138 161 MNSLD-VAQQAALDrLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEVMTPENLSEVFG 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
1.05e-33 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 121.76 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirKKIAYVEQRSAIDLTFP 80
Cdd:PRK09544 10 VSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------LRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLgtfpnlglfrRPkKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK09544 84 LTVNRFLRL----------RP-GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 161 MVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNKQLVASGSVE 212
Cdd:PRK09544 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-209 |
1.70e-33 |
|
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: 120.39 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---KSLD--VIRKKIAYVEQrsaidltfp 80
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDpaDLRRNIGYVPQ--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikvdEVVLL-GTF-PNLGLFRRPkkAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEA 147
Cdd:cd03245 86 ----DVTLFyGTLrDNITLGAPL--ADDERILRAAELAGVTDFVNKhpngldlQIGergrGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVhhdLHKTR--EYFDNLIIMNK-QLVASG 209
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIII---THRPSllDLVDRIIVMDSgRIVADG 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-215 |
2.95e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 122.49 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKK----AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV--------SGKSLDVIRKKIAYV 69
Cdd:COG1135 8 SKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdltalSERELRAARRKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 70 -------EQRSAID-LTFPIKVDEVvllgtfpnlglfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIAR 141
Cdd:COG1135 88 fqhfnllSSRTVAEnVALPLEIAGV--------------PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 142 ALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENgRIVEQGPVLDVF 229
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-209 |
3.29e-33 |
|
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: 126.52 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---KSLDV--IRKKIAYVEQrsaidltfp 80
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdiRQIDPadLRRNIGYVPQ--------- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikvDEVVLLGTF-PNLGLFRRpkKAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEAD 148
Cdd:TIGR03375 547 ---DPRLFYGTLrDNIALGAP--YADDEEILRAAELAGVTEFVRRhpdgldmQIGergrSLSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 149 IIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHkTREYFDNLIIMNK-QLVASG 209
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS-LLDLVDRIIVMDNgRIVADG 681
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-212 |
3.52e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.00 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQRSAiDLTFPIKV 83
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwVRSKVGLVFQDPD-DQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:PRK13647 98 WDDVAFGPV-NMGL---DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 164 EKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEgRVLAEGDKS 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
2-188 |
3.93e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.47 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAieNVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRkkiayVEQRsaidltfPI 81
Cdd:COG3840 8 TYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PAER-------PV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KV--DEVVLlgtFP------NLGLFRRPK----KAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:COG3840 74 SMlfQENNL---FPhltvaqNIGLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDL 188
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDP 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-212 |
4.27e-33 |
|
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: 119.57 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVI--------RKKIAYVEQRSAI- 75
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG--QDITklpmhkraRLGIGYLPQEASIf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 -DLTfpikVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:cd03218 88 rKLT----VEENILAV----LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEgKVLAEGTPE 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
8-219 |
5.21e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 120.70 E-value: 5.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---------KSLDVIRKKIAYVEQRSAIDLt 78
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKLRKKVSLVFQFPEAQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKVDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK13641 99 FENTVLKDVEFGPK-NFGF---SEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKN 219
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHgKLIKHASPKEIFSDKE 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-203 |
8.57e-33 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 118.98 E-value: 8.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK---SLDVIRKKIAYVEQRSAIdltFP-IKVD 84
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatDVPVQERNVGFVFQHYAL---FRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSE 164
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 165 KVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03296 173 KELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-187 |
1.17e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.20 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL---DVIRkkiAYVEQRSAIdltFP-I 81
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGADR---GVVFQKDAL---LPwL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID- 160
Cdd:COG4525 92 NVLDNVAFG----LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDa 167
|
170 180
....*....|....*....|....*..
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:COG4525 168 LTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-202 |
4.83e-32 |
|
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: 116.03 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirkkIAYVEQRSAIdltFPIKVDEVV 87
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEPWI---QNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 LLGtfpnlglfrRPKKAQK-EKVVE--CLKQ--VKMEDFSNRQIG----NLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:cd03250 87 LFG---------KPFDEERyEKVIKacALEPdlEILPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 159 IDMVSEKVIVD--LLKELRNqGKTIVIVHHDLHKTReYFDNLIIMN 202
Cdd:cd03250 158 VDAHVGRHIFEncILGLLLN-NKTRILVTHQLQLLP-HADQIVVLD 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-212 |
6.95e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 117.36 E-value: 6.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---------RKKIAYVEQ-------RS 73
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVFQsfallphRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AID-LTFPIKVDEVvllgtfpnlglfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:cd03294 119 VLEnVAFGLEVQGV--------------PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDgRLVQVGTPE 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-212 |
7.47e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.28 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKslDVI--------RKKIAYVEQRSAI- 75
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE--DIThlpmhkraRLGIGYLPQEASIf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 -DLTfpikVDEVVLLgtfpNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG1137 91 rKLT----VEDNILA----VLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKT-----REYfdnlIIMNKQLVASGSVE 212
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETlgicdRAY----IISEGKVLAEGTPE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-187 |
8.26e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.02 E-value: 8.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK---SLDVIRKKIAYVEQRSAI--- 75
Cdd:COG3839 10 SKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtDLPPKDRNIAMVFQSYALyph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 -----DLTFPIKVDevvllgtfpnlglfRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADII 150
Cdd:COG3839 90 mtvyeNIAFPLKLR--------------KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2282925441 151 FLDEPFVGID------MVSEkvIVDLLKELrnqGKTIVIVHHD 187
Cdd:COG3839 156 LLDEPLSNLDaklrveMRAE--IKRLHRRL---GTTTIYVTHD 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-225 |
1.15e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.43 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV---------SGKSLDVIRKKIAYVEQRSAIDLt 78
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLKPLRKKVGIVFQFPEHQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKVDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK13634 99 FEETVEKDICFGPM-NFGV---SEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 158 GIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKgTVFLQGTPREIFADPDELEAIG 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-203 |
1.72e-31 |
|
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: 115.51 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVIRKKIAYVEQRSAI-----DLTF 79
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVVfgqktQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLgtfpNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:cd03267 109 DLPVIDSFYL----LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2282925441 160 DMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-203 |
1.86e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 116.27 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLI---KTESGEVTVSGKSLDV-------IRKKIA--- 67
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlardIRKSRAntg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 68 YVEQRsaIDLTFPIKVDEVVLLGTFPNLGLFRRP----KKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARAL 143
Cdd:PRK09984 90 YIFQQ--FNLVNRLSVLENVLIGALGSTPFWRTCfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-223 |
2.25e-31 |
|
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: 116.06 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSaIDLTF---P 80
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRD-VQLVFqdsP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGTF---PNLGLFRRPKKAQKEKVVECLKQVKME-DFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:TIGR02769 99 SAVNPRMTVRQIigePLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKT-IVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF-----VTKNIQAA 223
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKgQIVEECDVAQLLsfkhpAGRNLQSA 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-201 |
2.50e-31 |
|
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: 117.08 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIK---TESGEV--------TVSGKSLDVIR-KKIAYVEQ--RSA 74
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEIlfdgedllKLSEKELRKIRgREIQMIFQdpMTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 IDLTFPIK--VDEVVLLgtfpnlgLFRRPKKAQKEKVVECLKQVKM---EDFSNRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:COG0444 99 LNPVMTVGdqIAEPLRI-------HGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-229 |
2.93e-31 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 115.66 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKaMIGLIKTES-GEVTVSGKSLD-----VIRKKIAYVEQR--SAIDLTfpikVDE 85
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSeGEILLDAQPLEswsskAFARKVAYLPQQlpAAEGMT----VRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 166 VIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYGDTMG 229
Cdd:PRK10575 185 DVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGTPAELMRGETLEQIYGIPMG 250
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-207 |
6.16e-31 |
|
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: 112.64 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE--SGEVTVSGKSLD--VIRKKIAYVEQrsaidltfpik 82
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDkrSFRKIIGYVPQ----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 vDEVVllgtFPNLglfrrpkkaqkeKVVECLkqvkmeDFSnRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMV 162
Cdd:cd03213 90 -DDIL----HPTL------------TVRETL------MFA-AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2282925441 163 SEKVIVDLLKELRNQGKTIVIVhhdLHKTR----EYFDNLIIMNKQLVA 207
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICS---IHQPSseifELFDKLLLLSQGRVI 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-209 |
8.57e-31 |
|
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: 113.52 E-value: 8.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLI---KTESGEVTVSGKSL--DVIRKKIAYVEQRsaiDLTFP-I 81
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRkpDQFQKCVAYVRQD---DILLPgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVllgTF-PNLGLFRRPKKAQKEKVVE--CLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:cd03234 97 TVRETL---TYtAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 159 IDMVSEKVIVDLLKELRNQGKTIVIvhhDLHKTR----EYFDNLIIMNK-QLVASG 209
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVIL---TIHQPRsdlfRLFDRILLLSSgEIVYSG 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-215 |
1.16e-30 |
|
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: 113.20 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK---SLDVIRKKIAYVEQRSAIdltFP-IKVDEV 86
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRDISYVPQNYAL---FPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 87 VLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKV 166
Cdd:cd03299 92 IAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 167 IVDLLKELRNQGKTIVI-VHHDLHKTREYFDNL-IIMNKQLVASGSVESTF 215
Cdd:cd03299 168 LREELKKIRKEFGVTVLhVTHDFEEAWALADKVaIMLNGKLIQVGKPEEVF 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
14-225 |
4.20e-30 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 112.33 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIkTESGEVTVSGKSLD--------VIRkkiAYVEQRSaidlTFPIKVDe 85
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaaelaRHR---AYLSQQQ----TPPFAMP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vvllgTFPNLGLFRRPK--KAQKEKVVECL-KQVKMEDFSNRQIGNLSGGQLQRVFIARALAQ-------EADIIFLDEP 155
Cdd:PRK03695 86 -----VFQYLTLHQPDKtrTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 156 FVGIDmVSEKVIVD-LLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYG 225
Cdd:PRK03695 161 MNSLD-VAQQAALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQgKLLASGRRDEVLTPENLAQVFG 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-220 |
8.72e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.01 E-value: 8.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEV-----TVSGKSLDVIRKKIAYVEQRSaiDLTF- 79
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgiTISKENLKEIRKKIGIIFQNP--DNQFi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK13632 98 GATVEDDIAFG----LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 160 DMVSEKVIVDLLKELRNQG-KTIVIVHHDLHKTREYfDNLIIMNK-QLVASGSVESTFVTKNI 220
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILA-DKVIVFSEgKLIAQGKPKEILNNKEI 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-212 |
9.71e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.87 E-value: 9.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVIRKKIAYVE-------QRSAI-- 75
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKEFARrigvvfgQRSQLww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFpikVDEVVLLGTfpnlgLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:COG4586 110 DLPA---IDSFRLLKA-----IYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 156 FVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHgRIIYDGSLE 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-224 |
1.57e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 110.75 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI------RKKIAYVEQRSAIDL 77
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplharaRRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKVDEVVLLGTFPNLGlfrrpKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLS-----AEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAY 224
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-209 |
4.20e-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: 108.73 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 15 SVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---KSLDVIRKKIAYVEQRSAIdltFP-IKVDEVVLLG 90
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRPVSMLFQENNL---FAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLfrrpKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDL 170
Cdd:cd03298 95 LSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2282925441 171 LKEL-RNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASG 209
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLdNGRIAAQG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-203 |
5.85e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.33 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKslDVIR-----KKIAYVEQRSAI------ 75
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRlhardRKVGFVFQHYALfrhmtv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 --DLTFPIKVdevvllgtfpnLGLFRRPKKAQ-KEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:PRK10851 92 fdNIAFGLTV-----------LPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNQGK-TIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-188 |
8.05e-29 |
|
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: 113.22 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQRSAIdltFPIKVD 84
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssldqDEVRRRVSVCAQDAHL---FDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGtfpnlglfrRPkKAQKEKVVECLKQVKMEDFSNRQIGNL-----------SGGQLQRVFIARALAQEADIIFLD 153
Cdd:TIGR02868 427 ENLRLA---------RP-DATDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 2282925441 154 EPFVGIDM-VSEKVIVDLLKELrnQGKTIVIVHHDL 188
Cdd:TIGR02868 497 EPTEHLDAeTADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-214 |
1.68e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYVEQRSAI--DLTfp 80
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprDAQAAGIAIIHQELNLvpNLS-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikVDEVVLLGTFP-NLGLFRRpkKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:COG1129 96 --VAENIFLGREPrRGGLIDW--RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 160 DmVSEKVIV-DLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVEST 214
Cdd:COG1129 172 T-EREVERLfRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLrDGRLVGTGPVAEL 227
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-212 |
3.46e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 107.12 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKslDVIRKK---IAyveqRSAI---------- 75
Cdd:COG4674 24 KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT--DLTGLDeheIA----RLGIgrkfqkptvf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 -DLTfpikVDEVVLL------GTFPNlgLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEAD 148
Cdd:COG4674 98 eELT----VFENLELalkgdrGVFAS--LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 149 IIFLDEPFVGI-DMVSEKViVDLLKELRnQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG4674 172 LLLLDEPVAGMtDAETERT-AELLKSLA-GKHSVVVVEHDMEFVRQIARKVTVLHQgSVLAEGSLD 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-214 |
4.98e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYVEQ-RSAID-LTfp 80
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprDAIALGIGMVHQhFMLVPnLT-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikVDEVVLLGTFPNLGLFRRPKKAqKEKVVECLKQVKME-DFsNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP---- 155
Cdd:COG3845 97 --VAENIVLGLEPTKGGRLDRKAA-RARIRELSERYGLDvDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPtavl 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 156 --------FvgidmvsekvivDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVEST 214
Cdd:COG3845 173 tpqeadelF------------EILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRgKVVGTVDTAET 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
5.38e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 107.63 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIayVEQRSAIDLT--------FPI 81
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGL--MKLRESVGMVfqdpdnqlFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:PRK13636 99 SVYQDVSFGAV-NLKL---PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 162 VSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNI 220
Cdd:PRK13636 175 MGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEgRVILQGNPKEVFAEKEM 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-184 |
5.39e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV-E--QRSAIDL 77
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprDAIRAGIAYVpEdrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKvDEVVL--LGTFPNLGLFRRpkKAQKEKVVECLKQ--VKMEDfSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:COG1129 344 DLSIR-ENITLasLDRLSRGGLLDR--RRERALAEEYIKRlrIKTPS-PEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190
....*....|....*....|....*....|..
gi 2282925441 154 EPFVGIDmVSEKV-IVDLLKELRNQGKTIVIV 184
Cdd:COG1129 420 EPTRGID-VGAKAeIYRLIRELAAEGKAVIVI 450
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-209 |
7.44e-28 |
|
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: 105.45 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 20 PGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTFpikvDEVVLlgtFPNL---- 95
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVF----QQYAL---FPHLnvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 96 ----GLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLL 171
Cdd:cd03297 95 nlafGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 172 KELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03297 175 KQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDgRLQYIG 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-206 |
8.75e-28 |
|
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: 104.22 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQRsaiDLTFPIKVDE 85
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwDPNELGDHVGYLPQD---DELFSGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVllgtfpnlglfrrpkkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:cd03246 95 NI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2282925441 166 VIVDLLKELRNQGKTIVIVHHDLhKTREYFDNLIIMNKQLV 206
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-209 |
1.90e-27 |
|
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: 103.16 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL----DVIRKKIAYVEQRsaidltfpi 81
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsdleKALSSLISVLNQR--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 kvdeVVLLGT--FPNLGlfRRpkkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:cd03247 84 ----PYLFDTtlRNNLG--RR----------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 160 DMVSEKVIVDLL-KELRNqgKTIVIVHHDLhKTREYFDNLIIM-NKQLVASG 209
Cdd:cd03247 130 DPITERQLLSLIfEVLKD--KTLIWITHHL-TGIEHMDKILFLeNGKIIMQG 178
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-188 |
2.03e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.17 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIdltFPIK-V 83
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGL---LPWRnV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:PRK11248 88 QDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*.
gi 2282925441 164 -EKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:PRK11248 164 rEQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-232 |
2.53e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKkAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---------KSLDVIRKKIAYVEQRSAI 75
Cdd:PRK13646 18 YEHQ-AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLtFPIKVDEVVLLGTfPNlglFRRPKKAQKEKVVECLKQVKME-DFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:PRK13646 97 QL-FEDTVEREIIFGP-KN---FKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELR-NQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNIQAAYGDTMGEIV 232
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEgSIVSQTSPKELFKDKKKLADWHIGLPEIV 251
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-215 |
5.34e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG-------KSLDVIRKKIAYVEQRSAIDLtFP 80
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkVKLSDIRKKVGLVFQYPEYQL-FE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGTfPNLGLfrrPKKAQKEKVVECLKQVKM--EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:PRK13637 99 ETIEKDIAFGP-INLGL---SEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 159 IDMVSEKVIVDLLKELRNQGK-TIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKgKCELQGTPREVF 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-188 |
8.26e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.55 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----------IRKKIAYVEQR- 72
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFsqkpsekairlLRQKVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 ------SAID--LTFPIKVdevvllgtfpnLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALA 144
Cdd:COG4161 92 nlwphlTVMEnlIEAPCKV-----------LGL---SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEV 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-187 |
9.99e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksldviRKKIAYVEQRSAIDLTFPI 81
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLRIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KvdEVVLLGTFPNLGLFRRPKKAQK---------EKVVEClkQVKMED------------------FS----NRQIGNLS 130
Cdd:COG0488 79 L--DTVLDGDAELRALEAELEELEAklaepdedlERLAEL--QEEFEAlggweaearaeeilsglgFPeedlDRPVSELS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 131 GGQLQRVFIARALAQEADIIFLDEPFVGIDMVSekvIVDLLKELRNQGKTIVIVHHD 187
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVSHD 208
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-225 |
1.01e-26 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 103.75 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIK--------TESGEVTVSGKSLDVI--------RK 64
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIdaprlarlRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 65 KIAYVEQRSaidltFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALA 144
Cdd:PRK13547 87 VLPQAAQPA-----FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 145 Q---------EADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVES 213
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVAHGAPAD 241
|
250
....*....|..
gi 2282925441 214 TFVTKNIQAAYG 225
Cdd:PRK13547 242 VLTPAHIARCYG 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-213 |
1.15e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.69 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEV--------TVSGKSLDVIRKKIAYVEQRSAI--DLTFpi 81
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipAMSRSRLYTVRKRMSMLFQSGALftDMNV-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 kVDEVvllgTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:PRK11831 102 -FDNV----AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 162 VSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDN-LIIMNKQLVASGSVES 213
Cdd:PRK11831 177 ITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHaYIVADKKIVAHGSAQA 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-215 |
1.25e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG-----KSLDVIRKKIAYVEQRSAiDLTFPIK 82
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVFQNPD-DQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMV 162
Cdd:PRK13652 96 VEQDIAFGPI-NLGL---DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 163 SEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13652 172 GVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIF 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
15-201 |
2.00e-26 |
|
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: 101.86 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 15 SVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS---LDVIRKKIAYVEQRSAIdltFP-IKVDEVVLLG 90
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtgLAPYQRPVSMLFQENNL---FAhLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLfrrpKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDL 170
Cdd:TIGR01277 95 LHPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|..
gi 2282925441 171 LKELRNQGK-TIVIVHHDLHKTREYFDNLIIM 201
Cdd:TIGR01277 171 VKQLCSERQrTLLMVTHHLSDARAIASQIAVV 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-216 |
2.11e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKA---MIGLIK--TESGEVTVSGKSL-----DV--IRKKIAY 68
Cdd:PRK14239 11 LSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPevTITGSIVYNGHNIysprtDTvdLRKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 69 VEQRSAidlTFPIKVDEVVLLGTFPNlGLfrRPKKAQKEKVVECLKQVKMED-----FSNRQIGnLSGGQLQRVFIARAL 143
Cdd:PRK14239 91 VFQQPN---PFPMSIYENVVYGLRLK-GI--KDKQVLDEAVEKSLKGASIWDevkdrLHDSALG-LSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLHKTREYFDNL-IIMNKQLVASGSVESTFV 216
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTgFFLDGDLIEYNDTKQMFM 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-203 |
2.37e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD----VIRKKIAYVEQRSAID 76
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPararLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVVLlgtfpnlGLFRRPKKAQKEKVVECLKQ-VKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK13536 127 LEFTVRENLLVF-------GRYFGMSTREIEAVIPSLLEfARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-205 |
2.95e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.82 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQ----HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL---------DVIRKKIAYVEQ 71
Cdd:PRK11629 15 YQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaakaELRNQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 RSAI--DLTFPIKVDEVVLLGTfpnlglfRRPKKAQkEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:PRK11629 95 FHHLlpDFTALENVAMPLLIGK-------KKPAEIN-SRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREyfdnliiMNKQL 205
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKR-------MSRQL 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-186 |
3.54e-26 |
|
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: 101.53 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKK-AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsaidlt 78
Cdd:cd03254 12 YDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdiSRKSLRSMIGVVLQ------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 fpikvDEVVLLGT-FPNLGLFRrpKKAQKEKVVECLKQVKMEDFSNRQI-----------GNLSGGQLQRVFIARALAQE 146
Cdd:cd03254 85 -----DTFLFSGTiMENIRLGR--PNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 147 ADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHH 186
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHR 197
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-187 |
3.56e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE---SGEVTVSGKSLDVI---RKKIAYVEQRsai 75
Cdd:COG4136 8 TITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALpaeQRRIGILFQD--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFP-IKVDEVVLLGTFPNLGlfrrpKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG4136 85 DLLFPhLSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 2282925441 155 PFVGIDM-----VSEKVivdlLKELRNQGKTIVIVHHD 187
Cdd:COG4136 160 PFSKLDAalraqFREFV----FEQIRQRGIPALLVTHD 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-203 |
4.87e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.86 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEV----------TVSG-------------------KSL 59
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKekekvleklviqktrfkkiKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 60 DVIRKKIAYVEQRSAIDLtFPIKVDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVF 138
Cdd:PRK13651 101 KEIRRRVGVVFQFAEYQL-FEQTIEKDIIFGPV-SMGV---SKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 139 IARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-188 |
5.18e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.33 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS--LDVIRKKIAYVEQRSAI--DLTfpikVDEvv 87
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVAEACHYLGHRNAMkpALT----VAE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 llgtfpNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVI 167
Cdd:PRK13539 93 ------NLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|..
gi 2282925441 168 VDLLKELRNQGKTIVIV-HHDL 188
Cdd:PRK13539 167 AELIRAHLAQGGIVIAAtHIPL 188
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-201 |
5.21e-26 |
|
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: 99.04 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDvirkkiayveqrsaidltfpikvdevvl 88
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 89 lgtfpnlglFRRPKKAQKEKvVECLKQvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVGIDmVSEKVIV 168
Cdd:cd03216 66 ---------FASPRDARRAG-IAMVYQ-------------LSVGERQMVEIARALARNARLLILDEPTAALT-PAEVERL 121
|
170 180 190
....*....|....*....|....*....|....
gi 2282925441 169 -DLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:cd03216 122 fKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-206 |
6.20e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 101.69 E-value: 6.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI--------RKKIAYVEQRS-- 73
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafRRDIQMVFQDSis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AIDLTFPIK--VDEvvllgtfPNLGLFRRPKKAQKEKVVECLKQVKMED-FSNRQIGNLSGGQLQRVFIARALAQEADII 150
Cdd:PRK10419 101 AVNPRKTVReiIRE-------PLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKELRNQGKT-IVIVHHDLHKTREYFDNLIIMNK-QLV 206
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNgQIV 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-197 |
7.31e-26 |
|
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: 100.17 E-value: 7.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-DVIRKKIAYVeqRSAIDLTFPikvDEVV 87
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIPYL--RRKIGVVFQ---DFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 L--LGTFPNLGLFRR----PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:cd03292 90 LpdRNVYENVAFALEvtgvPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2282925441 162 VSEKVIVDLLKELRNQGKTIVIVHHDlhktREYFDN 197
Cdd:cd03292 170 DTTWEIMNLLKKINKAGTTVVVATHA----KELVDT 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-210 |
1.04e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.81 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD----VIRKKIAYVEQRSAIDLTFP 80
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPsrarHARQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKvdevvllgtfPNLGLFRR----PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:PRK13537 97 VR----------ENLLVFGRyfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNL-IIMNKQLVASGS 210
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLcVIEEGRKIAEGA 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-210 |
1.21e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.52 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLkamiGLIKTE----SGEVTVSGKSL-----DVIRKKIAYVEQRsaid 76
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTRAwdpqQGEILLNGQPIadyseAALRQAISVVSQR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 ltfpikVDevVLLGTF-PNLgLFRRPKkAQKEKVVECLKQVKMEDFSN-------------RQignLSGGQLQRVFIARA 142
Cdd:PRK11160 423 ------VH--LFSATLrDNL-LLAAPN-ASDEALIEVLQQVGLEKLLEddkglnawlgeggRQ---LSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 143 LAQEADIIFLDEPFVGIDMVSEKVIVDLLKELrNQGKTIVIVHHDLHKTrEYFDNLIIM-NKQLVASGS 210
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGL-EQFDRICVMdNGQIIEQGT 556
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-187 |
1.28e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.44 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 13 NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQRsaIDLtFPIKVDEvv 87
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdrEELGRHIGYLPQD--VEL-FDGTIAE-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 llgtfpNLGLFRrpkKAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:COG4618 425 ------NIARFG---DADPEKVVAAAKLAGVHEMILRlpdgydtRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190
....*....|....*....|....*....|.
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHR 526
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
9-201 |
1.41e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.09 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKiAYVEQRSAIDLTF--PI----- 81
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDD-EWRAVRSDIQMIFqdPLaslnp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 --KVDEVVL--LGTF-PNLglfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK15079 114 rmTIGEIIAepLRTYhPKL-----SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2282925441 156 FVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-215 |
1.98e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.30 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV----IR-KKIAYVEQRSAIDLTFP 80
Cdd:COG4167 24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYgdykYRcKHIRMIFQDPNTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKV----DEVVLLGTfpNLglfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:COG4167 104 LNIgqilEEPLRLNT--DL-----TAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 156 FVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG4167 177 LAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVLVMHQgEVVEYGKTAEVF 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-215 |
2.00e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---RKKIAYVEQRSAIdl 77
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMMFQSYAL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 tFP-IKVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:PRK11607 103 -FPhMTVEQNIAFG----LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 157 VGID------MVSEkvIVDLLKELrnqGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK11607 178 GALDkklrdrMQLE--VVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIY 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-215 |
2.09e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.47 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-------VIRKKIAYVEQRSAIDL 77
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 tFPIKVDEVVLLgTFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK13638 91 -FYTDIDSDIAF-SLRNLGV---PEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEVF 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-215 |
2.37e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.42 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIE---NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV--------SGKSLDVIRKKIAYVEQ-- 71
Cdd:PRK11153 12 PQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalSEKELRKARRQIGMIFQhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 -----RSAID-LTFPIKVDevvllgtfpnlglfRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQ 145
Cdd:PRK11153 92 nllssRTVFDnVALPLELA--------------GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 146 EADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAgRLVEQGTVSEVF 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-201 |
2.64e-25 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 98.86 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG--------KSLDVIRKKIAYVEQ-------RSA 74
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGedvnrlrgRQLPLLRRRIGVVFQdfrllpdRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 ID-LTFPIKVDevvllgtfpnlglfRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:TIGR02673 97 YEnVALPLEVR--------------GKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:TIGR02673 163 EPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-206 |
2.89e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEV-----TVSGKSLDVIRKKIAYVEQRSaiDLTFpikVD 84
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLRKHIGIVFQNP--DNQF---VG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSE 164
Cdd:PRK13648 99 SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2282925441 165 KVIVDLLKELR-NQGKTIVIVHHDLHKTREYfDNLIIMNKQLV 206
Cdd:PRK13648 179 QNLLDLVRKVKsEHNITIISITHDLSEAMEA-DHVIVMNKGTV 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
13-215 |
2.96e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 101.33 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 13 NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV---------SGKSLDVIRKKIAYVEQRSAIdltfpikv 83
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsaRGIFLPPHRRRIGYVFQEARL-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 devvllgtFP------NL--GLFRRPKKAQK---EKVVECLKqvkMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:COG4148 89 --------FPhlsvrgNLlyGRKRAPRAERRisfDEVVELLG---IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNQGKT-IVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVL 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-214 |
2.96e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQRSaiDLTF- 79
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdIRHKIGMVFQNP--DNQFv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLGtFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK13650 96 GATVEDDVAFG-LENKGI---PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 160 DMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTrEYFDNLIIMNKqlvasGSVEST 214
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKN-----GQVEST 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-203 |
3.31e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.56 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---RKKIAYVEQRSAIdltFP 80
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaeNRHVNTVFQSYAL---FP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 -IKVDEVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK09452 100 hMTVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 160 D------MVSEkvivdlLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK09452 176 DyklrkqMQNE------LKALQRKlGITFVFVTHDQEEALTMSDRIVVMRD 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-189 |
7.09e-25 |
|
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: 97.89 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD---------VIRKKIAYVEQrsaidlTFPikvd 84
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldedararLRARHVGFVFQ------SFQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 evvLLGTFP---NLGL---FRRPKKAQkEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:COG4181 101 ---LLPTLTaleNVMLpleLAGRRDAR-ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|..
gi 2282925441 159 IDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLH 189
Cdd:COG4181 177 LDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-188 |
7.72e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAieNVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKslDVIRKKIAyveQRSAIDL--- 77
Cdd:PRK10771 7 ITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPS---RRPVSMLfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 --TFP-IKVDEVVLLGTFPNLGLfrrpKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:PRK10771 80 nnLFShLTVAQNIGLGLNPGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190
....*....|....*....|....*....|....*
gi 2282925441 155 PFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDL 188
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSL 190
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-213 |
7.87e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 7.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 3 VAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTEsGEVTVSG---KSLDVI--RKKIAYVEQRSaidL 77
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGielRELDPEswRKHLSWVGQNP---Q 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKVDEVVLLGTfPNlglfrrpkkAQKEKVVECLKQVKMEDFSNRQ-------IGN----LSGGQLQRVFIARALAQE 146
Cdd:PRK11174 434 LPHGTLRDNVLLGN-PD---------ASDEQLQQALENAWVSEFLPLLpqgldtpIGDqaagLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 147 ADIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHKTREYfDNLIIMNK-QLVASGSVES 213
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQW-DQIWVMQDgQIVQQGDYAE 569
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-188 |
9.91e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 96.35 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV---EQRSAIDLT 78
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrsprDAIRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKvdEVVLLGTFpnlglfrrpkkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:cd03215 93 LSVA--ENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190
....*....|....*....|....*....|
gi 2282925441 159 IDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSEL 164
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-224 |
1.29e-24 |
|
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: 101.30 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTEsGEVTVSGKSLDVIRKKiAYVEQRSAIDLTF--P---- 80
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRR-ALRPLRRRMQVVFqdPfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ---IKVDEVVLLGtfpnLGLFRRP--KKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:COG4172 376 sprMTVGQIIAEG----LRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 155 PFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFvtKNIQAAY 224
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDgKVVEQGPTEQVF--DAPQHPY 521
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-196 |
2.00e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTEsGEVTVSGK-------------SLDVIRKKIA 67
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRveffnqniyerrvNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 68 YVEQRSAIdltFPIKVDEVVLLGTfPNLGLfrRPKKAQKEKVVECLKQVKMEDFSNRQIG----NLSGGQLQRVFIARAL 143
Cdd:PRK14258 92 MVHPKPNL---FPMSVYDNVAYGV-KIVGW--RPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGK-TIVIVHHDLHKTREYFD 196
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
2.03e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKA---MIGLIKT--ESGEVTVSGKSL---DV----IRKKIAY 68
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyapDVdpveVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 69 VEQRSAidlTFPIKVDEVVLLGTFPNlGLfrrpkKAQKEKVVE-CLKQVKMEDFSN---RQIG-NLSGGQLQRVFIARAL 143
Cdd:PRK14243 96 VFQKPN---PFPKSIYDNIAYGARIN-GY-----KGDMDELVErSLRQAALWDEVKdklKQSGlSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLHKTREYFDNLIIMNKQLVASGS 210
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-221 |
2.47e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG------KSLDVIRKKIAYVEQRSAIDLTfPIKV 83
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVGIVFQNPETQFV-GRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGTfPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:PRK13644 96 EEDLAFGP-ENLCL---PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 164 EKVIVDLLKELRNQGKTIVIVHHDLHKTREYfDNLIIMNK-QLVASGSVESTFVTKNIQ 221
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRgKIVLEGEPENVLSDVSLQ 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-210 |
2.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQ-RSAIDLTFpikvdevv 87
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlRKEIGLVF-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 llgTFPNLGLFRRP---------------KKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:PRK13645 97 ---QFPEYQLFQETiekdiafgpvnlgenKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGS 210
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGS 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-215 |
2.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.51 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---------KSLDVIRKKIAYVEQRSAIDLtF 79
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIKQIRKKVGLVFQFPESQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLGTfPNLGLfrrpKKAQKEKVV-ECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK13649 100 EETVLKDVAFGP-QNFGV----SQEEAEALArEKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIF 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-187 |
2.99e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.78 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-DVIRKK--IAYVEQRSAI------ 75
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPKDrdIAMVFQNYALyphmtv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 --DLTFPIKvdevvllgtfpnlgLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:cd03301 90 ydNIAFGLK--------------LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 2282925441 154 EPFVGID-MVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:cd03301 156 EPLSNLDaKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
9-188 |
3.08e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 98.27 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVT--------VSGKSLDVIRKKIAYVEQ--RSAID-- 76
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditgLSGRELRPLRRRMQMVFQdpYASLNpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 ------LTFPIKVDEVVllgtfpnlglfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:COG4608 112 mtvgdiIAEPLRIHGLA-------------SKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2282925441 150 IFLDEPFVGIDmVS-EKVIVDLLKELRNQ-GKTIVIVHHDL 188
Cdd:COG4608 179 IVCDEPVSALD-VSiQAQVLNLLEDLQDElGLTYLFISHDL 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-215 |
3.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG------KSLDVIRKKIAYVEQRSAIDLTF 79
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQNPDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIkVDEVVLLGTfPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK13633 101 TI-VEEDVAFGP-ENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 160 DMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYfDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13633 176 DPSGRREVVNTIKELnKKYGITIILITHYMEEAVEA-DRIIVMDSgKVVMEGTPKEIF 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-189 |
3.35e-24 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 96.53 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQ-HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsai 75
Cdd:cd03253 7 TFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevTLDSLRRAIGVVPQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 dltfpikvDEVVLLGTFPNLGLFRRPKkAQKEKVVECLKQVKMEDFSNR-------QIGN----LSGGQLQRVFIARALA 144
Cdd:cd03253 83 --------DTVLFNDTIGYNIRYGRPD-ATDEEVIEAAKAAQIHDKIMRfpdgydtIVGErglkLSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRNqGKTIVIVHHDLH 189
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS 197
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-212 |
5.07e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirkkiayveqrsaidLTFPIKV- 83
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-------------------VSALLELg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 ----------DEVVLLGTFpnLGLFRRPKKAQKEKVV---EclkqvkMEDFSNRQIGNLSGGQLQRVFIARALAQEADII 150
Cdd:COG1134 97 agfhpeltgrENIYLNGRL--LGLSRKEIDEKFDEIVefaE------LGDFIDQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 151 FLDEPF-VGiDMV-SEKVIvDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:COG1134 169 LVDEVLaVG-DAAfQKKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKgRLVMDGDPE 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-210 |
7.24e-24 |
|
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: 99.41 E-value: 7.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsaidltfpikv 83
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladyTLASLRRQVALVSQ------------ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 dEVVLL-GTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEADIIF 151
Cdd:TIGR02203 414 -DVVLFnDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKlplgldtPIGengvLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLhKTREYFDNLIIMNK-QLVASGS 210
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLM-QGRTTLVIAHRL-STIEKADRIVVMDDgRIVERGT 550
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-203 |
9.12e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.47 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----------IRKKIAYVEQRS 73
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsktpsdkaireLRRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 74 AI--DLTF-------PIKVdevvllgtfpnLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALA 144
Cdd:PRK11124 92 NLwpHLTVqqnlieaPCRV-----------LGL---SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-210 |
1.12e-23 |
|
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: 94.99 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsaidltfpik 82
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdyTLASLRRQIGLVSQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 vdEVVLL-GTFPNLGLFRRPKkAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALAQEADII 150
Cdd:cd03251 84 --DVFLFnDTVAENIAYGRPG-ATREEVEEAARAANAHEFIMElpegydtVIGergvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLhKTREYFDNLIIM-NKQLVASGS 210
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRL-STIENADRIVVLeDGKIVERGT 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-207 |
1.16e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.16 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DV--IRKKIAYVEQR----- 72
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkvDErlIRQEAGMVFQQfylfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 --SAID-LTF-PIKVdevvllgtfpnlglfRRPKKAQKEKVV-ECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEA 147
Cdd:PRK09493 91 hlTALEnVMFgPLRV---------------RGASKEEAEKQArELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLVA 207
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-188 |
1.71e-23 |
|
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: 98.32 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 19 EPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR-----------KKIAYVEQRSAIDltfPIKVDEV- 86
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKrfrgtelqdyfKKLANGEIKVAHK---PQYVDLIp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 87 -VLLGTFPNLgLfrrpKKA-QKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDmVSE 164
Cdd:COG1245 174 kVFKGTVREL-L----EKVdERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-IYQ 247
|
170 180
....*....|....*....|....*
gi 2282925441 165 KV-IVDLLKELRNQGKTIVIVHHDL 188
Cdd:COG1245 248 RLnVARLIRELAEEGKYVLVVEHDL 272
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
26-203 |
1.81e-23 |
|
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: 96.41 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 26 IIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---RKKIAYVEQRSAIdltFP-IKVDEVVLLGtfpnLGLFRRP 101
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphLRHINMVFQSYAL---FPhMTVEENVAFG----LKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 102 KKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQ-GKT 180
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGIT 153
|
170 180
....*....|....*....|...
gi 2282925441 181 IVIVHHDLHKTREYFDNLIIMNK 203
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRK 176
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-220 |
1.93e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---------------------KSLDVIRKKIA 67
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpyskkiKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 68 YVEQRSAIDLtFPIKVDEVVLLGTFpNLGLfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQE 146
Cdd:PRK13631 120 MVFQFPEYQL-FKDTIEKDIMFGPV-ALGV---KKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 147 ADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKNI 220
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKgKILKTGTPYEIFTDQHI 269
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-186 |
2.28e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYVEQRSAI--DLTfp 80
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALAAGVAIIYQELHLvpEMT-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikVDEVVLLGTFPN-LGLFRRpkKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK11288 96 --VAENLYLGQLPHkGGIVNR--RLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180
....*....|....*....|....*..
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHH 186
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-202 |
3.15e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD------VIRKKIAYVEQRsaIDLTFPIKV 83
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghqIARMGVVRTFQH--VRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGTFPNL------GLFRRP--KKAQKEKV---VECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:PRK11300 98 IENLLVAQHQQLktglfsGLLKTPafRRAESEALdraATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMN 202
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-188 |
3.72e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 97.19 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 18 IEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRK----------------------KIAYVEQrsaI 75
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRfrgtelqnyfkklyngeikvvhKPQYVDL---I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFPIKVDEVVllgtfpnlglfrrpKKAQKEKVV-ECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:PRK13409 173 PKVFKGKVRELL--------------KKVDERGKLdEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*
gi 2282925441 155 PFVGIDmVSEKVIV-DLLKELrNQGKTIVIVHHDL 188
Cdd:PRK13409 239 PTSYLD-IRQRLNVaRLIREL-AEGKYVLVVEHDL 271
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-187 |
4.06e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVsGKSLdvirkKIAYVEQ-RSAIDLTFP 80
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-----KIGYFDQhQEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IkVDEVV-------------LLGTFpnlgLFrRPKKAQKekvveclkqvkmedfsnrQIGNLSGGQLQRVFIARALAQEA 147
Cdd:COG0488 396 V-LDELRdgapggteqevrgYLGRF----LF-SGDDAFK------------------PVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKELrnQGkTIVIVHHD 187
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD 488
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-217 |
4.98e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.96 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL----DVIRkkIAYVEQRSAIDLTFPIKv 83
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkDIFQ--IDAIKLRKEVGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 devvllGTFPNLGLFR-----------RPKKAQKEKVVECLKQV----KMEDFSNRQIGNLSGGQLQRVFIARALAQEAD 148
Cdd:PRK14246 100 ------NPFPHLSIYDniayplkshgiKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 149 IIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVESTFVT 217
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLyNGELVEWGSSNEIFTS 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-203 |
6.08e-23 |
|
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: 91.92 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 3 VAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAM-----IGLIKtesGEVTVSGKSLDV-IRKKIAYVEQrsaID 76
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKnFQRSTGYVEQ---QD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPikvdevvllgtfpnlglfrrpkkaqKEKVVECLKqvkmedFSNRQIGnLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:cd03232 89 VHSP-------------------------NLTVREALR------FSALLRG-LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVI-VHHDLHKTREYFDNLIIMNK 203
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKR 184
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-186 |
7.95e-23 |
|
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: 96.26 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-----DVIRKKIAYVEQrsAIDLtFP 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLkqwdrETFGKHIGYLPQ--DVEL-FP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEvvllgtfpNLGLFRRpkKAQKEKVVECLKQ-------VKMEDFSNRQIG----NLSGGQLQRVFIARALAQEADI 149
Cdd:TIGR01842 406 GTVAE--------NIARFGE--NADPEKIIEAAKLagvheliLRLPDGYDTVIGpggaTLSGGQRQRIALARALYGDPKL 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHH 186
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-210 |
9.46e-23 |
|
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: 96.35 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI-----RKKIAYVEQRSAIdltFPIKV 83
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrhtlRQFINYLPQEPYI---FSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGTFPNLG---LFRRPKKAQKEKVVECLKQVKMEDFSNRQiGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:TIGR01193 565 LENLLLGAKENVSqdeIWAACEIAEIKDDIENMPLGYQTELSEEG-SSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 161 MVSEKVIVDLLKELrnQGKTIVIVHHDLhKTREYFDNLIIMNK-QLVASGS 210
Cdd:TIGR01193 644 TITEKKIVNNLLNL--QDKTIIFVAHRL-SVAKQSDKIIVLDHgKIIEQGS 691
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-210 |
9.69e-23 |
|
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: 92.60 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---KSLDV--IRKKIAYVEQRSAIdltFPIKV 83
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLrwLRSQIGLVSQEPVL---FDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGTFPnlglfrrpkkAQKEKVVECLKQVKMEDFS-------NRQIGN----LSGGQLQRVFIARALAQEADIIFL 152
Cdd:cd03249 94 AENIRYGKPD----------ATDEEVEEAAKKANIHDFImslpdgyDTLVGErgsqLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHKTReYFDNLIIMNK-QLVASGS 210
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIR-NADLIAVLQNgQVVEQGT 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-189 |
9.94e-23 |
|
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: 92.01 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---------RKKIAYVEQRSAIdltFPI 81
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPsfeatrsrnRYSVAYAAQKPWL---LNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTfpnlglfrrPKKAQKEKVV--ECLKQ--VKMEDFSNR-QIG----NLSGGQLQRVFIARALAQEADIIFL 152
Cdd:cd03290 94 TVEENITFGS---------PFNKQRYKAVtdACSLQpdIDLLPFGDQtEIGergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2282925441 153 DEPFVGIDM-VSEKVIVD-LLKELRNQGKTIVIVHHDLH 189
Cdd:cd03290 165 DDPFSALDIhLSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-203 |
1.24e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKslDVIR-----KKIAYVEQRSAIdltFP-IKVD 84
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHrsiqqRDICMVFQSYAL---FPhMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGtfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSE 164
Cdd:PRK11432 97 ENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 165 KVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:PRK11432 173 RSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNK 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-187 |
1.35e-22 |
|
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: 92.47 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKIT-----GIIGPNGAGKSTLLKAMIGLIKTESGEVtvsgkslDVIRKKIAYVEQRSAIDltFPIK 82
Cdd:cd03237 7 KKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-------EIELDTVSYKPQYIKAD--YEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVvLLGTFPNLGlfrrpkkAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID-- 160
Cdd:cd03237 78 VRDL-LSSITKDFY-------THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDve 149
|
170 180 190
....*....|....*....|....*....|
gi 2282925441 161 ---MVSeKVIVDLLKelrNQGKTIVIVHHD 187
Cdd:cd03237 150 qrlMAS-KVIRRFAE---NNEKTAFVVEHD 175
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
14-220 |
1.54e-22 |
|
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: 94.02 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTFpikvDEVVLlgtFP 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVF----QEARL---FP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 94 NLGL---------FRRPK--KAQKEKVVECLKqvkMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMV 162
Cdd:TIGR02142 89 HLSVrgnlrygmkRARPSerRISFERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 163 SEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVESTFVTKNI 220
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-209 |
1.60e-22 |
|
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: 91.44 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIdltfpikvD 84
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPELTGR--------E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGTFpnLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF-VGIDMVS 163
Cdd:cd03220 104 NIYLNGRL--LGL---SRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2282925441 164 EKVIvDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:cd03220 179 EKCQ-RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKgKIRFDG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
2.86e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.51 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE-----SGEVTVSGKSLdvirKKIAYVEQRSAI 75
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDI----FKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFPI-------KVDEVVLLGtfPNLGLFRRPKKAQKEKVVECLKQVKM-EDFSNR---QIGNLSGGQLQRVFIARALA 144
Cdd:PRK14247 85 QMVFQIpnpipnlSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKgQIVEWGPTREVF 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-188 |
3.04e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 94.88 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKI-----TGIIGPNGAGKSTLLKAMIGLIKTESGEVtvsgkSLDVirkKIAYVEQRSAIDltFPIK 82
Cdd:PRK13409 347 TKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----DPEL---KISYKPQYIKPD--YDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVvLLGTFPNLG--LFRrpkkaqkekvVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK13409 417 VEDL-LRSITDDLGssYYK----------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180 190
....*....|....*....|....*....|
gi 2282925441 161 mVSEKVIV-DLLKEL-RNQGKTIVIVHHDL 188
Cdd:PRK13409 486 -VEQRLAVaKAIRRIaEEREATALVVDHDI 514
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
8-212 |
3.20e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE---SGEVTVSGKSLDV--IRKKIAYVEQRsaiDLTFP-I 81
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAkeMRAISAYVQQD---DLFIPtL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTfpNLGLFRR-PKKAQKEKVVECLKQVKMEDFSNRQIG------NLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:TIGR00955 115 TVREHLMFQA--HLRMPRRvTKKEKRERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGKTIVI-VHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEgRVAYLGSPD 252
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-215 |
3.50e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGE---VTVSGKSLDV-----IRKKIAYVEQRSAIDLTF 79
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAktvwdIREKVGIVFQNPDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLlgtfpnlGLFRR--PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK13640 100 ATVGDDVAF-------GLENRavPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTrEYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDgKLLAQGSPVEIF 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-187 |
4.42e-22 |
|
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: 88.27 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSldvirkKIAYVEQrsaidltfpi 81
Cdd:cd03221 7 SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------KIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 kvdevvllgtfpnlglfrrpkkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|....*.
gi 2282925441 162 VSEKVIVDLLKELRnqgKTIVIVHHD 187
Cdd:cd03221 104 ESIEALEEALKEYP---GTVILVSHD 126
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-186 |
4.62e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.06 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE-----SGEVTVSGKSL---DV----IRKKIAY 68
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspDVdpieVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 69 VEQrsaIDLTFP-IKVDEVVLLGTfpNLGLFRRPKKAQKEKVVECLKQV----KMEDFSNRQIGNLSGGQLQRVFIARAL 143
Cdd:PRK14267 90 VFQ---YPNPFPhLTIYDNVAIGV--KLNGLVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHH 186
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-206 |
4.74e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.18 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRK-----KIAYVEQ----RSAI 75
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlKVADKNQlrllRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DLTFP-------IKVDEVVLLGTFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQI-GNLSGGQLQRVFIARALAQEA 147
Cdd:PRK10619 95 TMVFQhfnlwshMTVLENVMEAPIQVLGL---SKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 148 DIIFLDEPFVGID--MVSEkvIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLV 206
Cdd:PRK10619 172 EVLLFDEPTSALDpeLVGE--VLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-187 |
5.51e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI---------RKKIAYVEQRSAI--DL 77
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaqlrREHFGFIFQRYHLlsHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKVdEV--VLLGTfpnlglfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK10535 102 TAAQNV-EVpaVYAGL---------ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|..
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-155 |
6.55e-22 |
|
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: 93.85 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVsGKSLdvirkKIAYVEQ-RSAIDltf 79
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----KLAYVDQsRDALD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIK-VDEVVLLGT-FPNLGLFRRPKKA-----------QKEKVveclkqvkmedfsnrqiGNLSGGQLQRVFIARALAQE 146
Cdd:TIGR03719 399 PNKtVWEEISGGLdIIKLGKREIPSRAyvgrfnfkgsdQQKKV-----------------GQLSGGERNRVHLAKTLKSG 461
|
....*....
gi 2282925441 147 ADIIFLDEP 155
Cdd:TIGR03719 462 GNVLLLDEP 470
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-155 |
7.02e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 93.64 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVsGKSLdvirkKIAYVEQ-RSAIDltfPIK 82
Cdd:PRK11819 333 SFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----KLAYVDQsRDALD---PNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 -VDEVVLLGT-FPNLGLFRRPKKA-----------QKEKVveclkqvkmedfsnrqiGNLSGGQLQRVFIARALAQEADI 149
Cdd:PRK11819 404 tVWEEISGGLdIIKVGNREIPSRAyvgrfnfkggdQQKKV-----------------GVLSGGERNRLHLAKTLKQGGNV 466
|
....*.
gi 2282925441 150 IFLDEP 155
Cdd:PRK11819 467 LLLDEP 472
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-188 |
7.32e-22 |
|
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: 93.70 E-value: 7.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKI-----TGIIGPNGAGKSTLLKAMIGLIKTESGEVtvsgkSLDVirkKIAYVEQRSAIDltFPIK 82
Cdd:COG1245 348 TKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDL---KISYKPQYISPD--YDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVllgtfpnlglfrrpKKAQKEKV------VECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:COG1245 418 VEEFL--------------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190
....*....|....*....|....*....|....
gi 2282925441 157 VGIDmVSEKVIV-DLLKEL-RNQGKTIVIVHHDL 188
Cdd:COG1245 484 AHLD-VEQRLAVaKAIRRFaENRGKTAMVVDHDI 516
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-208 |
7.62e-22 |
|
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: 89.39 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLdvirKKIAYVEQRSAIDLtfpIKVDEVVL 88
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLEDLRSSLTI---IPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 89 LGTF-PNLGLFrrpKKAQKEKVVECLKQVKMEDfsnrqigNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVI 167
Cdd:cd03369 95 SGTIrSNLDPF---DEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2282925441 168 VDLLKELRNqGKTIVIVHHDLHKTREYfDNLIIMNKQLVAS 208
Cdd:cd03369 165 QKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-210 |
1.23e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.02 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL---------DVIRKKIAYVEQrsaidlTFP 80
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisdaelrEVRRKKIAMVFQ------SFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 161 -MVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGS 210
Cdd:PRK10070 197 pLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGT 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-219 |
1.36e-21 |
|
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: 89.47 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI-----RKKIAYVEQRSaidLTFPIKVD 84
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlRRQVGVVLQEN---VLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGtfpnlglfrRPkKAQKEKVVECLKQVKMEDF------------SNRQIGnLSGGQLQRVFIARALAQEADIIFL 152
Cdd:cd03252 94 DNIALA---------DP-GMSMERVIEAAKLAGAHDFiselpegydtivGEQGAG-LSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELrNQGKTIVIVHHDLHKTREYfDNLIIMNKQLVASGSVESTFVTKN 219
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-212 |
1.42e-21 |
|
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: 88.35 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE--SGEVTVSGKSLdvirkkiayveqrsaIDLTfpikVDE 85
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDI---------------TDLP----PEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTFpnLGlFRRPKKAQKEKVVECLKQVKMedfsnrqigNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:cd03217 74 RARLGIF--LA-FQYPPEIPGVKNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 166 VIVDLLKELRNQGKTIVIVHHdlhkTREYFDNL------IIMNKQLVASGSVE 212
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITH----YQRLLDYIkpdrvhVLYDGRIVKSGDKE 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-188 |
3.04e-21 |
|
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: 87.55 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR----KKIAYVEQRSAIDltfpikvdevV 87
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiaRGLLYLGHAPGIK----------T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 LLGTFPNLGLFRRpkKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVI 167
Cdd:cd03231 87 TLSVLENLRFWHA--DHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|..
gi 2282925441 168 VDLLKELRNQGKTIVI-VHHDL 188
Cdd:cd03231 165 AEAMAGHCARGGMVVLtTHQDL 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-188 |
3.77e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.41 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR----KKIAYVEQRSAI--DLTfpikVDE 85
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephENILYLGHLPGLkpELS----ALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vvllgtfpNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:TIGR01189 93 --------NLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....
gi 2282925441 166 VIVDLLKE-LRNQGKTIVIVHHDL 188
Cdd:TIGR01189 165 LLAGLLRAhLARGGIVLLTTHQDL 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-188 |
1.03e-20 |
|
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: 87.42 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 19 EPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIR----------------------KKIAYVEQrsaID 76
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDefrgselqnyftkllegdvkviVKPQYVDL---IP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVvllgtfpnlgLFRRPKKAQKEKVVeclKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:cd03236 101 KAVKGKVGEL----------LKKKDERGKLDELV---DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|..
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
11-201 |
1.91e-20 |
|
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: 86.37 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-------VIRKKIAYVEQRSAIDlTFPIKV 83
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdrmVVFQNYSLLPWLTVRE-NIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVvllgtfpnlgLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:TIGR01184 80 DRV----------LPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 2282925441 164 EKVIVD-LLKELRNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:TIGR01184 150 RGNLQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-215 |
1.97e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-------------IRKKIAYVEQRSAIdltFP 80
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarslsqqkglirqLRQHVGFVFQNFNL---FP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IK-VDEVVLLGTfpnLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK11264 99 HRtVLENIIEGP---VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 160 D--MVSEkvIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK11264 176 DpeLVGE--VLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQgRIVEQGPAKALF 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-210 |
2.12e-20 |
|
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: 86.01 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsaidltfpikvD 84
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiGLHDLRSRISIIPQ------------D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGTF-PNLGLFrrpKKAQKEKVVECLKQVKMEDFSNRQIG-----------NLSGGQLQRVFIARALAQEADIIFL 152
Cdd:cd03244 87 PVLFSGTIrSNLDPF---GEYSDEELWQALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNqGKTIVIVHHDLHkTREYFDNLIIMNK-QLVASGS 210
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLD-TIIDSDRILVLDKgRVVEFDS 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
9-215 |
2.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG---------KSLDVIRKKIAYVEQRSAIDLtF 79
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIKPVRKKVGVVFQFPESQL-F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 PIKVDEVVLLGTfPNLGLfrrpKKAQKEKVV-ECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK13643 99 EETVLKDVAFGP-QNFGI----PKEKAEKIAaEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 158 GIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDVF 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-197 |
2.67e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.83 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIK--TESGEVTVSGKSL------DVIRKKIAYVEQRSAI--DLT 78
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELqasnirDTERAGIAIIHQELALvkELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 fpikVDEVVLLGTFPNLG-------LFRRPKKaqkekvveCLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIF 151
Cdd:PRK13549 99 ----VLENIFLGNEITPGgimdydaMYLRAQK--------LLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDN 197
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDT 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-208 |
3.00e-20 |
|
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: 88.73 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIK--TESGEVTVSGKSL------DVIRKKIAYVEQRsaIDLTFP 80
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkasnirDTERAGIVIIHQE--LTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSN-RQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNL-IIMNKQLVAS 208
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTIcVIRDGQHVAT 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-224 |
3.52e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTEsGEVTVSGKSLDV--------IRKKIAYVEQRSAIDLT 78
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNlnrrqllpVRHRIQVVFQDPNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKVDEVVLLGT---FPNLGlfrrpKKAQKEKVVECLKQVKME-DFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:PRK15134 377 PRLNVLQIIEEGLrvhQPTLS-----AAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 155 PFVGIDMVSEKVIVDLLKELRNQGKTIVI-VHHDLHKTREYFDNLIIMNK-QLVASGSVESTFVTKniQAAY 224
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQgEVVEQGDCERVFAAP--QQEY 521
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-187 |
3.59e-20 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 88.53 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKamigLIKTE-----SGEVTV------SGKSLDVIRKKIAYVE 70
Cdd:PRK10938 267 VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITGDhpqgySNDLTLfgrrrgSGETIWDIKKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 71 QRSAIDLTFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMED-FSNRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:PRK10938 343 SSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRNQGKT--IVIVHHD 187
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHHA 462
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-211 |
3.86e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAY-------VEQRSAIDltfPIK 82
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgigiiYQELSVID---ELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLLGTFPNLGLFRRPK---KAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK09700 97 VLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSV 211
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMkDGSSVCSGMV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-215 |
5.07e-20 |
|
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: 88.20 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKS-TLLKAMiGL----IKTESGEVTVSGKSL-----DVIRK----KIAYVEQ 71
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLlpdpAAHPSGSILFDGQDLlglseRELRRirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 R--SAIDLTFPI--KVDEVVLLgtfpNLGLfrrPKKAQKEKVVECLKQVKMEDFSNR------QignLSGGQLQRVFIAR 141
Cdd:COG4172 100 EpmTSLNPLHTIgkQIAEVLRL----HRGL---SGAAARARALELLERVGIPDPERRldayphQ---LSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 142 ALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQgEIVEQGPTAELF 245
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
14-193 |
2.35e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.70 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSG------------------KSLDVIRKKIAYVEQ---- 71
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvpadrRQLQRIRTRLGMVFQsfnl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 ---RSAID--LTFPIKVdevvllgtfpnLGlfrRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQE 146
Cdd:COG4598 107 wshMTVLEnvIEAPVHV-----------LG---RPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAME 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 147 ADIIFLDEPFVGID--MVSE--KVIVDLLKElrnqGKTIVIVHHDLHKTRE 193
Cdd:COG4598 173 PEVMLFDEPTSALDpeLVGEvlKVMRDLAEE----GRTMLVVTHEMGFARD 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-224 |
2.57e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD------VIRKKIAYV-EQRSAIDl 77
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtakIMREAVAIVpEGRRVFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 tfPIKVDEVVLLGtfpnlGLFRRPKKAQK--EKVVECLKqvKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK11614 94 --RMTVEENLAMG-----GFFAERDQFQEriKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFD-NLIIMNKQLVASGSVESTFVTKNIQAAY 224
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADrGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-187 |
2.65e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKkiayvEQRSAI---DLTFPIKVDEVV-LL 89
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE-----EARAKLrakHVGFVFQSFMLIpTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 GTFPNL---GLFRRPKKAQ-KEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:PRK10584 104 NALENVelpALLRGESSRQsRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|...
gi 2282925441 166 VIVDLLKEL-RNQGKTIVIVHHD 187
Cdd:PRK10584 184 KIADLLFSLnREHGTTLILVTHD 206
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-186 |
5.26e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE--SGEVTVSGKS-LDvirkkiAYVEQRSA--IDLTF--P 80
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDiLE------LSPDERARagIFLAFqyP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVvllgtfPNLGLFRRPKKAQKE----------KVVECLKQVKM-EDFSNRQI-GNLSGGQLQRVFIARALAQEAD 148
Cdd:COG0396 87 VEIPGV------SVSNFLRTALNARRGeelsareflkLLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2282925441 149 IIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHH 186
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-186 |
6.25e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.53 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD----VIRKKIAYVEQRSAIDltfp 80
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlcTYQKQLCFVGHRSGIN---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikvdevvllgtfPNLGL-----FRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK13540 87 ------------PYLTLrenclYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKTIVIVHH 186
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
9-217 |
6.99e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.80 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKtESGEVTVSGKSLD--------------VIRKKIAYVEQ--R 72
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNgidllklsprerrkIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 SAIDLTFPI--KVDEVVLLGTFPnlGLFRRPKKAQKEKVVECLKQVKMEDfsNRQIGN-----LSGGQLQRVFIARALAQ 145
Cdd:COG4170 100 SCLDPSAKIgdQLIEAIPSWTFK--GKWWQRFKWRKKRAIELLHRVGIKD--HKDIMNsypheLTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 146 EADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVESTFVT 217
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLyCGQTVESGPTEQILKS 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-210 |
7.60e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQRSAIDLTFP 80
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFgdysyRSQRIRMIFQDPSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGTFPNLGLfrrPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK15112 104 QRISQILDFPLRLNTDL---EPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 160 DMVSEKVIVDLLKELR-NQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGS 210
Cdd:PRK15112 181 DMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMhQGEVVERGS 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-188 |
7.67e-19 |
|
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: 81.71 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV--SGKSLDV----------IRKK-IAYVEQ----- 71
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLaqaspreilaLRRRtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 -R-SAIDLtfpikVDEVVL-LGTfpnlglfrrPKKAQKEKVVECLKQVkmedfsnrqigNL------------SGGQLQR 136
Cdd:COG4778 106 pRvSALDV-----VAEPLLeRGV---------DREEARARARELLARL-----------NLperlwdlppatfSGGEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 137 VFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDE 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-210 |
8.94e-19 |
|
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: 85.07 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK----SLDVIRKKIAYVEQRSAidLTFPIKV 83
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietNLDAVRQSLGMCPQHNI--LFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLgtFPNLglfrrPKKAQKEKVVEC---LKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:TIGR01257 1021 AEHILF--YAQL-----KGRSWEEAQLEMeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 161 MVSEKVIVDLLKELRNqGKTIVIVHHDLHKTREYFDNL-IIMNKQLVASGS 210
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIaIISQGRLYCSGT 1143
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-224 |
1.22e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGL----IKTESGEVTVSGKSL---DVIRKKIAYVEQ--RSAIDltfPI 81
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVapcALRGRKIATIMQnpRSAFN---PL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTFPNLGlfrrpKKAQKEKVVECLKQVKMEDfSNRQIG----NLSGGQLQRVFIARALAQEADIIFLDEPFV 157
Cdd:PRK10418 96 HTMHTHARETCLALG-----KPADDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 158 GIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVESTF------VTKNIQAAY 224
Cdd:PRK10418 170 DLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMsHGRIVEQGDVETLFnapkhaVTRSLVSAH 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2-203 |
1.32e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.16 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV---SGKSLDVIRKKIAYVEQRsaiDLT 78
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIlanNRKPTKQILKRTGFVTQD---DIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FP-IKVDEVVLLGTFPNL--GLFRRPKKAQKEKVVECLKQVKMEdfsNRQIGN-----LSGGQLQRVFIARALAQEADII 150
Cdd:PLN03211 152 YPhLTVRETLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCE---NTIIGNsfirgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVI-VHHDLHKTREYFDNLIIMNK 203
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSE 282
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-201 |
1.89e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV-EQRSAIDLTFPIKV 83
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqDGLANGIVYIsEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DE---VVLLGTFPNLGlFRRPKKAQKEKVVECLKQVKMEDFSNRQ-IGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK10762 348 KEnmsLTALRYFSRAG-GSLKHADEQQAVSDFIRLFNIKTPSMEQaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-188 |
1.98e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV-EQRSAiDLTFPIK-V 83
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprDAIRAGIMLCpEDRKA-EGIIPVHsV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLLGT---FPNLGLFRRPKKaQKEKVVECLKQVKMEDFSNRQ-IGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK11288 349 ADNINISArrhHLRAGCLINNRW-EAENADRFIRSLNIKTPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180
....*....|....*....|....*....
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQGVAVLFVSSDL 456
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6-207 |
2.00e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.61 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQRSAIdltFP 80
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklQLDSWRSRLAVVSQTPFL---FS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGtfpnlglfrRPKKAQKE-KVVECLKQVKmEDFSN------RQIGN----LSGGQLQRVFIARALAQEADI 149
Cdd:PRK10789 403 DTVANNIALG---------RPDATQQEiEHVARLASVH-DDILRlpqgydTEVGErgvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHKTREYfDNLIIMNKQLVA 207
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTEA-SEILVMQHGHIA 528
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-187 |
3.03e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIdltFP 80
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARL---LP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IK--VDEVvllgtfpNLGLfrrpKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:PRK11247 95 WKkvIDNV-------GLGL----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190
....*....|....*....|....*....|
gi 2282925441 159 IDMVSEKVIVDLLKEL-RNQGKTIVIVHHD 187
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHD 193
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-188 |
3.57e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV-E--QRSAIDLT 78
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprERRRLGVAYIpEdrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKvdEVVLLGTFPNLGLFRRP---KKAQKEKVVEClkqvkMEDFS------NRQIGNLSGGQLQRVFIARALAQEADI 149
Cdd:COG3845 351 MSVA--ENLILGRYRRPPFSRGGfldRKAIRAFAEEL-----IEEFDvrtpgpDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190
....*....|....*....|....*....|....*....
gi 2282925441 150 IFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDL 462
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-232 |
3.85e-18 |
|
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: 83.14 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS----LDVIRKKIAYVEQRSAIDltfpikvde 85
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISDVHQNMGYCPQFDAID--------- 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vVLLGTFPNLGLFRRPKKAQKEKVVEC----LKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:TIGR01257 2025 -DLLTGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 162 VSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKqlvasGSVESTFVTKNIQAAYGDtmGEIV 232
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVK-----GAFQCLGTIQHLKSKFGD--GYIV 2167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-186 |
4.66e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE--SGEV-----------------------TVS 55
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIiyhvalcekcgyverpskvgepcPVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 56 GKSLDV---------------IRKKIAYVEQRsaidlTFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMED 120
Cdd:TIGR03269 86 GGTLEPeevdfwnlsdklrrrIRKRIAIMLQR-----TFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 121 FSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHH 186
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSH 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-203 |
6.07e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 82.46 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKT---ESGEVTVSGKSLD-VIRKKIAYVEQRsaiDLTFP- 80
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDsSFQRSIGYVQQQ---DLHLPt 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVVLLGTFpnlglFRRPKK-AQKEK---VVECLKQVKMEDFSNRQIG----NLSGGQLQRVFIARAL-AQEADIIF 151
Cdd:TIGR00956 851 STVRESLRFSAY-----LRQPKSvSKSEKmeyVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELvAKPKLLLF 925
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRNQGKTIV-IVHHDLHKTREYFDNLIIMNK 203
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLLQK 978
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-185 |
1.47e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQH-KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-----VIRKKIAYVEQrsa 74
Cdd:PRK10790 346 VSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslshsVLRQGVAMVQQ--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 idltfpikvDEVVLLGTF-PNLGLFRrpkKAQKEKVVECLKQVKMEDFSNR-----------QIGNLSGGQLQRVFIARA 142
Cdd:PRK10790 423 ---------DPVVLADTFlANVTLGR---DISEEQVWQALETVQLAELARSlpdglytplgeQGNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2282925441 143 LAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVH 185
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-189 |
1.71e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 81.36 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSgksldvirKKIAYVEQRSAIdltfpikVDEVV 87
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------RSIAYVPQQAWI-------MNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 LlgtfPNLGLFRRPKKAQKEKVVEC------LKQVK--MEDfsnrQIG----NLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PTZ00243 738 R----GNILFFDEEDAARLADAVRVsqleadLAQLGggLET----EIGekgvNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190
....*....|....*....|....*....|....*.
gi 2282925441 156 FVGIDM-VSEKVIVD-LLKELRnqGKTIVIVHHDLH 189
Cdd:PTZ00243 810 LSALDAhVGERVVEEcFLGALA--GKTRVLATHQVH 843
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-209 |
1.85e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD-----VIRKKIAYVEQrsaidltfpikvdE 85
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhYLHRQVALVGQ-------------E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLL-GTFPN---LGLFRRPKKAQKEKVVECLKQ---VKMEDFSNRQIGN----LSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:TIGR00958 564 PVLFsGSVREniaYGLTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 155 PFVGIDMVSEKvivdLLKELRN-QGKTIVIVHHDLHkTREYFDNLIIMNK-QLVASG 209
Cdd:TIGR00958 644 ATSALDAECEQ----LLQESRSrASRTVLLIAHRLS-TVERADQILVLKKgSVVEMG 695
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-203 |
1.87e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.28 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQ---HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQR 72
Cdd:cd03248 17 VTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 SAIdltFPIKVDEVVL--LGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQiGNLSGGQLQRVFIARALAQEADII 150
Cdd:cd03248 97 PVL---FARSLQDNIAygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKElRNQGKTIVIVHHDLhKTREYFDNLIIMNK 203
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRL-STVERADQILVLDG 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-201 |
2.81e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKS------LDVIRKKIAYVEQRSAIDLTFP- 80
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspLDAVKKGMAYITESRRDNGFFPn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ------IKVDEVVLLGTFPN-LGLFRRPKKAQKEKVVECLKQVKMEDFsNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:PRK09700 356 fsiaqnMAISRSLKDGGYKGaMGLFHEVDEQRTAENQRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-203 |
3.13e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.20 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKslDVIRKKiayVEQRSA-IDLTF--Pikvd 84
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLP---EYKRAKyIGRVFqdP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 evvLLGTFPNL----------------GLFRRPKKAQKEKVVECLKQVKM--EDFSNRQIGNLSGGQLQRVFIARALAQE 146
Cdd:COG1101 90 ---MMGTAPSMtieenlalayrrgkrrGLRRGLTKKRRELFRELLATLGLglENRLDTKVGLLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 147 ADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-217 |
3.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV-----IRKKIAYVEQRSAIDLTFPIKVDE 85
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLlgTFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:PRK13642 103 VAF--GMENQGI---PREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 166 VIVDLLKELRNQGK-TIVIVHHDLHKTREYFDNLIIMNKQLVASGSVESTFVT 217
Cdd:PRK13642 178 EIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-197 |
3.88e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.98 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAI-ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSldvirkKIAYVEQRSAIDLTf 79
Cdd:TIGR03719 10 VSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI------KVGYLPQEPQLDPT- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 pIKVDEVVLLGTFPNLGLFRR---------PKKAQKEKVVEclKQVKMEDF--------SNRQ----------------I 126
Cdd:TIGR03719 83 -KTVRENVEEGVAEIKDALDRfneisakyaEPDADFDKLAA--EQAELQEIidaadawdLDSQleiamdalrcppwdadV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 127 GNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSekviVDLLKE-LRNQGKTIVIVHHDlhktREYFDN 197
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERhLQEYPGTVVAVTHD----RYFLDN 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
9-215 |
4.13e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.63 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLI----KTESGEVTVSGKSLDVIRKK---------IAYVEQRSAI 75
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKerrnlvgaeVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 DL----TFPIKVDEVVLLGTFPNlglfrrpKKAQKEKVVECLKQVKMEDFSNR---QIGNLSGGQLQRVFIARALAQEAD 148
Cdd:PRK11022 101 SLnpcyTVGFQIMEAIKVHQGGN-------KKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2282925441 149 IIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAgQVVETGKAHDIF 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-185 |
4.79e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 2 TVAYQHKK--AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQrsa 74
Cdd:PRK11176 348 TFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVALVSQ--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 idltfpikvdEVVLLG-TFPNLGLFRRPKKAQKEKVVECLKQV-------KMEDFSNRQIG----NLSGGQLQRVFIARA 142
Cdd:PRK11176 425 ----------NVHLFNdTIANNIAYARTEQYSREQIEEAARMAyamdfinKMDNGLDTVIGengvLLSGGQRQRIAIARA 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2282925441 143 LAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVH 185
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-230 |
5.25e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 13 NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV---EQRSAIDLTFPIKV 83
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalstaQRLARGLVYLpedRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVVLlgTFPNLGLFRRPKKaqKEKVVECLKQ---VKMEDfSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK15439 361 NVCAL--THNRRGFWIKPAR--ENAVLERYRRalnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNkQLVASGSVESTFV-TKNI-QAAYGDTMGE 230
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMH-QGEISGALTGAAInVDTImRLAFGEHQAQ 506
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-189 |
7.35e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.00 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL----DVIRKKIAYVEQRSAIDltfpikvdevV 87
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrDEYHQDLLYLGHQPGIK----------T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 LLGTFPNLGLFRR-PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKV 166
Cdd:PRK13538 88 ELTALENLRFYQRlHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|....
gi 2282925441 167 IVDLLKE-LRNQGKTIVIVHHDLH 189
Cdd:PRK13538 168 LEALLAQhAEQGGMVILTTHQDLP 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-222 |
7.52e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAyveQRSAIDLtfpikVDEVVLLgtFP 93
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA---HQLGIYL-----VPQEPLL--FP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 94 NLG-----LFRRPKKAQ-KEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVI 167
Cdd:PRK15439 100 NLSvkeniLFGLPKRQAsMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 168 VDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLVA-SGSVESTFVTKNIQA 222
Cdd:PRK15439 180 FSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAlSGKTADLSTDDIIQA 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-203 |
9.17e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 9.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDvIRKKIAYVEQRSAIdltfpikvdevvllgtFP 93
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPEDYRKLFSAV----------------FT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 94 NLGLFRR---PKK--AQKEKVVECLKQVKMED---FSNRQIGN--LSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:PRK10522 405 DFHLFDQllgPEGkpANPALVEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2282925441 164 EKVIV-DLLKELRNQGKTIVIVHHDLHktreYF---DNLIIMNK 203
Cdd:PRK10522 485 RREFYqVLLPLLQEMGKTIFAISHDDH----YFihaDRLLEMRN 524
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-201 |
1.22e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKaMIGLIKT-ESGEVTVSGKslDVIRKKIAYVEQ-RSAIDLTF------- 79
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLAR-LLTMIETpTGGELYYQGQ--DLLKADPEAQKLlRQKIQIVFqnpygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 -PIK-----VDEVVLLGTfpNLGlfrrpKKAQKEKVVECLKQVKME-DFSNRQIGNLSGGQLQRVFIARALAQEADIIFL 152
Cdd:PRK11308 106 nPRKkvgqiLEEPLLINT--SLS-----AAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-209 |
1.38e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.08 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQRSaidLTFPIK 82
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvTRASLRRNIAVVFQDA---GLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLLGtfpnlglfrRPKkAQKEKVVECLKQVKMEDFSNRQIGN-----------LSGGQLQRVFIARALAQEADIIF 151
Cdd:PRK13657 425 IEDNIRVG---------RPD-ATDEEMRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 152 LDEPFVGIDMVSEKVIVDLLKELRnQGKTIVIVHHDLHKTRE-----YFDNLIIMNK----QLVASG 209
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNadrilVFDNGRVVESgsfdELVARG 560
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-214 |
1.57e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK------IAYVEQRsaIDLTFPIK 82
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengISMVHQE--LNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLLGTFPNLGLFRRPKKAQKEkVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPfvgIDMV 162
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVDQDKMYRD-TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP---TSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 163 SEKVIVDLLK---ELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVEST 214
Cdd:PRK10982 166 TEKEVNHLFTiirKLKERGCGIVYISHKMEEIFQLCDEITILrDGQWIATQPLAGL 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
11-186 |
1.62e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.93 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV-SGKsldvirkKIAYVEQRSAIdltfPikvdevvlL 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGA-------RVLFLPQRPYL----P--------L 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 GT------FPNlglfrRPKKAQKEKVVECLKQVKMEDFSNR--------QIgnLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:COG4178 440 GTlreallYPA-----TAEAFSDAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|.
gi 2282925441 156 FVGIDMVSEKVIVDLLKElRNQGKTIVIVHH 186
Cdd:COG4178 513 TSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-213 |
1.72e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 13 NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-DVIRK--------KIAYVEQRSAIdltfpikv 83
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfDAEKGiclppekrRIGYVFQDARL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 devvllgtFP------NL--GLfRRPKKAQKEKVVECLKqvkMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK11144 88 --------FPhykvrgNLryGM-AKSMVAQFDKIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKT-IVIVHHDLHKTREYFDNLIIMNK-QLVASGSVES 213
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQgKVKAFGPLEE 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-220 |
4.04e-16 |
|
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: 76.79 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE-SGEVTVSGKSLDV------IRKKIAYV-EQRSAIDLT 78
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIrnpaqaIRAGIAMVpEDRKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVV-ECLKQVKMEDFS-NRQIGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:TIGR02633 352 PILGVGKNITLSVLKSFCFKMRIDAAAELQIIgSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKqlvasGSVESTFVTKNI 220
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE-----GKLKGDFVNHAL 490
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-216 |
4.31e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGliktesgEVTVSGKSLDVIRKKIAYVEQRSAIdltFPIKVDEVV 87
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------ELSHAETSSVVIRGSVAYVPQVSWI---FNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 LLGTFpnlglfRRPKKAQKEKVVECLkQVKMEDFSNR---QIG----NLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PLN03232 700 LFGSD------FESERYWRAIDVTAL-QHDLDLLPGRdltEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 161 M-VSEKVIVDLLKElRNQGKTIVIVHHDLHkTREYFDNLIIMNKQLVASgsvESTFV 216
Cdd:PLN03232 773 AhVAHQVFDSCMKD-ELKGKTRVLVTNQLH-FLPLMDRIILVSEGMIKE---EGTFA 824
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-189 |
4.49e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIG-LIKTESGEVtvsgksldVIRKKIAYVEQRSAIdltFPIKVDEV 86
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASV--------VIRGTVAYVPQVSWI---FNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 87 VLLGTfpnlglfrrPKKAQK-EKVVEC------LKQVKMEDFSnrQIG----NLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PLN03130 699 ILFGS---------PFDPERyERAIDVtalqhdLDLLPGGDLT--EIGergvNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190
....*....|....*....|....*....|....*.
gi 2282925441 156 FVGIDM-VSEKVIVDLLK-ELRnqGKTIVIVHHDLH 189
Cdd:PLN03130 768 LSALDAhVGRQVFDKCIKdELR--GKTRVLVTNQLH 801
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
14-196 |
4.98e-16 |
|
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: 76.38 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRkKIAYVEQRSAIdltfpikvdevvllgtFP 93
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN-REAYRQLFSAV----------------FS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 94 NLGLFRR----PKKAQKEKVVECLKQVKMED--------FSNRqigNLSGGQLQRVFIARALAQEADIIFLDE------P 155
Cdd:COG4615 414 DFHLFDRllglDGEADPARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALLVALLEDRPILVFDEwaadqdP 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 156 -----FVGidmvsekvivDLLKELRNQGKTIVIVHHDLHktreYFD 196
Cdd:COG4615 491 efrrvFYT----------ELLPELKARGKTVIAISHDDR----YFD 522
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-188 |
1.81e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 7 HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTES-GEVTVSGKSLDV------IRKKIAYV-EQRSAIDLT 78
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIrnpqqaIAQGIAMVpEDRKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVV-ECLKQVKMEDFSNRQ-IGNLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:PRK13549 354 PVMGVGKNITLAALDRFTGGSRIDDAAELKTIlESIQRLKVKTASPELaIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190
....*....|....*....|....*....|..
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQGVAIIVISSEL 465
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-224 |
1.90e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDV--------IRKKIAYVEQRSAIDLTfPI 81
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgklqaLRRDIQFIFQDPYASLD-PR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDEVVLLGTFPNLGLFrrPKKAQKEKVVECLKQVKME-DFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLL--PGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 161 MVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVESTFvtKNIQAAY 224
Cdd:PRK10261 496 VSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLgQIVEIGPRRAVF--ENPQHPY 559
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-213 |
2.63e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.45 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV-------------------SGKSLDVIRKKIAYV 69
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgrgrAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 70 EQRSAID-LTFPIKVDevvllgtfpnlglfrRPKKAQKEKVVECLKQVKMEDFSNRQIGN-----LSGGQLQRVFIARAL 143
Cdd:TIGR03269 378 PHRTVLDnLTEAIGLE---------------LPDELARMKAVITLKMVGFDEEKAEEILDkypdeLSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 144 AQEADIIFLDEPFVGIDMVSE-KVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIM-NKQLVASGSVES 213
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKvDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMrDGKIVKIGDPEE 514
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
8-212 |
2.79e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 72.68 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE--SGEVTVSGKSLdvirkkiayveqrsaidltFPIKVDE 85
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDL-------------------LELEPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTF------------PNLGLFRRPKKAQKEK--------------VVECLKQVKM-EDFSNRQIG-NLSGGQLQRV 137
Cdd:TIGR01978 74 RARAGLFlafqypeeipgvSNLEFLRSALNARRSArgeepldlldfeklLKEKLALLDMdEEFLNRSVNeGFSGGEKKRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 138 FIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHdlhkTREYFDNL------IIMNKQLVASGSV 211
Cdd:TIGR01978 154 EILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH----YQRLLNYIkpdyvhVLLDGRIVKSGDV 229
|
.
gi 2282925441 212 E 212
Cdd:TIGR01978 230 E 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
2.80e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKT-----ESGEVTVSGKSL----DVI--RKKIAYV 69
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyrDVLefRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 70 EQRSAidlTFPIKVDEVVLLGTFPNLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGN----LSGGQLQRVFIARALAQ 145
Cdd:PRK14271 107 FQRPN---PFPMSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 146 EADIIFLDEPFVGIDMVSEKVIVDLLKELRNQgKTIVIVHHDLHKTREYFDN-LIIMNKQLVASGSVESTF 215
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRaALFFDGRLVEEGPTEQLF 250
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-185 |
4.40e-15 |
|
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: 73.70 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAI-ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-DV----IRKKIAYVEQrsaidl 77
Cdd:COG5265 366 GYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrDVtqasLRAAIGIVPQ------ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 tfpikvdEVVLLGT--FPNLGlFRRPkKAQKEKVVECLKQVKMEDFSNR-------QIG----NLSGGQLQRVFIARALA 144
Cdd:COG5265 440 -------DTVLFNDtiAYNIA-YGRP-DASEEEVEAAARAAQIHDFIESlpdgydtRVGerglKLSGGEKQRVAIARTLL 510
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRnQGKT-IVIVH 185
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVA-RGRTtLVIAH 551
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-209 |
4.80e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTV---SGKSLDVI-----------RKKI 66
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYalseaerrrllRTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 67 AYVEQRSAIDLTFPI----KVDEVVLLGTFPNLGLFRrpkkaqkEKVVECLKQVKMEdfSNRqIGNL----SGGQLQRVF 138
Cdd:PRK11701 92 GFVHQHPRDGLRMQVsaggNIGERLMAVGARHYGDIR-------ATAGDWLERVEID--AAR-IDDLpttfSGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 139 IARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASG 209
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQgRVVESG 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-209 |
7.54e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 73.34 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLiKTE---SGEVTVSG--KSLDVIRKKIAYVEQRsaiDLTFP-IKVD 84
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR-KTGgyiEGDIRISGfpKKQETFARISGYCEQN---DIHSPqVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLGTFpnlglFRRPKKAQKEK----VVECLKQVKMEDFSNRQIG-----NLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PLN03140 972 ESLIYSAF-----LRLPKEVSKEEkmmfVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKTIV-IVHHDLHKTREYFDNLIIMNK--QLVASG 209
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNTVDTGRTVVcTIHQPSIDIFEAFDELLLMKRggQVIYSG 1103
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-197 |
1.09e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVsGKSLDVirkkiAYVEQ-RSAIDltfPIK--VD 84
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEV-----AYFDQhRAELD---PEKtvMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EV------VLLGTFPN--LG-----LFrRPKKAqkekvvecLKQVKMedfsnrqignLSGGQLQRVFIARALAQEADIIF 151
Cdd:PRK11147 403 NLaegkqeVMVNGRPRhvLGylqdfLF-HPKRA--------MTPVKA----------LSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2282925441 152 LDEPFVGIDMVSekviVDLLKELRN--QGkTIVIVHHDlhktREYFDN 197
Cdd:PRK11147 464 LDEPTNDLDVET----LELLEELLDsyQG-TVLLVSHD----RQFVDN 502
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-173 |
1.21e-14 |
|
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: 73.02 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQH--KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTEsGEVTVSGKSLDvirkKIAYVEQRSAIDLt 78
Cdd:TIGR01271 1223 LTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWN----SVTLQTWRKAFGV- 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 79 FPIKVdeVVLLGTF-PNLGLFRRPKKAQKEKVVE--CLKQVkMEDFSNR---QIGN----LSGGQLQRVFIARALAQEAD 148
Cdd:TIGR01271 1297 IPQKV--FIFSGTFrKNLDPYEQWSDEEIWKVAEevGLKSV-IEQFPDKldfVLVDggyvLSNGHKQLMCLARSILSKAK 1373
|
170 180
....*....|....*....|....*
gi 2282925441 149 IIFLDEPFVGIDMVSEKVIVDLLKE 173
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-201 |
1.30e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK------IAYVEQRsaIDLTFPIK 82
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqeagIGIIHQE--LNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPfvgIDMV 162
Cdd:PRK10762 96 IAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2282925441 163 SE-------KVIvdllKELRNQGKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:PRK10762 173 TDteteslfRVI----RELKSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-201 |
1.85e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQH----KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE-----SGEVTVSGKSL-----DVIRK-- 64
Cdd:PRK15134 11 LSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlhaseQTLRGvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 65 --KIAYVEQRSAIDL----TFPIKVDEVVLLgtfpNLGLFRRPKKAQkekVVECLKQV-------KMEDFSNRqignLSG 131
Cdd:PRK15134 91 gnKIAMIFQEPMVSLnplhTLEKQLYEVLSL----HRGMRREAARGE---ILNCLDRVgirqaakRLTDYPHQ----LSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 132 GQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQ-GKTIVIVHHDLHKTREYFDNLIIM 201
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-188 |
2.17e-14 |
|
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: 72.29 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirkkIAYVEQRSAIDltfPIKVDEVVLLG 90
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQAWIQ---NDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLFRRPKKAqkekvVECLKQVKMEDFSNR-QIG----NLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM---- 161
Cdd:TIGR00957 723 KALNEKYYQQVLEA-----CALLPDLEILPSGDRtEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgk 797
|
170 180 190
....*....|....*....|....*....|
gi 2282925441 162 -VSEKVI--VDLLKelrnqGKTIVIVHHDL 188
Cdd:TIGR00957 798 hIFEHVIgpEGVLK-----NKTRILVTHGI 822
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-215 |
4.52e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKK----AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEV------------------TVSGKS 58
Cdd:PRK10261 18 LNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielsEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 59 LDVIR-KKIAYVEQRSAIDLTFPIKVDEVVLLGTFPNLGLFRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRV 137
Cdd:PRK10261 98 MRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 138 FIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVI-VHHDLHKTREYFDNLIIMNK-QLVASGSVESTF 215
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQgEAVETGSVEQIF 257
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-187 |
7.36e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 13 NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL-DVIRKK--IAYVEQRSAI--------DLTFPI 81
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPAErgVGMVFQSYALyphlsvaeNMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KvdevvLLGTfpnlglfrrpKKAQKEKVVECLKQV-KMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK11000 101 K-----LAGA----------KKEEINQRVNQVAEVlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|...
gi 2282925441 161 ------MVSEkvIVDLLKELrnqGKTIVIVHHD 187
Cdd:PRK11000 166 aalrvqMRIE--ISRLHKRL---GRTMIYVTHD 193
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-210 |
8.08e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLkamiGLI----KTESGEVTVSGKSL------DVIRKKIAYVEQRSA 74
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLIagarKIQQGRVEVLGGDMadarhrRAVCPRIAYMPQGLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 IDLTFPIKVDEvvllgtfpNLGLFRR----PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADII 150
Cdd:NF033858 87 KNLYPTLSVFE--------NLDFFGRlfgqDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2282925441 151 FLDEPFVGIDMVSEKVIVDLLKELRNQ--GKTiVIVhhdlhKTR-----EYFDNLIIMNK-QLVASGS 210
Cdd:NF033858 159 ILDEPTTGVDPLSRRQFWELIDRIRAErpGMS-VLV-----ATAymeeaERFDWLVAMDAgRVLATGT 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-197 |
8.74e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKKAI-ENVSVSIEPG-KItGIIGPNGAGKSTLLKAMIGLIKTESGEVTVS-GksldvirKKIAYVEQRSAIDltfP 80
Cdd:PRK11819 15 VVPPKKQIlKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPApG-------IKVGYLPQEPQLD---P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IK-VDEVVLLGTFPNLGLFRR---------PKKAQKEKVVEclKQVKMEDF--------SNRQ----------------I 126
Cdd:PRK11819 84 EKtVRENVEEGVAEVKAALDRfneiyaayaEPDADFDALAA--EQGELQEIidaadawdLDSQleiamdalrcppwdakV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 127 GNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSekviVDLL-KELRNQGKTIVIVHHDlhktrEYF-DN 197
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLeQFLHDYPGTVVAVTHD-----RYFlDN 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-185 |
9.17e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 18 IEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK--IAYVEQRSAidltfpIKVDevvlLGTFPNL 95
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfMAYLGHLPG------LKAD----LSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 96 ----GLF-RRPKKAQKekvvECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDL 170
Cdd:PRK13543 104 hflcGLHgRRAKQMPG----SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 2282925441 171 LK-ELRNQGKTIVIVH 185
Cdd:PRK13543 180 ISaHLRGGGAALVTTH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-186 |
9.44e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.79 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSldvirkKIAYVEQRSaidlTFPikvdevvlLG 90
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------DLLFLPQRP----YLP--------LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFpnlglfrrpkkaqKEKVVECLKQVkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDL 170
Cdd:cd03223 79 TL-------------REQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*.
gi 2282925441 171 LKELrnqGKTIVIVHH 186
Cdd:cd03223 134 LKEL---GITVISVGH 146
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-187 |
9.80e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 3 VAYQ--HKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVI-----RKKIAYVEQRSAI 75
Cdd:PRK10247 13 VGYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeiyRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 76 -------DLTFPIKVdevvllgtfpnlglfrRPKKAQKEKVVECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARALAQEA 147
Cdd:PRK10247 93 fgdtvydNLIFPWQI----------------RNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHD 187
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHD 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-187 |
1.29e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKiayveqrsaidltfPIkVDE 85
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREA--------------SL-IDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 VVLLGTFPNlglfrrpkkaqkekVVECLKQVKMED--FSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:COG2401 106 IGRKGDFKD--------------AVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*.
gi 2282925441 164 EKVIV-DLLKELRNQGKTIVIV-HHD 187
Cdd:COG2401 172 AKRVArNLQKLARRAGITLVVAtHHY 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-186 |
2.25e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLD----VIRKKIAYVEQrsAIDLTFPIKVDE 85
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagdiATRRRVGYMSQ--AFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vvllgtfpNLGL----FRRPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:NF033858 359 --------NLELharlFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180
....*....|....*....|....*.
gi 2282925441 162 VSEKVIVDLLKEL-RNQGKTIVIVHH 186
Cdd:NF033858 431 VARDMFWRLLIELsREDGVTIFISTH 456
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-188 |
2.53e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK-IAYVeqRSAIDLTFPikvDEV 86
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFL--RRQIGMIFQ---DHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 87 VLL--GTFPNLGLFRRPKKAQKE----KVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK10908 90 LLMdrTVYDNVAIPLIIAGASGDdirrRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180
....*....|....*....|....*...
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-182 |
3.02e-13 |
|
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: 68.78 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirkkIAYVEQRSAIdltFPIKVDEVVLLG 90
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------ISFSPQTSWI---MPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLFRRPKKA-QKEKVVECLKQVKMEDFSNRQIgNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVD 169
Cdd:TIGR01271 511 LSYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
170
....*....|....*
gi 2282925441 170 --LLKELRNQGKTIV 182
Cdd:TIGR01271 590 scLCKLMSNKTRILV 604
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-219 |
4.05e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSL------DVIRKKIAYV--EQRSA-----ID 76
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhnanEAINHGFALVteERRSTgiyayLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 77 LTFPIKVDEVVLLGTfpNLGLFRRPK-KAQKEKVVECLKqVKMEDFSNrQIGNLSGGQLQRVFIARALAQEADIIFLDEP 155
Cdd:PRK10982 343 IGFNSLISNIRNYKN--KVGLLDNSRmKSDTQWVIDSMR-VKTPGHRT-QIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 156 FVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNKQLVAsGSVESTFVTKN 219
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA-GIVDTKTTTQN 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-188 |
4.97e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 66.80 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTEsGEVTVSGKSLDvirkKIAYVEQRSAIDLtFPIKVdeVVLLG 90
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWN----SVPLQKWRKAFGV-IPQKV--FIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TF-PNLGLFRRPKKAQKEKVVE--CLKQVkMEDFSNR-----QIGN--LSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:cd03289 92 TFrKNLDPYGKWSDEEIWKVAEevGLKSV-IEQFPGQldfvlVDGGcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180
....*....|....*....|....*...
gi 2282925441 161 MVSEKVIVDLLKElRNQGKTIVIVHHDL 188
Cdd:cd03289 171 PITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
4-201 |
6.19e-13 |
|
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: 64.65 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHkkAIENVSVSIEPGKITGIIGPNGAGKSTLLKAmiGLIKTesgevtvsgksldvirKKIAYVEQRSAIDLTFPIKV 83
Cdd:cd03238 6 ANVH--NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYAS----------------GKARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEvvlLGTFPNLGLFRRPkkaqkekvveclkqvkmedfSNRQIGNLSGGQLQRVFIARALAQEAD--IIFLDEPFVGIDM 161
Cdd:cd03238 66 DQ---LQFLIDVGLGYLT--------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 162 VSEKVIVDLLKELRNQGKTIVIVHHDLhKTREYFDNLIIM 201
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIIDF 161
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
9-217 |
1.25e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKtESGEVTVSGKSLDVI---------RKKIA-------YVEQR 72
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIdllrlspreRRKLVghnvsmiFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 SAIDltfPIKVDEVVLLGTFPNL---GLFRRPKKAQKEKVVECLKQVKMEDFSNRQIG---NLSGGQLQRVFIARALAQE 146
Cdd:PRK15093 100 SCLD---PSERVGRQLMQNIPGWtykGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 147 ADIIFLDEPFVGIDMVSEKVIVDLLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMN-KQLVASGSVESTFVT 217
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYcGQTVETAPSKELVTT 249
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-182 |
1.31e-12 |
|
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: 65.65 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsldvirkkIAYVEQRSAIdltFPIKVDEVVLLG 90
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFSWI---MPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLFRRPKKA-QKEKVVeclkqVKMEDFSNRQIG----NLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEK 165
Cdd:cd03291 122 VSYDEYRYKSVVKAcQLEEDI-----TKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170
....*....|....*....
gi 2282925441 166 VIVD--LLKELRNQGKTIV 182
Cdd:cd03291 197 EIFEscVCKLMANKTRILV 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-188 |
1.55e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.35 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGL--IKTESGEVTVSGKSL------DVIRKKIAYVEQRSAIdltfp 80
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCrfkdirDSEALGIVIIHQELAL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 ikvdeVVLLGTFPNLGLFRRPKK-------AQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLD 153
Cdd:NF040905 90 -----IPYLSIAENIFLGNERAKrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 2282925441 154 EPFVGI-DMVSEKvIVDLLKELRNQGKTIVIVHHDL 188
Cdd:NF040905 165 EPTAALnEEDSAA-LLDLLLELKAQGITSIIISHKL 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-216 |
3.42e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.86 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKK---IAYVEQRSAIdltFP-IKVDE 85
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdIAMVFQNYAL---YPhMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 86 vvllgtfpNL--GL-FRRPKKAQ-KEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID- 160
Cdd:PRK11650 96 --------NMayGLkIRGMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDa 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282925441 161 -----MVSEkvivdlLKEL-RNQGKTIVIVHHDLHKTREYFDNLIIMNKqlvasGSVE-------------STFV 216
Cdd:PRK11650 168 klrvqMRLE------IQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNG-----GVAEqigtpvevyekpaSTFV 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-188 |
3.96e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE---SGEVTVSG--------KSLDVIR-KKIAYVEQRSAIDL 77
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreilnlpeKELNKLRaEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKVDEVVLlgtfPNLGLFRRPKKAQK-EKVVECLKQVKMEDfSNRQIG----NLSGGQLQRVFIARALAQEADIIFL 152
Cdd:PRK09473 111 NPYMRVGEQLM----EVLMLHKGMSKAEAfEESVRMLDAVKMPE-ARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 2282925441 153 DEPFVGIDMVSEKVIVDLLKELRNQGKT-IVIVHHDL 188
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDL 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-209 |
4.53e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 15 SVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEV-----TVSGKSLDVIRKKIAYVEQRSAIDLTFPIKVD----- 84
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfsHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDtgrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 -EVVLLGTfpnlglfrrpKKAQKekvveCL---KQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGID 160
Cdd:PRK10938 103 aEIIQDEV----------KDPAR-----CEqlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNL-IIMNKQLVASG 209
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAgVLADCTLAETG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-201 |
5.94e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLI----KTESGEVTVSGKSLDVIRK----KIAYVEQrsaIDLTFPI- 81
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKhyrgDVVYNAE---TDVHFPHl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 ----KVDEVVLLGTFPNlglfrRPKKAQKEKVVECLKQVKMEDFS-----NRQIGN-----LSGGQLQRVFIARALAQEA 147
Cdd:TIGR00956 154 tvgeTLDFAARCKTPQN-----RPDGVSREEYAKHIADVYMATYGlshtrNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 148 DIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIV--HHDLHKTREYFDNLIIM 201
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaiYQCSQDAYELFDKVIVL 284
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
17-203 |
8.04e-12 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 62.29 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 17 SIEPGKITGIIGPNGAGKSTLLKAMiglikTES--GEVTVSGKSLDViRKKIAYVEQRSAIDLTFPI-----KVDEVVLL 89
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAI-----TYAlyGKTPRYGRQENL-RSVFAPGEDTAEVSFTFQLggkkyRVERSRGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 gtfpNLGLFRRpkkaqkekvVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALA-----QEA-----DIIFLDEPFVGI 159
Cdd:cd03279 98 ----DYDQFTR---------IVLLPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlQNRggarlEALFIDEGFGTL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2282925441 160 DMVSEKVIVDLLKELRNQGKTIVIVHHDLHkTREYFDNLIIMNK 203
Cdd:cd03279 165 DPEALEAVATALELIRTENRMVGVISHVEE-LKERIPQRLEVIK 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-207 |
8.29e-12 |
|
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: 64.58 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLdvirKKIAYVEQRSAIDLtfpIKVDEVVLLG 90
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----AKIGLHDLRFKITI---IPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFP-NLGLFrrpKKAQKEKVVECLKQVKMEDFSNRQIG-----------NLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:TIGR00957 1375 SLRmNLDPF---SQYSDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 159 IDMVSEKVIvdlLKELRNQGK--TIVIVHHDLHKTREYfDNLIIMNKQLVA 207
Cdd:TIGR00957 1452 VDLETDNLI---QSTIRTQFEdcTVLTIAHRLNTIMDY-TRVIVLDKGEVA 1498
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-212 |
1.86e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIG--LIKTESGEVTVSGKSldvIRKKIAyvEQRS--AIDLTF--PIKVD 84
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGES---ILDLEP--EERAhlGIFLAFqyPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EVVLLgTFPNLGLFRRPKKAQKEKV---------VECLKQVKMED-FSNRQIGN-LSGGQLQRVFIARALAQEADIIFLD 153
Cdd:CHL00131 98 GVSNA-DFLRLAYNSKRKFQGLPELdplefleiiNEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 154 EPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHdLHKTREYF--DNLIIM-NKQLVASGSVE 212
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSENSIILITH-YQRLLDYIkpDYVHVMqNGKIIKTGDAE 237
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
12-187 |
2.89e-11 |
|
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: 60.70 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGkITGIIGPNGAGKSTLLKAmigLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTF--PIKVDEVVLl 89
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEA---LKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFenANGKKYTIT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 gtfpnlglfRRPkkAQKEKVVEClKQVKMEDFSNRQIGNLSGGQ------LQRVFIARALAQEADIIFLDEPFVGIDMVS 163
Cdd:cd03240 89 ---------RSL--AILENVIFC-HQGESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180
....*....|....*....|....*..
gi 2282925441 164 -EKVIVDLLKELRNQG--KTIVIVHHD 187
Cdd:cd03240 157 iEESLAEIIEERKSQKnfQLIVITHDE 183
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-184 |
3.00e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLlkAM------IGliKTESGEVTVSGKSLDV------IRKKIAYV-EQ 71
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMsvfgrsYG--RNISGTVFKDGKEVDVstvsdaIDAGLAYVtED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 72 RSAIDLtfpIKVDEVVLLGTFPNLGlfrrpkKAQKEKVVECLKQVKM-EDFSNR----------QIGNLSGGQLQRVFIA 140
Cdd:NF040905 346 RKGYGL---NLIDDIKRNITLANLG------KVSRRGVIDENEEIKVaEEYRKKmniktpsvfqKVGNLSGGNQQKVVLS 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2282925441 141 RALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIV 184
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-198 |
4.87e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSldvirkKIAYVEQRSAIDltFP 80
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA------NIGYYAQDHAYD--FE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IkvDEVVllgtFPNLGLFRRPKkaQKEKVVECL--KQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:PRK15064 397 N--DLTL----FDWMSQWRQEG--DDEQAVRGTlgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 159 IDMVSekvIVDLLKELRNQGKTIVIVHHDlhktREYFDNL 198
Cdd:PRK15064 469 MDMES---IESLNMALEKYEGTLIFVSHD----REFVSSL 501
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
4-187 |
5.52e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 60.35 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 4 AYQHKkaIENVSVSIEPGKITGIIGPNGAGKSTL--------------------LKAMIGLIKTEsgEVT-VSGKSLDV- 61
Cdd:cd03270 6 AREHN--LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayARQFLGQMDKP--DVDsIEGLSPAIa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 62 IRKKIAYVEQRSAIDLTFPIKvDEVVLLgtFPNLGLFRRpkkaqkekvVECLKQVKMEDFS-NRQIGNLSGGQLQRVFIA 140
Cdd:cd03270 82 IDQKTTSRNPRSTVGTVTEIY-DYLRLL--FARVGIRER---------LGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2282925441 141 RAL-AQEADIIF-LDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:cd03270 150 TQIgSGLTGVLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-185 |
2.30e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVirKKIAYVEQRSAIDLtfpIKVDEVVLLG 90
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDV--AKFGLTDLRRVLSI---IPQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFP-NLGLFRRPKKAQkekVVECLKQVKMED-FSNRQIG----------NLSGGQLQRVFIARALAQEADIIFLDEPFVG 158
Cdd:PLN03232 1325 TVRfNIDPFSEHNDAD---LWEALERAHIKDvIDRNPFGldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180
....*....|....*....|....*..
gi 2282925441 159 IDMVSEKVIVDLLKELRNQGKTIVIVH 185
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVIAH 1428
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-212 |
2.74e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSgKSLdvirkKIAYVEQRSaidLTFp 80
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGI-----KLGYFAQHQ---LEF- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 IKVDEVvllgtfPNLGLFRRPKKAQKEKVVECLKQVKME-DFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGI 159
Cdd:PRK10636 388 LRADES------PLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 160 DMVSEKVIVDLLKELRNqgkTIVIVHHDLHKTREYFDNLIimnkqLVASGSVE 212
Cdd:PRK10636 462 DLDMRQALTEALIDFEG---ALVVVSHDRHLLRSTTDDLY-----LVHDGKVE 506
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-204 |
4.20e-10 |
|
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: 56.60 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 6 QHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAmIGLIktesgevtVSGKSLDVIRKKIAYV-EQRSAIDLTFpikvd 84
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDA-IGLA--------LGGAQSATRRRSGVKAgCIVAAVSAEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 evvllgtfpnlgLFRRPKkaqkekvveclkqvkmedfsnrqignLSGGQLQRVFIARALA----QEADIIFLDEPFVGID 160
Cdd:cd03227 72 ------------IFTRLQ--------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2282925441 161 MVSEKVIVDLLKELRNQGKTIVIVHHDlHKTREYFDNLIIMNKQ 204
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKLIHIKKV 156
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
18-188 |
1.55e-09 |
|
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: 55.66 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 18 IEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVtvsgkSLDVIRkkIAYveqrsaidltfpikvdevvllgtfpnlgl 97
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----EWDGIT--PVY----------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 98 frrpkKAQKEKvveclkqvkmedfsnrqignLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQ 177
Cdd:cd03222 66 -----KPQYID--------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170
....*....|..
gi 2282925441 178 G-KTIVIVHHDL 188
Cdd:cd03222 121 GkKTALVVEHDL 132
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-219 |
3.95e-09 |
|
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: 55.30 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVIRKKIAYVEQRSAIDLTFPIKVDEVV 87
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDPILFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 LLGTFPNlglfrrpKKAQKEKVVECLKQVKMEDFSNRQIG-----------NLSGGQLQRVFIARALAQEADIIFLDEPF 156
Cdd:cd03288 112 RFNLDPE-------CKCTDDRLWEALEIAQLKNMVKSLPGgldavvteggeNFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 157 VGIDMVSE----KVIVDLLKElrnqgKTIVIVHHDLHKTREYFDNLIIMNKQLVASGSVESTFVTKN 219
Cdd:cd03288 185 ASIDMATEnilqKVVMTAFAD-----RTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQED 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-188 |
4.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGksLDVIRKKIAYVEQRSAIdltfpIKVDEVVLLGTFP 93
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGLMDLRKVLGI-----IPQAPVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 94 -NLGLFRRPKKAQkekVVECLKQVKMEDFSNRQ-IG----------NLSGGQLQRVFIARALAQEADIIFLDEPFVGIDM 161
Cdd:PLN03130 1331 fNLDPFNEHNDAD---LWESLERAHLKDVIRRNsLGldaevseageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180
....*....|....*....|....*....
gi 2282925441 162 VSEKVIvdlLKELRNQGK--TIVIVHHDL 188
Cdd:PLN03130 1408 RTDALI---QKTIREEFKscTMLIIAHRL 1433
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-186 |
5.05e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE--SGEVTVSGKSLDVIRKkiayvEQRSA---- 74
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSP-----EDRAGegif 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 75 IDLTFPIKVDEV---VLLGTFPNLGLFRRPKKAQ-----KEKVVECLKQVKM-EDFSNRQIG-NLSGGQLQRVFIARALA 144
Cdd:PRK09580 82 MAFQYPVEIPGVsnqFFLQTALNAVRSYRGQEPLdrfdfQDLMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2282925441 145 QEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHH 186
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-199 |
1.39e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSldvirkKIAYVEQRSAidlTFPIKVDEVVLLG 90
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNW------QLAWVNQETP---ALPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLFRRPKKAQKEKVVECLKQV--KME------------------DFSNRQ----IGNLSGGQLQRVFIARALAQE 146
Cdd:PRK10636 88 DREYRQLEAQLHDANERNDGHAIATIhgKLDaidawtirsraasllhglGFSNEQlerpVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 147 ADIIFLDEPFVGIDMvseKVIVDLLKELRNQGKTIVIVHHDlhktREYFDNLI 199
Cdd:PRK10636 168 SDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGTLILISHD----RDFLDPIV 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
8-186 |
1.75e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAyveqrSAIDLTFPIKVDEVV 87
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-----TYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 88 llgtFPNLGLFRRPKKAqKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVI 167
Cdd:PRK13541 88 ----FENLKFWSEIYNS-AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*....
gi 2282925441 168 VDLLKELRNQGKTIVIVHH 186
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSH 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
20-205 |
2.03e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 20 PGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVsgksldvirkkiayveqrsaIDLtfpikvdevvllgtfpnlglfr 99
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------IDG---------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 100 rpkkaqkEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVD------LLKE 173
Cdd:smart00382 39 -------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLL 111
|
170 180 190
....*....|....*....|....*....|....*..
gi 2282925441 174 LRNQGKTIVIVHHDLHK-----TREYFDNLIIMNKQL 205
Cdd:smart00382 112 KSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-209 |
2.29e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE---SGEVTVSGKSLD--VIRKKIAYVEQRSA--------IDL 77
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNefVPRKTSAYISQNDVhvgvmtvkETL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 78 TFPIKVDEVvllGTFPNL--GLFRRPKKA-----------QKEKVVECLKQVKMEDFSNRQIG---------------NL 129
Cdd:PLN03140 261 DFSARCQGV---GTRYDLlsELARREKDAgifpeaevdlfMKATAMEGVKSSLITDYTLKILGldickdtivgdemirGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 130 SGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKEL--RNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLV 206
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvhLTEATVLMSLLQPAPETFDLFDDIILLSEgQIV 417
|
...
gi 2282925441 207 ASG 209
Cdd:PLN03140 418 YQG 420
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-194 |
2.33e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGkSLDVIRKKIAYVEQRSAIdltfpikvDEVVLL 89
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-SAALIAISSGLNGQLTGI--------ENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 GTFpnLGLfrrPKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVD 169
Cdd:PRK13545 110 GLM--MGL---TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180
....*....|....*....|....*
gi 2282925441 170 LLKELRNQGKTIVIVHHDLHKTREY 194
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSF 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-187 |
3.00e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGkslDVIrkkIAYVEQ---RSAIDLTFPI---KVD 84
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ---DLI---VARLQQdppRNVEGTVYDFvaeGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 85 EV-----------VLLGTFPNLGLFRRPKKAQKE-----------KVVECLKQVKMEdfSNRQIGNLSGGQLQRVFIARA 142
Cdd:PRK11147 93 EQaeylkryhdisHLVETDPSEKNLNELAKLQEQldhhnlwqlenRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2282925441 143 LAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNqgkTIVIVHHD 187
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHD 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-207 |
3.01e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 14 VSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK-----SLDVIRKKIAYVEQRsaidltfPIKVDEVVL 88
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayGLRELRRQFSMIPQD-------PVLFDGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 89 LGTFPNLglfrrpkKAQKEKVVECLKQVKM--------EDFSNRQI---GNLSGGQLQRVFIARALAQE-ADIIFLDEPF 156
Cdd:PTZ00243 1402 QNVDPFL-------EASSAEVWAALELVGLrervasesEGIDSRVLeggSNYSVGQRQLMCMARALLKKgSGFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 157 VGIDMVSEKVIVDLLKELRNqGKTIVIVHHDLHKTREYfDNLIIMNKQLVA 207
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFS-AYTVITIAHRLHTVAQY-DKIIVMDHGAVA 1523
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-202 |
3.47e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 3.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 128 NLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQG-KTIVIVHHDLHKTREYfDNLIIMN 202
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRS-DKIVVFN 1432
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-203 |
3.51e-08 |
|
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: 51.88 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 8 KKAIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTE---SGEVTVSGKSLDVIRKK----IAYVEQRsaiDLTFP 80
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKypgeIIYVSEE---DVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 81 -IKVDEVVllgtfpnlglfrrpkkaqkekvveclkqvkmeDFSNRQIGN-----LSGGQLQRVFIARALAQEADIIFLDE 154
Cdd:cd03233 97 tLTVRETL--------------------------------DFALRCKGNefvrgISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 155 PFVGIDMVSekvIVDLLKELRNQGK-----TIVIVHHDLHKTREYFDNLIIMNK 203
Cdd:cd03233 145 STRGLDSST---ALEILKCIRTMADvlkttTFVSLYQASDEIYDLFDKVLVLYE 195
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-187 |
4.38e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 4.38e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282925441 123 NRQIGNLSGGQLQRVFIARALAQEADII--FLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHD 187
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-212 |
1.05e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGKITGIIGPNGAG--KSTLLKAMIGlikTESGEVTVSGKSLDVIRKKIayveqRSAIDLTFPIKVDEV 86
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRAL-----RRTIG*HRPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 87 VLLGTFPNLGLFRR----PKKAQKEKVVECLKQVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMV 162
Cdd:NF000106 99 ESFSGRENLYMIGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2282925441 163 SEKVIVDLLKELRNQGKTIVIVHHDLHKTREYFDNLIIMNK-QLVASGSVE 212
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRgRVIADGKVD 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-204 |
2.20e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 5 YQHKKAIE---NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGK------SLDVIRKKIAYVEQR--- 72
Cdd:PTZ00265 392 YDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdiNLKWWRSKIGVVSQDpll 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 73 --------------SAIDLTF------------------------PIKVDEVVLLGTFPNLGLFRRPKKAQ---KEKVVE 111
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEAlsnyynedgndsqenknkrnscraKCAGDLNDMSNTTDSNELIEMRKNYQtikDSEVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 112 CLKQVKMEDFSN-----------RQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELR-NQGK 179
Cdd:PTZ00265 552 VSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
|
250 260
....*....|....*....|....*
gi 2282925441 180 TIVIVHHDLHKTReYFDNLIIMNKQ 204
Cdd:PTZ00265 632 ITIIIAHRLSTIR-YANTIFVLSNR 655
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
10-194 |
3.33e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 10 AIENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKsLDVIRKKIAYVEQRSAIDltfpiKVDEVVLL 89
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAGLSGQLTGIE-----NIEFKMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 90 gtfpnLGLFRRPKKAQKEKVVEClkqVKMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMVSEKVIVD 169
Cdd:PRK13546 113 -----MGFKRKEIKAMTPKIIEF---SELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180
....*....|....*....|....*
gi 2282925441 170 LLKELRNQGKTIVIVHHDLHKTREY 194
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQF 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
11-175 |
1.33e-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: 48.59 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSldvirkKIAYVEQRSAIDltfpikvdevvlLG 90
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG------KLFYVPQRPYMT------------LG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFPNLGLFRRPKKAQKEK------VVECLKQVKMEDFSNRQIG---------NLSGGQLQRVFIARALAQEADIIFLDE- 154
Cdd:TIGR00954 530 TLRDQIIYPDSSEDMKRRglsdkdLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDEc 609
|
170 180
....*....|....*....|..
gi 2282925441 155 -PFVGIDMvsEKVIVDLLKELR 175
Cdd:TIGR00954 610 tSAVSVDV--EGYMYRLCREFG 629
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
129-189 |
2.25e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 2.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 129 LSGGQLQRVFIARALAQEAD---IIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLH 189
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-212 |
3.04e-06 |
|
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: 47.70 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 129 LSGGQLQRVFIARALAQEAD---IIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLH--KTREYfdnlII--- 200
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDviKTADY----IIdlg 905
|
90
....*....|....*..
gi 2282925441 201 -----MNKQLVASGSVE 212
Cdd:TIGR00630 906 peggdGGGTVVASGTPE 922
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-212 |
8.22e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 123 NRQIGNLSGGQLQRVFIARALAQE--ADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDlHKTREYFDNLII 200
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYVID 561
|
90
....*....|....*....
gi 2282925441 201 MNK-------QLVASGSVE 212
Cdd:TIGR00630 562 IGPgagehggEVVASGTPE 580
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-194 |
8.86e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 8.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282925441 124 RQIGNLSGGQLQRVFIARAL---AQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLH--KTREY 194
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHvvKVADY 880
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
9-40 |
1.48e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.31 E-value: 1.48e-05
10 20 30
....*....|....*....|....*....|..
gi 2282925441 9 KAIENVSVSIEPgkITGIIGPNGAGKSTLLKA 40
Cdd:COG4637 11 KSLRDLELPLGP--LTVLIGANGSGKSNLLDA 40
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
123-187 |
2.56e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 2.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 123 NRQIGNLSGGQLQRVFIARAL-AQEADIIF-LDEPFVGI---DMvsEKVIvDLLKELRNQGKTIVIVHHD 187
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQIgSGLVGVLYvLDEPSIGLhqrDN--DRLI-ETLKRLRDLGNTVIVVEHD 546
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
9-224 |
2.85e-05 |
|
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: 44.22 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIEPGkITGIIGPNGAGKSTLLKAmIGLIKTESGEVTVS---------------------GKSLDVIRKKIA 67
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEA-LRLLLGPSSSRKFDeedfylgddpdlpeieieltfGSLLSRLLRLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 68 YVEQRSAIDL---TFPIKVDEVV----------LLGTFPNLGLFRRPKKAQKEKVVECLKqVKMEDFSNRQIGNLSGGQL 134
Cdd:COG3593 90 KEEDKEELEEaleELNEELKEALkalnellseyLKELLDGLDLELELSLDELEDLLKSLS-LRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 135 QRVFIA--RALAQ-----EADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDLHKTREY-FDNLIIMNKQlv 206
Cdd:COG3593 169 RLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRD-- 246
|
250
....*....|....*...
gi 2282925441 207 aSGSVESTFVTKNIQAAY 224
Cdd:COG3593 247 -SGGTTSTKLIDLDDEDL 263
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-189 |
4.01e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 12 ENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVS-GKSLDVIRK-KIAYvEQRSAIDLTF---------- 79
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQdQFAF-EEFTVLDTVImghtelwevk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 80 ---------P-------IKVDEvvLLGTFPNLGLFRRPKKAQkekvvECLKQVKM-EDFSNRQIGNLSGGQLQRVFIARA 142
Cdd:PRK15064 97 qerdriyalPemseedgMKVAD--LEVKFAEMDGYTAEARAG-----ELLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2282925441 143 LAQEADIIFLDEPFVGIDMVSekvIVDLLKELRNQGKTIVIVHHDLH 189
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMIIISHDRH 213
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
11-174 |
4.83e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.49 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLIKTESGEVTVSGKSLDVIRKKIAYVEQRSAIDLTFpiKVDEVVLLG 90
Cdd:COG1106 19 LSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPSEFEILF--LLDGVRYEY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 91 TFpnlglfrrpkKAQKEKVVECLKQV--KMEDFSNRQIGNLSGGQLQRVFIARALAQEADIIFLDEPFvgidmvsEKVIV 168
Cdd:COG1106 97 GF----------ELDKERIISEWLYFlsTAAQLNVPLLSPLYDWFDNNISLDTSSDGLTLLLKEDESL-------KEELL 159
|
....*.
gi 2282925441 169 DLLKEL 174
Cdd:COG1106 160 ELLKIA 165
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
9-66 |
5.01e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.45 E-value: 5.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIE-PGKITGIIGPNGAGKSTLLKAM-IGLIKTESGEVTVSGKSLDVIRKKI 66
Cdd:COG3950 12 RGFEDLEIDFDnPPRLTVLVGENGSGKTTLLEAIaLALSGLLSRLDDVKFRKLLIRNGEF 71
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-45 |
8.49e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 8.49e-05
10 20 30
....*....|....*....|....*....|...
gi 2282925441 13 NVSVSIEPGKITGIIGPNGAGKSTLLKAMIGLI 45
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
122-203 |
1.84e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 122 SNRQIGNLSGGQLQRVFIARALA----------QEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHdLHKT 191
Cdd:TIGR00618 944 SVRPSATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISH-VPEF 1022
|
90
....*....|..
gi 2282925441 192 REYFDNLIIMNK 203
Cdd:TIGR00618 1023 RERIPHRILVKK 1034
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-215 |
3.07e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 11 IENVSVSIEPGKITGIIGPNGAGKSTLLKAMigliktesgevtvSGKSLDVIRK--KIAYVEQR------SAIDLTFPIK 82
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYM-------------AMHAIDGIPKncQILHVEQEvvgddtTALQCVLNTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 83 VDEVVLL----------GTFPNLGLFRRPKKAQK---------EKVVECLKQVKMED----------------FS----N 123
Cdd:PLN03073 260 IERTQLLeeeaqlvaqqRELEFETETGKGKGANKdgvdkdavsQRLEEIYKRLELIDaytaearaasilaglsFTpemqV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 124 RQIGNLSGGQLQRVFIARALAQEADIIFLDEPFVGIDMvseKVIVDLLKELRNQGKTIVIVHHdlhkTREYF-----DNL 198
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSH----AREFLntvvtDIL 412
|
250
....*....|....*..
gi 2282925441 199 IIMNKQLVASGSVESTF 215
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTF 429
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
23-186 |
3.27e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 23 ITGIIGPNGAGKSTLLKAM-----------------IGLIKTESGEVTVS----GKSLDVIRkkiAYVEQRSAIDLTFPI 81
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIryalygkarsrsklrsdLINVGSEEASVELEfehgGKRYRIER---RQGEFAEFLEAKPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 82 KVDevvLLGTFPNLGLFRRPKKAQKEKVVECLKQV---------------KMEDFSNrqIGNLSGGQLQRVFIARALAqe 146
Cdd:COG0419 102 RKE---ALKRLLGLEIYEELKERLKELEEALESALeelaelqklkqeilaQLSGLDP--IETLSGGERLRLALADLLS-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2282925441 147 adiIFLDepFVGIDMVSEKVIVDLLKELRnqgktiVIVHH 186
Cdd:COG0419 175 ---LILD--FGSLDEERLERLLDALEELA------IITHV 203
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
20-97 |
4.25e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 41.26 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 20 PGKITGIIGPNGAGKSTLLKAMI-----GLIKTESGEVTV-SGKsldviRKKIAYVEQRSAIDLTFPI-KVDEVVLLGTF 92
Cdd:COG5192 68 PPFIVAVVGPPGTGKSTLIRSLVrrftkQTIDEIRGPITVvSGK-----TRRITFLECPSDLHQMIDVaKIADLVLLLID 142
|
....*
gi 2282925441 93 PNLGL 97
Cdd:COG5192 143 GNFGF 147
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
129-188 |
4.94e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 4.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282925441 129 LSGGQLQRVFIARALAQEAD---IIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVIVHHDL 188
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
23-41 |
6.41e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 6.41e-04
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
123-173 |
1.72e-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: 36.44 E-value: 1.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282925441 123 NRQIGNLSGGQLQRVF---IARALAQ---EAD-------IIFLDEPFVGIDMVSEKVIVDLLKE 173
Cdd:pfam13558 27 YRRSGGLSGGEKQLLAylpLAAALAAqygSAEgrppaprLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
12-40 |
3.28e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.44 E-value: 3.28e-03
10 20
....*....|....*....|....*....
gi 2282925441 12 ENVSVSIEPGkITGIIGPNGAGKSTLLKA 40
Cdd:cd03278 14 DKTTIPFPPG-LTAIVGPNGSGKSNIIDA 41
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-41 |
3.37e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 3.37e-03
10 20 30
....*....|....*....|....*....|...
gi 2282925441 9 KAIENVSVSIEPGkITGIIGPNGAGKSTLLKAM 41
Cdd:pfam13476 7 RSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
9-183 |
3.95e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 37.64 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 9 KAIENVSVSIepGKITGIIGPNGAGKSTLLKAMIGLiktesgevtvsgKSLDVI-----RKKIAYVEQRSAIDLTFPIKV 83
Cdd:COG4938 10 GPFKEAELEL--KPLTLLIGPNGSGKSTLIQALLLL------------LQSNFIylpaeRSGPARLYPSLVRELSDLGSR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282925441 84 DEVV--LLGTFPNLGLFRRPKKAQKEKVVECLK------------------QVKMEDFSNRQ-IGNLSGGQLQR---VFI 139
Cdd:COG4938 76 GEYTadFLAELENLEILDDKSKELLEQVEEWLEkifpgkvevdassdlvrlVFRPSGNGKRIpLSNVGSGVSELlpiLLA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2282925441 140 ARALAQEADIIFLDEPFVGIDMVSEKVIVDLLKELRNQGKTIVI 183
Cdd:COG4938 156 LLSAAKPGSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVII 199
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
21-52 |
4.36e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 4.36e-03
10 20 30
....*....|....*....|....*....|..
gi 2282925441 21 GKITGIIGPNGAGKSTLLKAMIGLIKTESGEV 52
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-35 |
5.75e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 37.61 E-value: 5.75e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
17-42 |
5.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 5.96e-03
10 20
....*....|....*....|....*..
gi 2282925441 17 SIEP-GKITGIIGPNGAGKSTLLKAMI 42
Cdd:COG4913 19 TIDFdGRGTLLTGDNGSGKSTLLDAIQ 45
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
12-63 |
6.09e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 36.89 E-value: 6.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2282925441 12 ENVSVSIEPGKiTGIIGPNGAGKSTLLKAmIGLIKTESGEVTVSGKslDVIR 63
Cdd:cd03242 13 AELELEFEPGV-TVLVGENAQGKTNLLEA-ISLLATGKSHRTSRDK--ELIR 60
|
|
| PRK12289 |
PRK12289 |
small ribosomal subunit biogenesis GTPase RsgA; |
21-57 |
7.75e-03 |
|
small ribosomal subunit biogenesis GTPase RsgA;
Pssm-ID: 237040 [Multi-domain] Cd Length: 352 Bit Score: 36.92 E-value: 7.75e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2282925441 21 GKITGIIGPNGAGKSTLLKAMIGLIKTESGEvtVSGK 57
Cdd:PRK12289 172 NKITVVAGPSGVGKSSLINRLIPDVELRVGK--VSGK 206
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
21-52 |
8.52e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 36.72 E-value: 8.52e-03
10 20 30
....*....|....*....|....*....|..
gi 2282925441 21 GKITGIIGPNGAGKSTLLKAMIGLIKTESGEV 52
Cdd:PRK00098 164 GKVTVLAGQSGVGKSTLLNALAPDLELKTGEI 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-38 |
9.01e-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: 36.91 E-value: 9.01e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2282925441 1 MTVAYQHKKAIENVSVSIEPGKITGIIGPNGAGKSTLL 38
Cdd:TIGR00630 614 LTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
21-52 |
9.23e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 35.98 E-value: 9.23e-03
10 20 30
....*....|....*....|....*....|..
gi 2282925441 21 GKITGIIGPNGAGKSTLLKAMIGLIKTESGEV 52
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
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