|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
4.08e-95 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 278.13 E-value: 4.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNAIGYLPQLSE 77
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkppRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 78 FDRQFPISVRDLVLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDE 157
Cdd:COG1121 86 VDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316063307 158 PFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHLTPDGHRWGEAQPIL 218
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-212 |
9.41e-88 |
|
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: 258.62 E-value: 9.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 4 LQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNAIGYLPQLSEFDR 80
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 QFPISVRDLVLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:cd03235 82 DFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 161 GIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHLTPDGHRWG 212
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-202 |
1.16e-70 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 214.41 E-value: 1.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 10 GYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLSEFDRQFPISVRDL 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR---VAYVPQRSEVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:NF040873 78 VAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|...
gi 2316063307 170 LLQIIEQLHAEGRTILAVLHDLELVGQHFPNIL 202
Cdd:NF040873 158 IIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-197 |
1.40e-63 |
|
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: 198.34 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNA--IGYL 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslSRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSEFDrqFPISVRDLVLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:COG1120 81 PQEPPAP--FGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELVGQH 197
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARY 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-197 |
1.63e-45 |
|
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: 149.89 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 3 ALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNA--IGYLPQ 74
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlaslSPKELArkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 lsefdrqfpisvrdlvlmgslphrgllrsihvnwhrkatdALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIIL 154
Cdd:cd03214 81 ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELVGQH 197
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARY 164
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-191 |
3.04e-45 |
|
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: 150.77 E-value: 3.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG---DGSKDNAIGYLPQLSEFDRQFPISVRDLVLMGSLPHRGLL 101
Cdd:TIGR03771 4 DKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAgasPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHIGWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 102 RSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEG 181
Cdd:TIGR03771 84 RRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGAG 163
|
170
....*....|
gi 2316063307 182 RTILAVLHDL 191
Cdd:TIGR03771 164 TAILMTTHDL 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-204 |
4.22e-43 |
|
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: 145.17 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG--DGSKDNA------IGYL 72
Cdd:COG1122 1 IELENLSFSYPGGTPaLDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkDITKKNLrelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSefDRQF--PiSVRDLVLMGsLPHRGLLRS-IHvnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQ 149
Cdd:COG1122 81 FQNP--DDQLfaP-TVEEDVAFG-PENLGLPREeIR----ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 150 APIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-204 |
2.13e-42 |
|
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: 142.99 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 4 LQELAFGYRSQPPLAtLSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSG----------SFSLGDGSKDnaIG 70
Cdd:cd03225 2 LKNLSFSYPDGARPA-LDDIsltIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGevlvdgkdltKLSLKELRRK--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQlsEFDRQF-PISVRDLVLMGsLPHRGLLRSIHVnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQ 149
Cdd:cd03225 79 LVFQ--NPDDQFfGPTVEEEVAFG-LENLGLPEEEIE---ERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 150 APIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-206 |
3.77e-42 |
|
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: 142.23 E-value: 3.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA-------IGYLP 73
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAredyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 74 QLSEFDRQFpiSVRD-LVLMGSLphRGLLRSihvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:COG4133 82 HADGLKPEL--TVREnLRFWAAL--YGLRAD-----REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVgqHFPNILHLTP 206
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-202 |
9.66e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.12 E-value: 9.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA----------- 68
Cdd:COG3638 2 MLELRNLSKRYPGGTPaLDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 IGYLPQlsefdrQFPI----SVRDLVLMGSLPHRGLLRSIHVNWHR----KATDALDAVSMKDFADRHIGVLSGGQLQRV 140
Cdd:COG3638 82 IGMIFQ------QFNLvprlSVLTNVLAGRLGRTSTWRSLLGLFPPedreRALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 141 LFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELVGQHFPNIL 202
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRII 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-191 |
9.79e-42 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 143.10 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL-----GDGSKDNAIGYLPQLSEFDRQFPISVRDLVLMGSLPHRGLL 101
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 102 RSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEG 181
Cdd:PRK15056 113 RRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG 192
|
170
....*....|
gi 2316063307 182 RTILAVLHDL 191
Cdd:PRK15056 193 KTMLVSTHNL 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-194 |
2.86e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.27 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG--DGSKDNA-----IGYLPQ 74
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgeDVARDPAevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 LSEFDRQFpiSVRD-LVLMGSLphRGLLRSIhvnWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPII 153
Cdd:COG1131 81 EPALYPDL--TVREnLRFFARL--YGLPRKE---ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 154 LLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEA 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-191 |
3.86e-39 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 135.91 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNA--IGYL 72
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlSSRQLArrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQlsefdrQFP----ISVRDLVLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLT 148
Cdd:PRK11231 82 PQ------HHLtpegITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 149 QAPIILLDEPFTGID-SHTTQaLLQIIEQLHAEGRTILAVLHDL 191
Cdd:PRK11231 156 DTPVVLLDEPTTYLDiNHQVE-LMRLMRELNTQGKTVVTVLHDL 198
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-194 |
4.61e-38 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 132.67 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL-GDGSKDN------AIGYLP 73
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVRKEprearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 74 QLSEF-DRqfpISVRDLVLMGSLPHRGLLRSIHvnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:COG4555 81 DERGLyDR---LTVRENIRYFAELYGLFDEELK----KRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEV 195
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-204 |
2.40e-37 |
|
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: 130.77 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA-----------IGYLPQlsefdrQFPI----SVRD 88
Cdd:cd03256 24 INPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkalrqlrrqIGMIFQ------QFNLierlSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 LVLMGSLPHRGLLRSIHVNWHR----KATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:cd03256 98 NVLSGRLGRRSTWRSLFGLFPKeekqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 165 HTTQALLQIIEQLHAE-GRTILAVLHDLELVGQHFPNILHL 204
Cdd:cd03256 178 ASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGL 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
5.40e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 125.23 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSG----------SFSLGDGSKDNAIg 70
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGevrlngrplaAWSPWELARRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 yLPQLSEFdrQFPISVRDLVLMGSLPHRgllrSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLL--- 147
Cdd:COG4559 80 -LPQHSSL--AFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 148 ----TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQ 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-208 |
1.16e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 127.65 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA--------IGYL 72
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraasrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQlsEFDRQFPISVRDLVLMGSLPHRGLLrSIHVNWHRKATD-ALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAP 151
Cdd:PRK09536 83 PQ--DTSLSFEFDVRQVVEMGRTPHRSRF-DTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 152 IILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQhFPNILHLTPDG 208
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAAR-YCDELVLLADG 215
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
27-221 |
4.89e-34 |
|
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: 122.62 E-value: 4.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDG--------SKDNAIGYLPQlsEFDRQFPISVRDLVLMGSLPHR 98
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrrARARRVALVEQ--DSDTAVPLTVRDVVALGRIPHR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 GLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLH 178
Cdd:TIGR03873 105 SLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 179 AEGRTILAVLHDLELVGQHFPNILHLtpDGHRWGEAQPILHSL 221
Cdd:TIGR03873 185 ATGVTVVAALHDLNLAASYCDHVVVL--DGGRVVAAGPPREVL 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-204 |
5.13e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 119.66 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 4 LQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgskdnaigylpqlSEFDRQFP 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------KDIAKLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 ISVRDLVlmGSLPHrgllrsihvnwhrkatdaldavsmkdfadrhigvLSGGQLQRVLFARLLLTQAPIILLDEPFTGID 163
Cdd:cd00267 69 EELRRRI--GYVPQ----------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 164 SHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-196 |
6.52e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.57 E-value: 6.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA--------IGYL 72
Cdd:COG4988 337 IELEDVSFSYPGGRPaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpaswrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSEFdrqFPISVRDLVLMGslphrgllrsihvnwHRKATD-----ALDAVSMKDFADR-------HIGV----LSGGQ 136
Cdd:COG4988 417 PQNPYL---FAGTIRENLRLG---------------RPDASDeeleaALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQ 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 137 LQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLELVGQ 196
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ 537
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
24-209 |
7.29e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 121.30 E-value: 7.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD----GSKDNA--------IGYLPQ----LSEFdrqfpiSVR 87
Cdd:COG1136 31 IEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisSLSERElarlrrrhIGFVFQffnlLPEL------TAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 88 DLVLMGSLPhRGLLRSIHvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPfTG-IDSHT 166
Cdd:COG1136 105 ENVALPLLL-AGVSRKER---RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEP-TGnLDSKT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 167 TQALLQIIEQLHAE-GRTILAVLHDLELVgQHFPNILHLTpDGH 209
Cdd:COG1136 180 GEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLR-DGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-209 |
2.20e-33 |
|
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: 119.90 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--------FSLGDGSKD----NAIGYLPQ----LSEFdrqfpiSVR 87
Cdd:cd03255 27 IEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdiSKLSEKELAafrrRHIGFVFQsfnlLPDL------TAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 88 DLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPfTG-IDSHT 166
Cdd:cd03255 101 ENVELP-LLLAGVPKK---ERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEP-TGnLDSET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 167 TQALLQIIEQLHAE-GRTILAVLHDLELVgQHFPNILHLtPDGH 209
Cdd:cd03255 176 GKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRIIEL-RDGK 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-192 |
2.29e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.96 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQP-PLATLSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGS---KDNAIGYLP 73
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVsltVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 74 QlsEfDRQFP-ISVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:COG1116 87 Q--E-PALLPwLTVLDNVALG-LELRGVPKA---ERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVD 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-193 |
3.36e-33 |
|
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: 118.90 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 7 LAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKD--NAIGYLPQlsEFDR 80
Cdd:cd03226 5 ISFSYKKGTEiLDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpiKAKErrKSIGYVMQ--DVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 Q-FPISVRDLVLMGS-LPHRGLlrsihvnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:cd03226 83 QlFTDSVREELLLGLkELDAGN---------EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2316063307 159 FTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLEL 193
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF 188
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-160 |
1.77e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 115.44 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 20 LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--FSLGDGSKDNA------IGYLPQlseFDRQFP-ISVRDLV 90
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilLDGQDLTDDERkslrkeIGYVFQ---DPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 91 LMGSLPHRglLRSIHVNwhRKATDALDAVSMKDFADRHIGV----LSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:pfam00005 81 RLGLLLKG--LSKREKD--ARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-206 |
2.87e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA--------IGYLP 73
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 74 QLSEFdrqFPISVRDLvlmgsLPHRGLLRSIHVNWHRkATDALDAVSM-KDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:COG4619 81 QEPAL---WGGTVRDN-----LPFPFQLRERKFDRER-ALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQII-EQLHAEGRTILAVLHDLELVGQHFPNILHLTP 206
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLrEYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-191 |
3.29e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.49 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG-------SKDNA--IGY 71
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-DGldvattpSRELAkrLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQlsefDRQFP--ISVRDLVLMGSLPH-RGLLRSIHvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLT 148
Cdd:COG4604 80 LRQ----ENHINsrLTVRELVAFGRFPYsKGRLTAED---REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 149 QAPIILLDEPFTGIDSHTTQALLQIIEQL-HAEGRTILAVLHDL 191
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDI 196
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-194 |
1.01e-31 |
|
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: 114.03 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS-FSLGDGSKDNA------IGYLPQ 74
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEiKVLGKDIKKEPeevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 LSEFDRQFpiSVRDLVLmgslphrgllrsihvnwhrkatdaldavsmkdfadrhigvLSGGQLQRVLFARLLLTQAPIIL 154
Cdd:cd03230 81 EPSLYENL--TVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEA 158
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
25-192 |
1.27e-31 |
|
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: 115.26 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGS---KDNAIGYLPQLsefDRQFP-ISVRDLVLMGsLPHRGL 100
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtgPGPDRGYVFQQ---DALLPwLTVLDNVALG-LELQGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 LRSIhvnWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHT----TQALLQIIEQ 176
Cdd:cd03293 104 PKAE---ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRE 180
|
170
....*....|....*.
gi 2316063307 177 lhaEGRTILAVLHDLE 192
Cdd:cd03293 181 ---TGKTVLLVTHDID 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-194 |
1.85e-31 |
|
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: 115.23 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD----GSKDNAIGYL--------PQLsefdrqFP-ISVRDLV 90
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditGLPPHEIARLgigrtfqiPRL------FPeLTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LMGSLPHRGLLRSIHVNWHR------KATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:cd03219 97 MVAAQARTGSGLLLARARREereareRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 165 HTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03219 177 EETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-204 |
3.60e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 119.87 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP--LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKD--------NAIGY 71
Cdd:COG4987 334 LELEDVSFRYPGAGRpvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldeddlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFdrqFPISVRDLVLMGSlphrgllrsihvnwhRKATD-----ALDAVSMKDFADR-------HIGV----LSGG 135
Cdd:COG4987 414 VPQRPHL---FDTTLRENLRLAR---------------PDATDeelwaALERVGLGDWLAAlpdgldtWLGEggrrLSGG 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 136 QLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQlHAEGRTILAVLHDLELVGqHFPNILHL 204
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLE-RMDRILVL 542
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-192 |
7.19e-31 |
|
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: 113.00 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 4 LQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGS------KDNAIGYLPQlse 77
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvppERRNIGMVFQ--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 78 FDRQFP-ISVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:cd03259 80 DYALFPhLTVAENIAFG-LKLRGVPKA---EIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQE 192
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-193 |
2.08e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.94 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKD--------NAIGYL 72
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspaelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSEFDrqFPISVRDLVLMGSLPHRGllrsihvnwHRKATD-----ALDAVSMKDFADRHIGVLSGGQLQRVLFARlLL 147
Cdd:PRK13548 82 PQHSSLS--FPFTVEEVVAMGRAPHGL---------SRAEDDalvaaALAQVDLAHLAGRDYPQLSGGEQQRVQLAR-VL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 148 TQ-------APIILLDEPFTGIDSHTTQALLQIIEQL-HAEGRTILAVLHDLEL 193
Cdd:PRK13548 150 AQlwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNL 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-194 |
3.71e-30 |
|
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: 112.20 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGY----RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSkdnaigylPQLS 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF-DGR--------PVTR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 77 EFDRQFPISVRdLVL---MGSL-PHRGLLRSI--------HVNWHRKATDALDAVSM-KDFADRHIGVLSGGQLQRVLFA 143
Cdd:COG1124 72 RRRKAFRRRVQ-MVFqdpYASLhPRHTVDRILaeplrihgLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 144 RLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVV 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-204 |
8.32e-30 |
|
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: 109.01 E-value: 8.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDN--------AIGY 71
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFdrqFPISVRDlvlmgslphrgllrsihvNwhrkatdaldavsmkdfadrhigVLSGGQLQRVLFARLLLTQAP 151
Cdd:cd03228 81 VPQDPFL---FSGTIRE------------------N-----------------------ILSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 152 IILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLELVgQHFPNILHL 204
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTI-RDADRIIVL 167
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-192 |
2.63e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYR--SQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA--------IGY 71
Cdd:PRK13635 6 IRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdvrrqVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQlsEFDRQF-PISVRDLVLMGsLPHRGLLRSIHVnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:PRK13635 86 VFQ--NPDNQFvGATVQDDVAFG-LENIGVPREEMV---ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQLHAEGR-TILAVLHDLE 192
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLD 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-194 |
3.01e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 114.23 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLAT--LSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDNAIGYLPQL 75
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVraVDDVsltLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF-DG-KDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 SEFDR------QFPIS-------VRDLVLMGSLPHRGLLRSihvNWHRKATDALDAVSM-KDFADRHIGVLSGGQLQRVL 141
Cdd:COG1123 338 RELRRrvqmvfQDPYSslnprmtVGDIIAEPLRLHGLLSRA---ERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 142 FARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVV 468
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-194 |
6.92e-29 |
|
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: 108.97 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDnaIGYLP-------------QLSefdRQFP-ISVRDLV 90
Cdd:COG0411 28 ERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF-DG-RD--ITGLPphriarlgiartfQNP---RLFPeLTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LMGSLPHRG--LLRSIHVNW---------HRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:COG0411 101 LVAAHARLGrgLLAALLRLPrarreereaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:COG0411 181 AGLNPEETEELAELIRRLRDErGITILLIEHDMDLV 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
24-192 |
8.64e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.01 E-value: 8.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-------GSKDNAIGYLPQ---LsefdrqFP-ISVRDLVLM 92
Cdd:COG1118 25 IASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlPPRERRVGFVFQhyaL------FPhMTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GsLPHRGLLRS-IHvnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALL 171
Cdd:COG1118 99 G-LRVRPPSKAeIR----ARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELR 173
|
170 180
....*....|....*....|..
gi 2316063307 172 QIIEQLHAE-GRTILAVLHDLE 192
Cdd:COG1118 174 RWLRRLHDElGGTTVFVTHDQE 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
30-192 |
1.21e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 108.25 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 30 TAIIGANGSGKSTLLKTLAGLLPPLSG-SFSLGD---GSKD-----NAIGYLPqlSEFDRQFP--ISVRDLVLMGSLPHR 98
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrGGEDvwelrKRIGLVS--PALQLRFPrdETVLDVVLSGFFDSI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 GLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLH 178
Cdd:COG1119 110 GLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLA 189
|
170
....*....|....*
gi 2316063307 179 AEG-RTILAVLHDLE 192
Cdd:COG1119 190 AEGaPTLVLVTHHVE 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-192 |
1.73e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSgcFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaigyLPQLSEFDR 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------LTALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 ------Q----FP-ISVRDLVLMGSLPHRGLLRsihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQ 149
Cdd:COG3840 72 pvsmlfQennlFPhLTVAQNIGLGLRPGLKLTA----EQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 150 APIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPE 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-206 |
3.83e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 105.73 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDN-----AIGYL-------PQLS-----EFD 79
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeACHYLghrnamkPALTvaenlEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFpisvrdlvlmgslpHRGLLRSIHvnwhrkatDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:PRK13539 98 AAF--------------LGGEELDIA--------AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAEGRTILAVLH-DLELVGQHfpnILHLTP 206
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLPGAR---ELDLGP 200
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-204 |
8.52e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 105.84 E-value: 8.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA-----------IGYLPQlsEFDRQFPISVRDLVLM 92
Cdd:TIGR02315 25 INPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkklrklrrrIGMIFQ--HYNLIERLTVLENVLH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLPHRGLLRSIHVNWHR----KATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:TIGR02315 103 GRLGYKPTWRSLLGRFSEedkeRALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSK 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 169 ALLQIIEQLHAE-GRTILAVLHDLELVGQHFPNILHL 204
Cdd:TIGR02315 183 QVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-204 |
1.12e-27 |
|
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: 105.21 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA---------IGYLPQlsefDRQ-FP-ISVRDLVLMG 93
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppheraragIGYVPE----GRRiFPeLTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPHRGllrsihvnwhRKATDALDAV-SM----KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:cd03224 100 AYARRR----------AKRKARLERVyELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 169 ALLQIIEQLHAEGRTILavlhdleLVGQHFPNILHL 204
Cdd:cd03224 170 EIFEAIRELRDEGVTIL-------LVEQNARFALEI 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
25-194 |
1.90e-27 |
|
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: 104.51 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA-----------IGYLPQ--LSEFDRQFpiSVRDLVL 91
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrkirrkeIQMVFQdpMSSLNPRM--TIGEQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 92 MGSLPHRGLlrsiHVNWHRKATDALDAVSM---KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:cd03257 107 EPLRIHGKL----SKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
170 180
....*....|....*....|....*..
gi 2316063307 169 ALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:cd03257 183 QILDLLKKLQEElGLTLLFITHDLGVV 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-197 |
1.92e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 109.22 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLAT--LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPP---LSGSFSLGDGSKDNA------- 68
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVdgVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 -IGYLPQlsEFDRQF-PISVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLL 146
Cdd:COG1123 84 rIGMVFQ--DPMTQLnPVTVGDQIAEA-LENLGLSRA---EARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELVGQH 197
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEI 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-191 |
1.94e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 105.45 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 5 QELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG-------SKDNA--IGYLPQl 75
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGehiqhyaSKEVArrIGLLAQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 sefDRQFP--ISVRDLVLMGSLPHRGLLrsihVNWHRKATDA----LDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQ 149
Cdd:PRK10253 89 ---NATTPgdITVQELVARGRYPHQPLF----TRWRKEDEEAvtkaMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 150 APIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDL 191
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDL 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-197 |
2.50e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 105.25 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 3 ALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNA--IGYLPQ 74
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswSSKAFArkVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 lsefdrQFP----ISVRDLVLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:PRK10575 93 ------QLPaaegMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQL-HAEGRTILAVLHDLELVGQH 197
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARY 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-204 |
2.88e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS-----FSLGDGSKDN------A 68
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngQDLSRLKRREipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 IGY-------LPQLSEFDR-QFPisvrdLVLMGsLPHRgllrsihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRV 140
Cdd:COG2884 81 IGVvfqdfrlLPDRTVYENvALP-----LRVTG-KSRK--------EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 141 LFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-192 |
8.87e-27 |
|
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: 102.27 E-value: 8.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGsLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL--GDGSKDN-----AIGYLPQ 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLKQPqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 lsEFDRQFPISVRDLvlmgsLPHRGLLRSIHVNWHRKATD-ALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPII 153
Cdd:cd03264 80 --EFGVYPNFTVREF-----LDYIAWLKGIPSKEVKARVDeVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316063307 154 LLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLE 192
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVE 190
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-194 |
1.09e-26 |
|
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: 102.75 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDnaigyLPQLSEFDR 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DG-QD-----ITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 -----------QFP-----ISVRDLVlmgSLP---HRGLLRS-IHvnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRV 140
Cdd:COG1127 78 yelrrrigmlfQGGalfdsLTVFENV---AFPlreHTDLSEAeIR----ELVLEKLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 141 LFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSA 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-194 |
1.33e-26 |
|
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: 107.23 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLAtLSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKD----------NA 68
Cdd:COG2274 474 IELENVSFRYPGDSPPV-LDNIsltIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG--IDlrqidpaslrRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 IGYLPQLSEFdrqFPISVRDLVLMGSlPHRGLlrsihvnwhRKATDALDAVSMKDFADRH-------IG----VLSGGQL 137
Cdd:COG2274 551 IGVVLQDVFL---FSGTIRENITLGD-PDATD---------EEIIEAARLAGLHDFIEALpmgydtvVGeggsNLSGGQR 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 138 QRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLELV 194
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTI 673
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-192 |
2.34e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLA--TLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG---SKDNaigyLPQL 75
Cdd:PRK13632 7 MIKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGitiSKEN----LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 SEF--------DRQF-PISVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLL 146
Cdd:PRK13632 82 RKKigiifqnpDNQFiGATVEDDIAFG-LENKKVPPK---KMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEG-RTILAVLHDLE 192
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMD 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-192 |
6.03e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 103.25 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKDNA--------IGYL 72
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--RDVTglppekrnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQ---LsefdrqFP-ISVRDLVLMGsLPHRGLLRS-IHvnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLL 147
Cdd:COG3842 83 FQdyaL------FPhLTVAENVAFG-LRMRGVPKAeIR----ARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 148 TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQE 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-192 |
1.18e-25 |
|
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: 99.89 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 9 FGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKD-------NAIGYLPQlseFDRQ 81
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdrkaarQSLGYCPQ---FDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 FP-ISVRD-LVLMGSLphRGLLRSI---HVNWHrkatdaLDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:cd03263 87 FDeLTVREhLRFYARL--KGLPKSEikeEVELL------LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLE 192
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMD 193
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-194 |
1.24e-25 |
|
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: 98.41 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPqlsEFDRQFPISVRDLVLMgslPHRgllrs 103
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP---PLRRRIGMVFQDFALF---PHL----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 104 ihvnwhrkatDALDAVSMkdfadrhigVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GR 182
Cdd:cd03229 92 ----------TVLENIAL---------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGI 152
|
170
....*....|..
gi 2316063307 183 TILAVLHDLELV 194
Cdd:cd03229 153 TVVLVTHDLDEA 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-192 |
1.46e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 99.29 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG-----DGSK-------DNAIGYLPQLSEFdrqFP-ISVRDLVLMG 93
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKkinlppqQRKIGLVFQQYAL---FPhLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPHRGLLRSIHVNwhrkatDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQI 173
Cdd:cd03297 100 LKRKRNREDRISVD------ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180
....*....|....*....|
gi 2316063307 174 IEQLHAE-GRTILAVLHDLE 192
Cdd:cd03297 174 LKQIKKNlNIPVIFVTHDLS 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
1.72e-25 |
|
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: 103.91 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA--------IGYL 72
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPaLRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdadswrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSEFdrqFPISVRDLVLMGSlphrgllrsihvnwhRKATD-----ALDAVSMKDFA-------DRHIGV----LSGGQ 136
Cdd:TIGR02857 402 PQHPFL---FAGTIAENIRLAR---------------PDASDaeireALERAGLDEFVaalpqglDTPIGEggagLSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316063307 137 LQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLELV 194
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA 520
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-192 |
3.93e-25 |
|
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: 98.73 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDNAIGYLPQLSEFDRQ 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-DG-EDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 FPI-----------SVRDLVLMGSLPHRGLLRSIhvnWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:cd03261 79 MGMlfqsgalfdslTVFENVAFPLREHTRLSEEE---IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-192 |
5.07e-25 |
|
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: 99.04 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLA--TLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS---FSLGDGSKDN------AIG 70
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAlkNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKvtvDGLDTLDEENlweirkKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLpqlseF---DRQF-PISVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLL 146
Cdd:TIGR04520 81 MV-----FqnpDNQFvGATVEDDVAFG-LENLGVPRE---EMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDME 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-194 |
5.11e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 97.43 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGskdnaigylpqlsEFDRQ 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-------------PLAEQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 FPISVRDLVLMGSLPhrGL------------LRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQ 149
Cdd:TIGR01189 68 RDEPHENILYLGHLP--GLkpelsalenlhfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 150 APIILLDEPFTGIDSHTTQALLQIIEQ-LHAEGRTILAVLHDLELV 194
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-194 |
1.01e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 97.05 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQEL--AFGYRSQPPLAT--LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG--DGSKDNA-----I 69
Cdd:cd03266 1 MITADALtkRFRDVKKTVQAVdgVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAearrrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 70 GYLP-QLSEFDRqfpISVRDLVLMGSLPHrGLLRsihvnwhRKATDALDAVS----MKDFADRHIGVLSGGQLQRVLFAR 144
Cdd:cd03266 81 GFVSdSTGLYDR---LTARENLEYFAGLY-GLKG-------DELTARLEELAdrlgMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEV 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-192 |
1.25e-24 |
|
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: 97.25 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLP-----PLSGSFSLgDGSKDNAIGYLPqlS 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLL-DGKDIYDLDVDV--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 77 EFDRQ----------FPISVRDLVLMGsLPHRGLLRSIHVnwHRKATDALDAVSMKD-FADR-HIGVLSGGQLQRVLFAR 144
Cdd:cd03260 78 ELRRRvgmvfqkpnpFPGSIYDNVAYG-LRLHGIKLKEEL--DERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEgRTILAVLHDLE 192
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
27-192 |
1.91e-24 |
|
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: 96.67 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG--DGSKDNA-----IGYLPQLSEFDRQFpISVRDLVLMGSLphRG 99
Cdd:cd03265 26 GEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghDVVREPRevrrrIGIVFQDLSVDDEL-TGWENLYIHARL--YG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 100 LLRSIhvnWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHA 179
Cdd:cd03265 103 VPGAE---RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKE 179
|
170
....*....|....
gi 2316063307 180 E-GRTILAVLHDLE 192
Cdd:cd03265 180 EfGMTILLTTHYME 193
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-192 |
2.31e-24 |
|
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: 97.33 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIGYlPQLSEFDRQfPISvrdLVL--MGSLPHRGLLR 102
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-DGQDIAAMSR-KELRELRRK-KIS---MVFqsFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 103 SI----------HVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:cd03294 122 NVafglevqgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180
....*....|....*....|.
gi 2316063307 173 IIEQLHAE-GRTILAVLHDLE 192
Cdd:cd03294 202 ELLRLQAElQKTIVFITHDLD 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-194 |
6.85e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNA-----IGYLPQ---LsefdrqFP-ISVRD-LVLMGS 94
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPedrrrIGYLPEergL------YPkMKVGEqLVYLAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LphRGLLRSIHvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:COG4152 98 L--KGLSKAEA---KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170 180
....*....|....*....|
gi 2316063307 175 EQLHAEGRTILAVLHDLELV 194
Cdd:COG4152 173 RELAAKGTTVIFSSHQMELV 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-194 |
1.25e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 94.27 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKD----NAIGYLPQlse 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarNRIGYLPE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 78 fDRQF--PISVRD-LVLMGSLphRGLLRSIHVNWhrkATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIIL 154
Cdd:cd03269 78 -ERGLypKMKVIDqLVYLAQL--KGLKKEEARRR---IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELV 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-204 |
1.38e-23 |
|
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: 94.10 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPplATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNAIGYLPQLSEF 78
Cdd:cd03298 1 VRLDKIRFSYGEQP--MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQFP-ISVRDLVLMGSLPhrgllrSIHVN-WHRKATD-ALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILL 155
Cdd:cd03298 79 NNLFAhLTVEQNVGLGLSP------GLKLTaEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316063307 156 DEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELVGQHFPNILHL 204
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-204 |
1.49e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 94.66 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA---------IGYLPQlsefDRQ-FP-ISVRDLVLMG 93
Cdd:COG0410 27 EEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpphriarlgIGYVPE----GRRiFPsLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPHRGllrsihvnwHRKATDALDAV-----SMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:COG0410 103 AYARRD---------RAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 169 ALLQIIEQLHAEGRTILavlhdleLVGQHFPNILHL 204
Cdd:COG0410 174 EIFEIIRRLNREGVTIL-------LVEQNARFALEI 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-195 |
2.27e-23 |
|
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: 93.33 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaigylpqlseFDRQFPISVRDLVLMGSLPHRGLLRSIH 105
Cdd:cd03231 25 AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-------------LDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 106 VN---WHRKATD-----ALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQl 177
Cdd:cd03231 92 ENlrfWHADHSDeqveeALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG- 170
|
170 180
....*....|....*....|
gi 2316063307 178 HAE--GRTILAVLHDLELVG 195
Cdd:cd03231 171 HCArgGMVVLTTHQDLGLSE 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
26-191 |
3.07e-23 |
|
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: 92.98 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAigyLPQLSEFDRQ----------FP-ISVRDLVLMGS 94
Cdd:cd03262 25 KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD---KKNINELRQKvgmvfqqfnlFPhLTVLENITLAP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRSIHVnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:cd03262 102 IKVKGMSKAEAE---ERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVM 178
|
170
....*....|....*..
gi 2316063307 175 EQLHAEGRTILAVLHDL 191
Cdd:cd03262 179 KDLAEEGMTMVVVTHEM 195
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
24-193 |
3.77e-23 |
|
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: 92.68 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKD-------------NAIGYLPQ---LSEFDrqfpiSVR 87
Cdd:TIGR03608 21 IEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL-NGQETpplnskkaskfrrEKLGYLFQnfaLIENE-----TVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 88 ---DLVLMGSlphrgllRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:TIGR03608 95 enlDLGLKYK-------KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP 167
|
170 180
....*....|....*....|....*....
gi 2316063307 165 HTTQALLQIIEQLHAEGRTILAVLHDLEL 193
Cdd:TIGR03608 168 KNRDEVLDLLLELNDEGKTIIIVTHDPEV 196
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-194 |
5.68e-23 |
|
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: 96.86 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNA-----IGY 71
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdiRQIDPAdlrrnIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSefdRQFPISVRDLVLMGSlPHrgllrsihvnwhrkATD-----ALDAVSMKDFADRH-------IG----VLSGG 135
Cdd:TIGR03375 544 VPQDP---RLFYGTLRDNIALGA-PY--------------ADDeeilrAAELAGVTEFVRRHpdgldmqIGergrSLSGG 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 136 QLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHD---LELV 194
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRtslLDLV 666
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-158 |
8.45e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLSEFDRQFpiSVRDLVLMGSLPHRGLLRS 103
Cdd:COG0488 21 INPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR---IGYLPQEPPLDDDL--TVLDTVLDGDAELRALEAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 104 IHV----------------------------NWHRKATDALDA--VSMKDFaDRHIGVLSGGQLQRVLFARLLLTQAPII 153
Cdd:COG0488 96 LEEleaklaepdedlerlaelqeefealggwEAEARAEEILSGlgFPEEDL-DRPVSELSGGWRRRVALARALLSEPDLL 174
|
....*
gi 2316063307 154 LLDEP 158
Cdd:COG0488 175 LLDEP 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-191 |
1.10e-22 |
|
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: 95.89 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 4 LQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD--------GSKDNAIGYLPQ 74
Cdd:TIGR02868 337 LRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 LSEFdrqFPISVRDLVLMGslphRG---------LLRSIHV-NWHRKATDALDAVSMKDFAdrhigVLSGGQLQRVLFAR 144
Cdd:TIGR02868 417 DAHL---FDTTVRENLRLA----RPdatdeelwaALERVGLaDWLRALPDGLDTVLGEGGA-----RLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLqiiEQLHA--EGRTILAVLHDL 191
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELL---EDLLAalSGRTVVLITHHL 530
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-194 |
1.39e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG----DGSKDNAIGYLPQLS 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 77 EF----DRQFPISVRDLVLMGSLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:PRK13638 81 TVfqdpEQQIFYTDIDSDIAFSLRNLGVPEA---EITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-204 |
1.89e-22 |
|
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: 91.16 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYrsQPPLATLSGC-FH--QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgskdNAIGYLP--QL 75
Cdd:TIGR02673 1 MIEFHNVSKAY--PGGVAALHDVsLHirKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAG----EDVNRLRgrQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 SEFDRQFPISVRDLVLmgsLPHRGLLRSIHV----------NWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARL 145
Cdd:TIGR02673 75 PLLRRRIGVVFQDFRL---LPDRTVYENVALplevrgkkerEIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 146 LLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-196 |
1.94e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRS-QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGdGSKDNA---------IGY 71
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVNAenekwvrskVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEfDRQFPISVRDLVLMGslPHRGLLRSIHVNwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAP 151
Cdd:PRK13647 84 VFQDPD-DQVFSSTVWDDVAFG--PVNMGLDKDEVE--RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316063307 152 IILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAE 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-189 |
2.04e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 95.23 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKD----------NAIG 70
Cdd:COG1132 340 IEFENVSFSYPGDRPvLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG--VDirdltleslrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLSE-FDRqfpiSVRDLVLMGSLphrgllrsihvnwhrKATD-----ALDAVSMKDFADR-------HIG----VLS 133
Cdd:COG1132 418 VVPQDTFlFSG----TIRENIRYGRP---------------DATDeeveeAAKAAQAHEFIEAlpdgydtVVGergvNLS 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 134 GGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLH 189
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-194 |
3.98e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 89.84 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGskdnaIGYLPQ----LSEfdrqfpiSVRDLVLMGSlphrg 99
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----IAYVSQepwiQNG-------TIRENILFGK----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 100 llrSIHVNWHRKATDA--LDavsmKDFA-----DR-HIGV----LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTT 167
Cdd:cd03250 91 ---PFDEERYEKVIKAcaLE----PDLEilpdgDLtEIGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG 163
|
170 180
....*....|....*....|....*....
gi 2316063307 168 QALLQ--IIEQLhAEGRTILAVLHDLELV 194
Cdd:cd03250 164 RHIFEncILGLL-LNNKTRILVTHQLQLL 191
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
25-191 |
4.17e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 90.82 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS-----FSLGDGSKD-NAIgylpqlsefdRQ-----------FP-ISV 86
Cdd:COG1126 25 EKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTitvdgEDLTDSKKDiNKL----------RRkvgmvfqqfnlFPhLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 87 RDLVLMGSLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPftgidsht 166
Cdd:COG1126 95 LENVTLAPIKVKKMSKA---EAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP-------- 163
|
170 180 190
....*....|....*....|....*....|...
gi 2316063307 167 TQAL--------LQIIEQLHAEGRTILAVLHDL 191
Cdd:COG1126 164 TSALdpelvgevLDVMRDLAKEGMTMVVVTHEM 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-192 |
6.53e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG----------SKDNAIGYLPQlsEFDrQFP-ISVRDLVLM 92
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL-DGepvrfrsprdAQAAGIAIIHQ--ELN-LVPnLSVAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLPHRGLLrsihVNW---HRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:COG1129 103 GREPRRGGL----IDWramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVER 178
|
170 180
....*....|....*....|...
gi 2316063307 170 LLQIIEQLHAEGRTILAVLHDLE 192
Cdd:COG1129 179 LFRIIRRLKAQGVAIIYISHRLD 201
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-197 |
6.81e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 20 LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgdgsKDNAIGylpqlsefdRQFPISVRDLVLMGSLPhrG 99
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW----QGEPIR---------RQRDEYHQDLLYLGHQP--G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 100 L---------LR---SIHVNWHRKAT-DALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHT 166
Cdd:PRK13538 85 IkteltalenLRfyqRLHGPGDDEALwEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180 190
....*....|....*....|....*....|...
gi 2316063307 167 TQALLQIIEQlHAE--GRTILAVLHDLELVGQH 197
Cdd:PRK13538 165 VARLEALLAQ-HAEqgGMVILTTHQDLPVASDK 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-192 |
7.08e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 90.09 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNAIGYLPQLSEFDRQfpISVRDLVLMGSLPH 97
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvPVQERNVGFVFQHYALFRH--MTVFDNVAFGLRVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 RGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQL 177
Cdd:cd03296 103 PRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
170
....*....|....*.
gi 2316063307 178 HAE-GRTILAVLHDLE 192
Cdd:cd03296 183 HDElHVTTVFVTHDQE 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-192 |
9.77e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 9.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 10 GYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG------SKDNAI-----GYLPQLSef 78
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-DGvpvtgpGADRGVvfqkdALLPWLN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 drqfpisVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:COG4525 93 -------VLDNVAFG-LRLRGVPKA---ERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2316063307 159 FTGIDSHTTQALLQIIEQL-HAEGRTILAVLHDLE 192
Cdd:COG4525 162 FGALDALTREQMQELLLDVwQRTGKGVFLITHSVE 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-194 |
1.15e-21 |
|
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: 88.04 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNA---------IG 70
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQwdpnelgdhVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQlsefdrqfpisvRDLVLMGSLphrgllrsihvnwhrkatdaldavsmkdfADrhiGVLSGGQLQRVLFARLLLTQA 150
Cdd:cd03246 80 YLPQ------------DDELFSGSI-----------------------------AE---NILSGGQRQRLGLARALYGNP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-194 |
1.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.56 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSG-CFH--QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS-FSLGDG-SKDNA------I 69
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDvSFHvkQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQiIIDGDLlTEENVwdirhkI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 70 GYLPQlsEFDRQF-PISVRDLVLMGsLPHRGLlrsIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLT 148
Cdd:PRK13650 84 GMVFQ--NPDNQFvGATVEDDVAFG-LENKGI---PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316063307 149 QAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV 204
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-192 |
1.64e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 88.76 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSgcFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGY---LPQLSEF 78
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLN--VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYqrpVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQFP-ISVRDLVLMGSLPhrGLlrSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDE 157
Cdd:TIGR01277 79 NNLFAhLTVRQNIGLGLHP--GL--KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 158 PFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLCSErQRTLLMVTHHLS 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-192 |
2.04e-21 |
|
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: 88.90 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKDNA----------IG 70
Cdd:cd03295 1 IEFENVTKRYGGGKKaVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG--EDIReqdpvelrrkIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLsefdrqfpisvrdlvlMGSLPHRGLLRSIHV-----NWHR-----KATDALDAVSM--KDFADRHIGVLSGGQLQ 138
Cdd:cd03295 79 YVIQQ----------------IGLFPHMTVEENIALvpkllKWPKekireRADELLALVGLdpAEFADRYPHELSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 139 RVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDID 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-194 |
2.46e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.02 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLSEFDR 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR---IGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 QFPISV-RDLVLMGSLPHRGLLrsihvnwhrkatDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:PRK09544 81 TLPLTVnRFLRLRPGTKKEDIL------------PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-211 |
2.63e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQ-LSEFD 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK---IGYFDQhQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQfpISVRDlvlmgslphrgllrsiHVNWHRKATDALDAVSM-KDF------ADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:COG0488 392 PD--KTVLD----------------ELRDGAPGGTEQEVRGYlGRFlfsgddAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLhaEGrTILAVLHDLELVGQHFPNILHLTPDGHRW 211
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-192 |
2.95e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSgcFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL-GDGSKDNAIGYLP--QLSE 77
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLT--VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPvsMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 78 FDRQFP-ISVRDLVLMGSlpHRGLlrSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:PRK10771 79 ENNLFShLTVAQNIGLGL--NPGL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLHAEGR-TILAVLHDLE 192
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLE 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-194 |
3.74e-21 |
|
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: 87.65 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCF--HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNA-----IGY 71
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLtiRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPAdlrrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFdrqFPISVRDLVLMGSLPH--RGLLRsihvnwhrkatdALDAVSMKDFADRH-------IG----VLSGGQLQ 138
Cdd:cd03245 83 VPQDVTL---FYGTLRDNITLGAPLAddERILR------------AAELAGVTDFVNKHpngldlqIGergrGLSGGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 139 RVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHD---LELV 194
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRpslLDLV 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-209 |
4.32e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLAT-----LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-----GSKDNAIG 70
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvssTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLSEFDRQFPIS-------VRDLVLmgSLPHRGLLRSihvNWHRKATDALDAVSM-KDFADRHIGVLSGGQLQRVLF 142
Cdd:PRK13643 81 PVRKKVGVVFQFPESqlfeetvLKDVAF--GPQNFGIPKE---KAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 143 ARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQhFPNILHLTPDGH 209
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVAD-YADYVYLLEKGH 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-208 |
4.33e-21 |
|
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: 85.58 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQlsefdrq 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK---IGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 fpisvrdlvlmgslphrgllrsihvnwhrkatdaldavsmkdfadrhigvLSGGQLQRVLFARLLLTQAPIILLDEPFTG 161
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316063307 162 IDSHTTQALlqiIEQLHAEGRTILAVLHDLELVGQHFPNILHLTPDG 208
Cdd:cd03221 101 LDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-204 |
7.67e-21 |
|
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: 87.08 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 15 PPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD----GSKDNAIGYLpqlsefDRQFPISVRDLV 90
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsDLRGRAIPYL------RRKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LmgsLPHRGLLRSI----------HVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:cd03292 89 L---LPDRNVYENVafalevtgvpPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 161 GIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-192 |
8.95e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 87.89 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLAT-----LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNA----- 68
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKkalddVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrdiTAKKKKklkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 ---IGYLPQLSEfdRQ-FPISVRDLVLMGslPHRGLLRSIHVnwHRKATDALDAVSM-KDFADRHIGVLSGGQLQRVLFA 143
Cdd:TIGR04521 81 rkkVGLVFQFPE--HQlFEETVYKDIAFG--PKNLGLSEEEA--EERVKEALELVGLdEEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316063307 144 RLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSME 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-192 |
1.01e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPP---LSGSFSLGDGSKDN------AIGY 71
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlpaeqrRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLsefDRQFP-ISVRDLVLMGsLPhRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:COG4136 81 LFQD---DLLFPhLSVGENLAFA-LP-PTIGRA---QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQ-IIEQLHAEGRTILAVLHDLE 192
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-192 |
1.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRS--QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL--GDGSKDNA--------- 68
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitVDGITLTAktvwdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 IGYLPQlsEFDRQF-PISVRDLVLMGsLPHRGLLRSIHVnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLL 147
Cdd:PRK13640 86 VGIVFQ--NPDNQFvGATVGDDVAFG-LENRAVPRPEMI---KIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 148 TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDID 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-189 |
1.38e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.56 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 20 LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPplSGSFSLG----DGSKDNA------IGYLPQlseFDRQFP-ISVRD 88
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGqilfNGQPRKPdqfqkcVAYVRQ---DDILLPgLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 lvlmgSLPHRGLLRSihvnwHRKATDALDA-----VSMKDFADRHIG-----VLSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:cd03234 101 -----TLTYTAILRL-----PRKSSDAIRKkrvedVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 159 FTGIDSHTTQALLQIIEQLHAEGRTILAVLH 189
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-204 |
1.65e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.19 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLP--------PLSGSFSLgDGSKDNAI--- 69
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTL-NGEPLAAIdap 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 70 ------GYLPQLSEfdRQFPISVRDLVLMGSLPH--RGLLRSIH---VNWH---RKATDALDAvsmkdfadRHIGVLSGG 135
Cdd:PRK13547 80 rlarlrAVLPQAAQ--PAFAFSAREIVLLGRYPHarRAGALTHRdgeIAWQalaLAGATALVG--------RDVTTLSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 136 QLQRVLFARLLLTQAP---------IILLDEPFTGIDSHTTQALLQIIEQLHAEGRT-ILAVLHDLELVGQHFPNILHL 204
Cdd:PRK13547 150 ELARVQFARVLAQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAML 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-209 |
1.68e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLP----PLSGSFSLG-----------DGSK 65
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGrtvqregrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 66 DNA-IGYLPQlsEFDRQFPISVRDLVLMGSLPHRGLLRSIhVNW-----HRKATDALDAVSMKDFADRHIGVLSGGQLQR 139
Cdd:PRK09984 84 SRAnTGYIFQ--QFNLVNRLSVLENVLIGALGSTPFWRTC-FSWftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316063307 140 VLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHA-EGRTILAVLHDLELVGQHFPNILHLTpDGH 209
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALR-QGH 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-192 |
2.13e-20 |
|
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: 86.24 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKD--------NAIGYLPQLSEFdrqFP-ISVRDLVLMGsLPHRGLL 101
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILL-NG-KDitnlppekRDISYVPQNYAL---FPhMTVYKNIAYG-LKKRKVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 102 RsihVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE- 180
Cdd:cd03299 103 K---KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEf 179
|
170
....*....|..
gi 2316063307 181 GRTILAVLHDLE 192
Cdd:cd03299 180 GVTVLHVTHDFE 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
27-192 |
3.31e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSG--SFSLGDGS----KDNAIGYLPQLSEFDRQfpISVRDLVLMG--SLPHR 98
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGhiRFHGTDVSrlhaRDRKVGFVFQHYALFRH--MTVFDNIAFGltVLPRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 GLLRSIHVNwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLH 178
Cdd:PRK10851 106 ERPNAAAIK--AKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLH 183
|
170
....*....|....*
gi 2316063307 179 AEGR-TILAVLHDLE 192
Cdd:PRK10851 184 EELKfTSVFVTHDQE 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-204 |
4.57e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.90 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGdgskdnaiGYLPQLSEFD 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD--------GVPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFPISVrdlvlmgslphrgLLRSIHVnwhrkatdaLDAVSMKDFADRhigvLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:cd03247 73 LSSLISV-------------LNQRPYL---------FDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316063307 160 TGIDSHTTQALLQIIEQlHAEGRTILAVLHDLELVgQHFPNILHL 204
Cdd:cd03247 127 VGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGI-EHMDKILFL 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-192 |
5.59e-20 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 84.98 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKDnaigyLPQLSEFDRQ 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--KD-----ITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 ----------FP-ISVRDLVLMGsLPHRGLLRSIHvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:cd03300 74 vntvfqnyalFPhLTVFENIAFG-LRLKKLPKAEI---KERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQE 192
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-189 |
7.13e-20 |
|
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: 83.75 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 20 LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPP--LSGS-----FSLGDGSKDNAIGYLPQlsefdrqfpisvrDLVLM 92
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEvlingRPLDKRSFRKIIGYVPQ-------------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLPHRGLLrsihvnwhrkatdaldavsmkDFAdRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:cd03213 95 PTLTVRETL---------------------MFA-AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170
....*....|....*..
gi 2316063307 173 IIEQLHAEGRTILAVLH 189
Cdd:cd03213 153 LLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-192 |
9.11e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.46 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATL-----SGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-----GSKDNAIGY 71
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFDRQFPISvrdlvlmgSLPHRGLLRSIH---VNW-------HRKATDALDAVSM-KDFADRHIGVLSGGQLQRV 140
Cdd:PRK13634 83 LRKKVGIVFQFPEH--------QLFEETVEKDICfgpMNFgvseedaKQKAREMIELVGLpEELLARSPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 141 LFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSME 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-192 |
1.01e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 82.48 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 23 CFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSkdnaigylpqlsefdrqfPISVRDlvlmgslphrgllr 102
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGK------------------EVSFAS-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 103 sihvnwhrkATDALDA-VSMkdfadrhIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEG 181
Cdd:cd03216 69 ---------PRDARRAgIAM-------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG 132
|
170
....*....|.
gi 2316063307 182 RTILAVLHDLE 192
Cdd:cd03216 133 VAVIFISHRLD 143
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
27-190 |
1.12e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEFDRQFPI-SVRDLVLMGslphrglLRSih 105
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWkKVIDNVGLG-------LKG-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 106 vNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTI 184
Cdd:PRK11247 109 -QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTV 187
|
....*.
gi 2316063307 185 LAVLHD 190
Cdd:PRK11247 188 LLVTHD 193
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-208 |
1.17e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 86.87 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 4 LQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgdgSKDNAIGYLPQLSEFDrqFP 83
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---SENANIGYYAQDHAYD--FE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 IsvrDLVLMgslphrgllrsihvNW---HRKATDALDAV-SM-------KDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:PRK15064 397 N---DLTLF--------------DWmsqWRQEGDDEQAVrGTlgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLhaEGrTILAVLHDLELVGQHFPNILHLTPDG 208
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMALEKY--EG-TLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-189 |
1.40e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 21 SGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPP---LSGSFSLgDGSKDNAiGYLPQLSEFDRQFpisvrDLvLMGSLPH 97
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLL-NGMPIDA-KEMRAISAYVQQD-----DL-FIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 R-GLLRSIHVNWHRKAT---------DALDAVSMKDFADRHIGV------LSGGQLQRVLFARLLLTQAPIILLDEPFTG 161
Cdd:TIGR00955 117 ReHLMFQAHLRMPRRVTkkekrervdEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180
....*....|....*....|....*...
gi 2316063307 162 IDSHTTQALLQIIEQLHAEGRTILAVLH 189
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-192 |
1.41e-19 |
|
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: 85.92 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 30 TAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG-----DGSKD-------NAIGYLPQLSefdRQFP-ISVRdlvlmgslp 96
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSARGiflpphrRRIGYVFQEA---RLFPhLSVR--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 hRGLLRSIHVNWHRKATDALDAVS----MKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:COG4148 96 -GNLLYGRKRAPRAERRISFDEVVellgIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180
....*....|....*....|.
gi 2316063307 173 IIEQLHAEGRT-ILAVLHDLE 192
Cdd:COG4148 175 YLERLRDELDIpILYVSHSLD 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-232 |
1.55e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.74 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSK---DN--------AIGYLPQLSEfDRQFPISVRDLVLMGS 94
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPikyDKksllevrkTVGIVFQNPD-DQLFAPTVEEDVAFGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LpHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:PRK13639 105 L-NLGLSKE---EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316063307 175 EQLHAEGRTILAVLHDLELVGQhFPNILHLTPDGHRWGEAQPilhslRQADSDTPTLR 232
Cdd:PRK13639 181 YDLNKEGITIIISTHDVDLVPV-YADKVYVMSDGKIIKEGTP-----KEVFSDIETIR 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-190 |
2.02e-19 |
|
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: 83.61 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 22 GCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPlsgsfSLGDGSKDNA-IGYLPQLSEFDrqFPISVRDLvLMGSLPHRGl 100
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKP-----DEGDIEIELDtVSYKPQYIKAD--YEGTVRDL-LSSITKDFY- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 lrsIHVNWHrkaTDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS----HTTQALLQIIEq 176
Cdd:cd03237 91 ---THPYFK---TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAE- 163
|
170
....*....|....
gi 2316063307 177 lHAEgRTILAVLHD 190
Cdd:cd03237 164 -NNE-KTAFVVEHD 175
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-195 |
3.04e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSK----------DNAIGYLPQlsefDRQ----FPI-SVRD- 88
Cdd:COG1129 276 RAGEILGIAGLVGAGRTELARALFGADPADSGEIRL-DGKPvrirsprdaiRAGIAYVPE----DRKgeglVLDlSIREn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 --LVLMGSLPHRGLLRsihvnwHRKATDALDAVsMKDF------ADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:COG1129 351 itLASLDRLSRGGLLD------RRRERALAEEY-IKRLriktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 161 GIDSHTTQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAEGKAVIVISSELpELLG 459
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-194 |
3.09e-19 |
|
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: 83.01 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--------FSLGDGSKDNA---IGYLPQlsefdrQFPI----SVRDLV 90
Cdd:cd03258 30 KGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdlTLLSGKELRKArrrIGMIFQ------HFNLlssrTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 lmgSLPHRgLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQAL 170
Cdd:cd03258 104 ---ALPLE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSI 179
|
170 180
....*....|....*....|....*
gi 2316063307 171 LQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:cd03258 180 LALLRDINRElGLTIVLITHEMEVV 204
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
26-198 |
3.41e-19 |
|
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: 82.96 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG--DGSKDNA-------IGYLPQlsefDRQ-FP-ISVRDLVLMGS 94
Cdd:TIGR03410 25 KGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgeDITKLPPheraragIAYVPQ----GREiFPrLTVEENLLTGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRSIhvnwhrkATDALDAVS-MKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQI 173
Cdd:TIGR03410 101 AALPRRSRKI-------PDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRV 173
|
170 180
....*....|....*....|....*
gi 2316063307 174 IEQLHAEGRtiLAVLhdleLVGQHF 198
Cdd:TIGR03410 174 IRRLRAEGG--MAIL----LVEQYL 192
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-221 |
4.87e-19 |
|
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: 85.48 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 14 QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDN---------AIGYLPQLSEFdrqFPI 84
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKqwdretfgkHIGYLPQDVEL---FPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 85 SV-RDLVLMGSLPHrgllrSIHVNWHRKATDALDAV-SMKDFADRHIGV----LSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:TIGR01842 407 TVaENIARFGENAD-----PEKIIEAAKLAGVHELIlRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 159 FTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQhfPNILHLTPDG--HRWGEAQPILHSL 221
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGC--VDKILVLQDGriARFGERDEVLAKL 544
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-209 |
9.03e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLSefdrQFPI-SVRDLVLmgsL 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR---VLFLPQRP----YLPLgTLREALL---Y 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 96 PHRGLLRSihvnwHRKATDALDAVSMKDFADRH------IGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:COG4178 449 PATAEAFS-----DAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 170 LLQIIEQLHAEGrTILAVLHDLELVgQHFPNILHLTPDGH 209
Cdd:COG4178 524 LYQLLREELPGT-TVISVGHRSTLA-AFHDRVLELTGDGS 561
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-189 |
9.72e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.48 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-----LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-----GSKDNAIGY 71
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFDRQFPIS------VRDLVLMGSlphrgllRSIHVNWHRKATDALDAVSM----KDFADRHIGVLSGGQLQRVL 141
Cdd:PRK13649 83 IRKKVGLVFQFPESqlfeetVLKDVAFGP-------QNFGVSQEEAEALAREKLALvgisESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316063307 142 FARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLH 189
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-196 |
1.12e-18 |
|
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: 81.33 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 15 PPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--FSLGDGSKD--------------NAIGYLpqlSEF 78
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDlaqaspreilalrrRTIGYV---SQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQFP-ISVRDLVlMGSLPHRGLLRSIHvnwHRKATDALdavsmkdfadRHIGV-----------LSGGQLQRVLFARLL 146
Cdd:COG4778 102 LRVIPrVSALDVV-AEPLLERGVDREEA---RARARELL----------ARLNLperlwdlppatFSGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREA 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-191 |
1.24e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFH--QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA--------IG 70
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNipKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfeklrkhIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLSEfdRQFPIS-VRDLVLMG----SLPHRgllrsihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARL 145
Cdd:PRK13648 87 IVFQNPD--NQFVGSiVKYDVAFGlenhAVPYD--------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316063307 146 LLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGR-TILAVLHDL 191
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDL 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-198 |
1.55e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 80.72 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQL-SEFDR 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 Q--FP-ISVRDLVLMGSLPHRGLLRSIHVnwhrkatdALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDE 157
Cdd:cd03268 81 PgfYPnLTARENLRLLARLLGIRKKRIDE--------VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 158 PFTGIDSHTTQALLQIIEQLHAEGRTILA---VLHDLELVGQHF 198
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLIsshLLSEIQKVADRI 196
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-190 |
2.99e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.04 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNAIGYLPQ 74
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 ---LsefdrqFP-ISVRDLVLMGsLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:COG3839 83 syaL------YPhMTVYENIAFP-LKLRKVPKA---EIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHD 190
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHD 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-192 |
3.44e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-----GSKDNAIG-----------YLPQLsefdr 80
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAALAagvaiiyqelhLVPEM----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 qfpiSVRDLVLMGSLPHR-GLLRSIHVNwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:PRK11288 95 ----TVAENLYLGQLPHKgGIVNRRLLN--YEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|...
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAEGRTILAVLHDLE 192
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRME 201
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-185 |
4.27e-18 |
|
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: 79.89 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDN---------AIGYLPQLSEFDRQfpISVRDlVLMGS 94
Cdd:cd03218 23 VKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrarlGIGYLPQEASIFRK--LTVEE-NILAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRSIhvnWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:cd03218 100 LEIRGLSKKE---REEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKII 176
|
170
....*....|.
gi 2316063307 175 EQLHAEGRTIL 185
Cdd:cd03218 177 KILKDRGIGVL 187
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-192 |
4.44e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL------GDGSKDNAI----G 70
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVfqneG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLsefdrqfpiSVRDLVLMGsLPHRGLLRSIHVnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:PRK11248 81 LLPWR---------NVQDNVAFG-LQLAGVEKMQRL---EIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQL-HAEGRTILAVLHDLE 192
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIE 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-196 |
6.14e-18 |
|
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: 82.10 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG------SKD---NAIGYLPQLSEFdrqFPISVRDlvlmgslph 97
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-DGadlsqwDREelgRHIGYLPQDVEL---FDGTIAE--------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 rgllrsihvNWHR-------KATDALDAVSMKDFADR-------HIG----VLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:COG4618 425 ---------NIARfgdadpeKVVAAAKLAGVHEMILRlpdgydtRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA 532
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-191 |
9.08e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKD---------NAIGYLPQ-LSEFDRqfpISVRDLVLMGSLP 96
Cdd:PRK09700 31 GEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkldhklaaqLGIGIIYQeLSVIDE---LTVLENLYIGRHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSIHVNWHR---KATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQI 173
Cdd:PRK09700 108 TKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLI 187
|
170
....*....|....*...
gi 2316063307 174 IEQLHAEGRTILAVLHDL 191
Cdd:PRK09700 188 MNQLRKEGTAIVYISHKL 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-193 |
1.43e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.07 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS-FSLGDGSKDNAIGYLPQLSEFD 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEiLFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFPISvrdlvlmgslPHRGLLRSIHVNWHRKA-----TDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIIL 154
Cdd:PRK13540 81 HRSGIN----------PYLTLRENCLYDIHFSPgavgiTELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLH-DLEL 193
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-195 |
1.57e-17 |
|
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: 77.09 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNA----------IGYLPQlsefDRQfpisvrdlvlmgs 94
Cdd:cd03215 24 RAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-DGKPVTRrsprdairagIAYVPE----DRK------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 lpHRGLL--RSIHVNwhrkatdaldaVSMKDFadrhigvLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:cd03215 86 --REGLVldLSVAEN-----------IALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180
....*....|....*....|....
gi 2316063307 173 IIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:cd03215 146 LIRELADAGKAVLLISSELdELLG 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-190 |
1.94e-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: 80.75 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 19 TLSgcFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLSEFDRQfpISVRDLVLMGslphr 98
Cdd:TIGR03719 25 SLS--FFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK---VGYLPQEPQLDPT--KTVRENVEEG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 glLRSIhvnwhRKATDALDAVSMK----------------------DFADRH---------------------IGVLSGG 135
Cdd:TIGR03719 93 --VAEI-----KDALDRFNEISAKyaepdadfdklaaeqaelqeiiDAADAWdldsqleiamdalrcppwdadVTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 136 QLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALlqiiEQ-LHAEGRTILAVLHD 190
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL----ERhLQEYPGTVVAVTHD 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
25-193 |
2.14e-17 |
|
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: 77.86 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKdnaigyLPQLSEFDRQfpiSVR-DLV--------LMGSL 95
Cdd:COG4181 36 EAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL-AGQD------LFALDEDARA---RLRaRHVgfvfqsfqLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 96 --------PhrgLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTT 167
Cdd:COG4181 106 talenvmlP---LELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATG 182
|
170 180
....*....|....*....|....*..
gi 2316063307 168 QALLQIIEQLHAE-GRTILAVLHDLEL 193
Cdd:COG4181 183 EQIIDLLFELNRErGTTLVLVTHDPAL 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-191 |
2.23e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.62 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSlGDGSKDNAI---------GYLPQLSEFD--------------RQF 82
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE-EEPSWDEVLkrfrgtelqNYFKKLYNGEikvvhkpqyvdlipKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 83 PISVRDLVLmgSLPHRGLLRSIhvnwhrkatdaLDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:PRK13409 177 KGKVRELLK--KVDERGKLDEV-----------VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*....
gi 2316063307 163 DSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:PRK13409 244 DIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-191 |
2.69e-17 |
|
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: 80.21 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSlGDGSKDNAI---------GYLPQLSEFD--------------RQF 82
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEVLkrfrgtelqDYFKKLANGEikvahkpqyvdlipKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 83 PISVRDlvLMGSLPHRGLLRSIhvnwhrkatdaLDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:COG1245 177 KGTVRE--LLEKVDERGKLDEL-----------AEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*....
gi 2316063307 163 DSHTTQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-192 |
3.41e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.10 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 11 YRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFS-LGDGSKDNA------IGYLPQLSEFDRQFp 83
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPARArlararIGVVPQFDNLDLEF- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 iSVRD-LVLMGslphrgllrsihvNWHRKATDALDAV--SMKDFA------DRHIGVLSGGQLQRVLFARLLLTQAPIIL 154
Cdd:PRK13536 130 -TVREnLLVFG-------------RYFGMSTREIEAVipSLLEFArleskaDARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLE 192
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFME 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-196 |
3.92e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPP-------LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGdgSKDNAIGYLP 73
Cdd:PRK10535 1 MTALLELKDIRRSYPSgeeqvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA--GQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 74 QLSEFDRQ---FPISVRDLVLMGSLPHRGLLRSIHVNWHRK-----ATDALDAVSMKDFADRHIGVLSGGQLQRVLFARL 145
Cdd:PRK10535 79 ALAQLRREhfgFIFQRYHLLSHLTAAQNVEVPAVYAGLERKqrllrAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2316063307 146 LLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-197 |
4.58e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRsqppLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLP----------PLSgSFSLGDGSKDNAigY 71
Cdd:COG4138 1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeillngrPLS-DWSAAELARHRA--Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQlsefdRQFPISVRDL--VLMGSLPHrgllrSIHVNWHRKATDAL-DAVSMKDFADRHIGVLSGGQLQRVLFARLLLT 148
Cdd:COG4138 74 LSQ-----QQSPPFAMPVfqYLALHQPA-----GASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 149 -------QAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQH 197
Cdd:COG4138 144 vwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRH 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-192 |
4.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNA--------- 68
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVsfsITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAenvwnlrrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 IGYLPQlsEFDRQF-PISVRDLVLMGsLPHRGLLRSIHVnwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLL 147
Cdd:PRK13642 83 IGMVFQ--NPDNQFvGATVEDDVAFG-MENQGIPREEMI---KRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 148 TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGR-TILAVLHDLE 192
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLD 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-191 |
6.41e-17 |
|
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: 76.89 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYR-SQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDG---------SKDNAIGY 71
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDGqdirevtldSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFdrqFPISVRDLVLMGSLphrgllrsihvnwhrKATD------ALDA------VSMKDFADRHIG----VLSGG 135
Cdd:cd03253 80 VPQDTVL---FNDTIGYNIRYGRP---------------DATDeevieaAKAAqihdkiMRFPDGYDTIVGerglKLSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 136 QLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-192 |
7.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGY-RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSG-----SFSLGDGSKDNAIGYL-- 72
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvlvsGIDTGDFSKLQGIRKLvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 -----PQLSEFDRqfpiSVRDLVLMGslPHRGLLRSIHVnwhRKATD-ALDAVSMKDFADRHIGVLSGGQLQRVLFARLL 146
Cdd:PRK13644 81 ivfqnPETQFVGR----TVEEDLAFG--PENLCLPPIEI---RKRVDrALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLE 192
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE 197
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-209 |
9.46e-17 |
|
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: 74.88 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 32 IIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGskdNAIGYLPQLSefdrQFPisvrdlvlmgslphRGLLRSIHVN-WHR 110
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRP----YLP--------------LGTLREQLIYpWDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 111 katdaldavsmkdfadrhigVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAegrTILAVLHD 190
Cdd:cd03223 91 --------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI---TVISVGHR 147
|
170
....*....|....*....
gi 2316063307 191 LELvGQHFPNILHLTPDGH 209
Cdd:cd03223 148 PSL-WKFHDRVLDLDGEGG 165
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-190 |
1.52e-16 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 75.37 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDNAIGYL-------PQLSEFDR-QFPISVRDLv 90
Cdd:cd03301 24 ADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlPPKDRDIAMVfqnyalyPHMTVYDNiAFGLKLRKV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 lmgslPHRGLlrsihvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQAL 170
Cdd:cd03301 103 -----PKDEI--------DERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQM 169
|
170 180
....*....|....*....|.
gi 2316063307 171 LQIIEQLHAE-GRTILAVLHD 190
Cdd:cd03301 170 RAELKRLQQRlGTTTIYVTHD 190
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-191 |
1.68e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQ---LSE 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 78 FDRQFPISVRDLVLmgsLPHRGLLRSI-----------HVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLL 146
Cdd:PRK11264 83 LRQHVGFVFQNFNL---FPHRTVLENIiegpvivkgepKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-192 |
1.69e-16 |
|
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: 77.15 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 32 IIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEFDRQ---FP-ISVRDLVLMGsLPHRGLLRSihvn 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSyalFPhMTVEENVAFG-LKMRKVPRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 108 wHRKA--TDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTI 184
Cdd:TIGR01187 76 -EIKPrvLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
....*...
gi 2316063307 185 LAVLHDLE 192
Cdd:TIGR01187 155 VFVTHDQE 162
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-192 |
2.11e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.18 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKdnaigyLPQLSEFDR 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVD------LSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 QFPISVRDLVLmgsLPHRGLLRSIHVNWHR----------KATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:PRK11607 92 PINMMFQSYAL---FPHMTVEQNIAFGLKQdklpkaeiasRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 151 PIILLDEPFTGIDSHTTQAL-LQIIEQLHAEGRTILAVLHDLE 192
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQE 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-197 |
5.00e-16 |
|
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: 74.11 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSK----DNAIGYLPQLsefdrqfpiSVRD-LVLMGSLphR 98
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVssllGLGGGFNPEL---------TGREnIYLNGRL--L 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 GLLRsihvnwhRKATDALDAVSM----KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:cd03220 113 GLSR-------KEIDEKIDEIIEfselGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180
....*....|....*....|...
gi 2316063307 175 EQLHAEGRTILAVLHDLELVGQH 197
Cdd:cd03220 186 RELLKQGKTVILVSHDPSSIKRL 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-201 |
5.81e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-----GSKDNAIGYLPQLSEFDRQFPIS------VRDLVLM 92
Cdd:PRK13646 30 FEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVRKRIGMVFQFPESqlfedtVEREIIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLPHRGLLRSIHVNWHRKATD---ALDAVSMKDFAdrhigvLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:PRK13646 110 GPKNFKMNLDEVKNYAHRLLMDlgfSRDVMSQSPFQ------MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
170 180 190
....*....|....*....|....*....|...
gi 2316063307 170 LLQIIEQLHAE-GRTILAVLHDLELVGQHFPNI 201
Cdd:PRK13646 184 VMRLLKSLQTDeNKTIILVSHDMNEVARYADEV 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-194 |
5.83e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 13 SQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaIGYLPQLSEFdrqFPISVRDLVLM 92
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS----VAYVPQVSWI---FNATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GS--LPHRgLLRSIHVNWHRKATDALDAVSMKDFADRHIGVlSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQAL 170
Cdd:PLN03232 702 GSdfESER-YWRAIDVTALQHDLDLLPGRDLTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180
....*....|....*....|....*..
gi 2316063307 171 LQIIEQLHAEGRTILAV---LHDLELV 194
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVtnqLHFLPLM 806
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
26-192 |
5.85e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.36 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDGSKDNAigylPQLSEFD-RQ-----------FP-ISVRDLVLM 92
Cdd:PRK09493 26 QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVND----PKVDERLiRQeagmvfqqfylFPhLTALENVMF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:PRK09493 101 GPLRVRGASKE---EAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180
....*....|....*....|
gi 2316063307 173 IIEQLHAEGRTILAVLHDLE 192
Cdd:PRK09493 178 VMQDLAEEGMTMVIVTHEIG 197
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-194 |
6.29e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.88 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEF--------DRQ-FPISVRDLVLMG--- 93
Cdd:PRK13636 31 KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESvgmvfqdpDNQlFSASVYQDVSFGavn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 -SLPHRGLlrsihvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:PRK13636 111 lKLPEDEV--------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMK 182
|
170 180
....*....|....*....|...
gi 2316063307 173 IIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK13636 183 LLVEMQKElGLTIIIATHDIDIV 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-194 |
9.06e-16 |
|
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: 74.07 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 14 QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG-------DGSKDNAIGYLPQLSEFDRQFPISV 86
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlyqlDRKQRRAFRRDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 87 RDLV--LMGSlPHRGLLRSIHVNWHRKATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGID 163
Cdd:TIGR02769 104 RMTVrqIIGE-PLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190
....*....|....*....|....*....|..
gi 2316063307 164 SHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAfGTAYLFITHDLRLV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-194 |
1.02e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 75.15 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 30 TAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG-----DGSKD-------NAIGYLPQLSefdRQFP-ISVRDLVLMGSLP 96
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfDSRKGiflppekRRIGYVFQEA---RLFPhLSVRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSIhvNWHRkatdALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQ 176
Cdd:TIGR02142 103 ARPSERRI--SFER----VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170
....*....|....*....
gi 2316063307 177 LHAEGRT-ILAVLHDLELV 194
Cdd:TIGR02142 177 LHAEFGIpILYVSHSLQEV 195
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-194 |
1.35e-15 |
|
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: 74.32 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPL---SGSFSLgDGsKDnaigyLPQLSEFDRQfPISVRDLVL-----MGSL- 95
Cdd:COG0444 29 RRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILF-DG-ED-----LLKLSEKELR-KIRGREIQMifqdpMTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 96 P--------------HRGLLRSihvNWHRKATDALDAVSM---KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:COG0444 101 PvmtvgdqiaeplriHGGLSKA---EARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 159 FTGIDShTTQAllQIIE---QLHAE-GRTILAVLHDLELV 194
Cdd:COG0444 178 TTALDV-TIQA--QILNllkDLQRElGLAILFITHDLGVV 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-190 |
1.42e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 19 TLSgcFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLSEFDRQFpiSVRDLVLMGSLPHR 98
Cdd:PRK11819 27 SLS--FFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIK---VGYLPQEPQLDPEK--TVRENVEEGVAEVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 GLLrsihvnwhrkatDALDAVSMK------DF-------------------------------------ADRHIGVLSGG 135
Cdd:PRK11819 100 AAL------------DRFNEIYAAyaepdaDFdalaaeqgelqeiidaadawdldsqleiamdalrcppWDAKVTKLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 136 QLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALlqiiEQ-LHAEGRTILAVLHD 190
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL----EQfLHDYPGTVVAVTHD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-191 |
1.44e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSlgdgsKDNAIGYLPQLSEFDrqFPISVRDLvlmgslphrglLRSI 104
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-----PELKISYKPQYIKPD--YDGTVEDL-----------LRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 105 ----HVNWHRkaTDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSH----TTQALLQIIEQ 176
Cdd:PRK13409 425 tddlGSSYYK--SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEE 502
|
170
....*....|....*
gi 2316063307 177 lhaEGRTILAVLHDL 191
Cdd:PRK13409 503 ---REATALVVDHDI 514
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-194 |
2.00e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-----LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--FSLGDGSKDNA------ 68
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTieWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 69 ------------------------IGYLPQLSEF---------DRQF-PISvrdlvlMGSLPHRGLlrsihvnwhRKATD 114
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrrVGVVFQFAEYqlfeqtiekDIIFgPVS------MGVSKEEAK---------KRAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 115 ALDAVSM-KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLEL 193
Cdd:PRK13651 148 YIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDN 227
|
.
gi 2316063307 194 V 194
Cdd:PRK13651 228 V 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-204 |
2.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-------GSKD-----NAIGYLPQLSEfDRQFPISVRDLVLMG 93
Cdd:PRK13641 32 EGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetGNKNlkklrKKVSLVFQFPE-AQLFENTVLKDVEFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLpHRGL----LRSIHVNWHRKATDALDAVSMKDFAdrhigvLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:PRK13641 111 PK-NFGFsedeAKEKALKWLKKVGLSEDLISKSPFE------LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190
....*....|....*....|....*....|....*
gi 2316063307 170 LLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-194 |
2.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-------GSKDNAIGYLP-QLSEFDR---------QFP--- 83
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkkNNHELITNPYSkKIKNFKElrrrvsmvfQFPeyq 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 ---ISVRDLVLMGSLPhrglLRSIHVNWHRKATDALDAVSMKD-FADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:PRK13631 129 lfkDTIEKDIMFGPVA----LGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPT 204
|
170 180 190
....*....|....*....|....*....|....*
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:PRK13631 205 AGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHV 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-192 |
3.07e-15 |
|
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: 72.11 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIGylPqlsefDRQ--------FP-ISVRDLVlmgSLP 96
Cdd:TIGR01184 10 QGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPG--P-----DRMvvfqnyslLPwLTVRENI---ALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSIHVNWHRKATDA-LDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHT----TQALL 171
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrgnlQEELM 158
|
170 180
....*....|....*....|.
gi 2316063307 172 QIIEQLHAegrTILAVLHDLE 192
Cdd:TIGR01184 159 QIWEEHRV---TVLMVTHDVD 176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-194 |
3.35e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD----GSKDNAIGYLPQLSEFD--RQFpisvRDLVLMGSL--- 95
Cdd:PRK11300 29 REQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhieGLPGHQIARMGVVRTFQhvRLF----REMTVIENLlva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 96 PHR--------GLLRSihVNWHRKATDA-------LDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:PRK11300 105 QHQqlktglfsGLLKT--PAFRRAESEAldraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190
....*....|....*....|....*....|....*
gi 2316063307 161 GIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEhNVTVLLIEHDMKLV 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-196 |
3.35e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.16 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSF--------SLGDGSK----DNAIGYLPQ----LSEFDRQFPISVrDL 89
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSAAKaelrNQKLGFIYQfhhlLPDFTALENVAM-PL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VLMGSLPHRGllrsihvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:PRK11629 113 LIGKKKPAEI---------NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|....*...
gi 2316063307 170 LLQIIEQLHA-EGRTILAVLHDLELVGQ 196
Cdd:PRK11629 184 IFQLLGELNRlQGTAFLVVTHDLQLAKR 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-207 |
3.62e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGL--LPPLSGSFSLgDGsKDnaigyLPQLSEFDR---------QFP-----ISVR 87
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILL-DG-ED-----ILELSPDERaragiflafQYPveipgVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 88 DLvLMGSLPHRGLLRSIHVNWHRKATDALDAVSM-KDFADRHIGV-LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSH 165
Cdd:COG0396 96 NF-LRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDID 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 166 TTQALLQIIEQLHAEGRTILAVlhdlelvgQHFPNIL-HLTPD 207
Cdd:COG0396 175 ALRIVAEGVNKLRSPDRGILII--------THYQRILdYIKPD 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-191 |
3.69e-15 |
|
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: 71.88 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFH--QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGskDNAIGYlpQLSEFD 79
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDipAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DG--HDVRDY--TLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFPISVRDLVLMGSLPHRGLLRSIHVNWHRKATDALDAVSMKDFADR-------HIGV----LSGGQLQRVLFARLLLT 148
Cdd:cd03251 76 RQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQRQRIAIARALLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2316063307 149 QAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRL 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-192 |
4.54e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSK----------DNAIGYLPQ---LSEfdrqfPISVRDLV 90
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DGKPvrirsprdaiALGIGMVHQhfmLVP-----NLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LMGSLPHRGLLRSIhvnwhRKATDALDAVSmKDF-----ADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSH 165
Cdd:COG3845 102 VLGLEPTKGGRLDR-----KAARARIRELS-ERYgldvdPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ 175
|
170 180
....*....|....*....|....*..
gi 2316063307 166 TTQALLQIIEQLHAEGRTILAVLHDLE 192
Cdd:COG3845 176 EADELFEILRRLAAEGKSIIFITHKLR 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-168 |
5.24e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.00 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaIGYLPQLSEFdrqFPISVRDLVLMGSL--PHRgLLRSI 104
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT----VAYVPQVSWI---FNATVRDNILFGSPfdPER-YERAI 714
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 105 HVNWHRKATDALDAVSMKDFADRhiGV-LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:PLN03130 715 DVTALQHDLDLLPGGDLTEIGER--GVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-204 |
5.73e-15 |
|
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: 71.35 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 5 QELAFGYRSQPP---LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG------------SKDNAI 69
Cdd:cd03248 15 QNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-DGkpisqyehkylhSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 70 GYLPQLsefdrqFPISVRDLVLMGslphrglLRSIHVNwhrKATDALDAVSMKDF-----------ADRHIGVLSGGQLQ 138
Cdd:cd03248 94 GQEPVL------FARSLQDNIAYG-------LQSCSFE---CVKEAAQKAHAHSFiselasgydteVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 139 RVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHaEGRTILAVLHDLELVgQHFPNILHL 204
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTV-ERADQILVL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-194 |
6.03e-15 |
|
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: 73.28 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 21 SGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFslgdgSKDNAIGYLPQLSEFDrqFPISVRDLvLMGSLPHRgl 100
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKISYKPQYISPD--YDGTVEEF-LRSANTDD-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 lrsIHVNWHRkaTDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS----HTTQALLQIIEQ 176
Cdd:COG1245 430 ---FGSSYYK--TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN 504
|
170
....*....|....*...
gi 2316063307 177 lhaEGRTILAVLHDLELV 194
Cdd:COG1245 505 ---RGKTAMVVDHDIYLI 519
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-215 |
8.85e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 8.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--FSLGDGSKDNAIGYLPQLSeF 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTllFEGEDISTLKPEIYRQQVS-Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQFPI----SVRDLVLmgsLPHrgLLRSIHVNWHRKATDaLDAVSMKD-FADRHIGVLSGGQLQRVLFARLLLTQAPII 153
Cdd:PRK10247 86 CAQTPTlfgdTVYDNLI---FPW--QIRNQQPDPAIFLDD-LERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 154 LLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELVgQHFPNILHLTPDGHRWGEAQ 215
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEI-NHADKVITLQPHAGEMQEAR 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-191 |
9.44e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 70.72 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDG---------SKDNAIGY 71
Cdd:cd03254 3 IEFENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGidirdisrkSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFdrqFPISVRDLVLMGSLphrgllrsihvnwhrKATD-----ALDAVSMKDFADR-------HIG----VLSGG 135
Cdd:cd03254 82 VLQDTFL---FSGTIMENIRLGRP---------------NATDeevieAAKEAGAHDFIMKlpngydtVLGenggNLSQG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 136 QLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRL 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
27-193 |
1.03e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEFDRQFPISVRDLVLMgSLPHRGLLRSIHV 106
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRTRLTM-VFQHFNLWSHMTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 107 -----------------NWHRKATDALDAVSMKDFADRHIGV-LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:PRK10619 110 lenvmeapiqvlglskqEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
|
170 180
....*....|....*....|....*
gi 2316063307 169 ALLQIIEQLHAEGRTILAVLHDLEL 193
Cdd:PRK10619 190 EVLRIMQQLAEEGKTMVVVTHEMGF 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-191 |
1.09e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 5 QELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---------GSKDNAIGYLPQL 75
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 SEFDRQfpISVRDlVLMGSLPHRGLLRSIHVNwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILL 155
Cdd:PRK10895 87 ASIFRR--LSVYD-NLMAVLQIRDDLSAEQRE--DRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 156 DEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-193 |
1.31e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgskdnaigylpqlSEFDRQ 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG-------------HQFDFS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 FPISVRDLVLM----GSL-------PHR--------------GLLRSIHVNwhrKATDALDAVSMKDFADRHIGVLSGGQ 136
Cdd:COG4161 70 QKPSEKAIRLLrqkvGMVfqqynlwPHLtvmenlieapckvlGLSKEQARE---KAMKLLARLRLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 137 LQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLEL 193
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEF 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-191 |
1.72e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.05 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 11 YRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGdgskdnaiGYLP--QLSEFDRQFPisvrd 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA--------GLVPwkRRKKFLRRIG----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 lVLMGS-------LPHR---GLLRSIH-------VNWHRKATDALDavsMKDFADRHIGVLSGGQLQRVLFARLLLTQAP 151
Cdd:cd03267 98 -VVFGQktqlwwdLPVIdsfYLLAAIYdlpparfKKRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 152 IILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDL 191
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYM 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-191 |
2.07e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.78 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaigyLPQLSEFD 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-------IADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFPISV---RDLVLMGSLPHRGLLRSIHVNWHrKATDALDAVSMKDFADRHIGV----------LSGGQLQRVLFARLL 146
Cdd:PRK11160 412 LRQAISVvsqRVHLFSATLRDNLLLAAPNASDE-ALIEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARAL 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316063307 147 LTQAPIILLDEPFTGIDSHTTQALLQIIEQlHAEGRTILAVLHDL 191
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRL 534
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-191 |
4.95e-14 |
|
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: 69.32 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSlGDGSKDNAIGYL----------------------PQ-LSEFDRQFP 83
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFrgselqnyftkllegdvkvivkPQyVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 ISVRDLvlMGSLPHRGLLRSIhvnwhrkatdaLDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGID 163
Cdd:cd03236 105 GKVGEL--LKKKDERGKLDEL-----------VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|....*...
gi 2316063307 164 SHTTQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-197 |
5.93e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRsqppLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPlSGSFSLGDGSKDNAI--------GYLP 73
Cdd:PRK03695 1 MQLNDVAVSTR----LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSaaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 74 QlsefdRQFPISVRDLVLMGSLpHRGLLRsiHVNWHRKATDAL-DAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPI 152
Cdd:PRK03695 76 Q-----QQTPPFAMPVFQYLTL-HQPDKT--RTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 153 I-------LLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQH 197
Cdd:PRK03695 148 InpagqllLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRH 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-191 |
6.50e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKdnAIGYLPQLSEF 78
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllGGR--SIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQ----------FPISVRDLVLMGSLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIG----VLSGGQLQRVLFAR 144
Cdd:PRK14271 100 RRRvgmlfqrpnpFPMSIMDNVLAGVRAHKLVPRK---EFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNL 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-191 |
8.16e-14 |
|
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: 70.13 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 9 FGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGskdNAIGYLpQLSEFDRQFPISVRD 88
Cdd:TIGR02203 340 YPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL-DG---HDLADY-TLASLRRQVALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 LVLM-GSLPHrgllrsiHVNWHRKAT-------DALDAVSMKDFADR-------HIGV----LSGGQLQRVLFARLLLTQ 149
Cdd:TIGR02203 415 VVLFnDTIAN-------NIAYGRTEQadraeieRALAAAYAQDFVDKlplgldtPIGEngvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316063307 150 APIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRL 528
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-194 |
8.48e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSG---CFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKdnaigylpqLSEF 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGltfTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVP---------LVQY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 D-----RQFPISVRDLVLMGslphRGLLRSIHVNWHRKATDALDAVSMKDFADRHIG---------------VLSGGQLQ 138
Cdd:TIGR00958 549 DhhylhRQVALVGQEPVLFS----GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMefpngydtevgekgsQLSGGQKQ 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 139 RVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQlhaEGRTILAVLHDLELV 194
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTV 677
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
26-190 |
9.96e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.36 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS-FSLGDGSKDNAIGylpqlsefDRQFPISVRDLVLmgsLPHRGL---- 100
Cdd:PRK11432 31 QGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQiFIDGEDVTHRSIQ--------QRDICMVFQSYAL---FPHMSLgenv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 ---LRSIHVNWHRKAT---DALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:PRK11432 100 gygLKMLGVPKEERKQrvkEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170
....*....|....*..
gi 2316063307 175 EQLHAE-GRTILAVLHD 190
Cdd:PRK11432 180 RELQQQfNITSLYVTHD 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-194 |
1.00e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS----------FSLGDGskdnaigylpqlseFDRQFpiSVRDLV-LM 92
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngrvsalLELGAG--------------FHPEL--TGRENIyLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLphRGLlrsihvnwHRKATDA-LDAV----SMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPF-TGiDSHT 166
Cdd:COG1134 113 GRL--LGL--------SRKEIDEkFDEIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAF 181
|
170 180
....*....|....*....|....*...
gi 2316063307 167 TQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:COG1134 182 QKKCLARIRELRESGRTVIFVSHSMGAV 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-194 |
1.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.88 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP-----LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLS 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 77 EFDR------QFP------ISVRDLVLMGSLpHRGLLRSihvNWHRKATDALDAVSM-KDFADRHIGVLSGGQLQRVLFA 143
Cdd:PRK13645 87 RLRKeiglvfQFPeyqlfqETIEKDIAFGPV-NLGENKQ---EAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 144 RLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQV 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-192 |
1.16e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL-GDGSKDNA------IGYLPQLSEFDRQFPISVRDLVL-----MGS 94
Cdd:PRK13537 33 GECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRArharqrVGVVPQFDNLDPDFTVRENLLVFgryfgLSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRSIhvnwhrkatdaLDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:PRK13537 113 AAARALVPPL-----------LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL 181
|
170
....*....|....*...
gi 2316063307 175 EQLHAEGRTILAVLHDLE 192
Cdd:PRK13537 182 RSLLARGKTILLTTHFME 199
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-196 |
1.22e-13 |
|
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: 69.77 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY-RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDN--------AIGYL 72
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidrhtlrqFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSEFdrqFPISVRDLVLMGSLPHRGllrsihvnwHRKATDALDAVSMKDFADR-----------HIGVLSGGQLQRVL 141
Cdd:TIGR01193 554 PQEPYI---FSGSILENLLLGAKENVS---------QDEIWAACEIAEIKDDIENmplgyqtelseEGSSISGGQKQRIA 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 142 FARLLLTQAPIILLDEPFTGIDSHTTQallQIIEQL-HAEGRTILAVLHDLELVGQ 196
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEK---KIVNNLlNLQDKTIIFVAHRLSVAKQ 674
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-213 |
1.22e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.59 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FH--QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgskdNAIGYLPqlsefDRQFPISVRDLVLMGSLPHRGLL 101
Cdd:PRK10908 23 FHmrPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG----HDITRLK-----NREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 102 RSIHVN--------------WHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTT 167
Cdd:PRK10908 94 RTVYDNvaipliiagasgddIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 168 QALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHLTpDGHRWGE 213
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS-DGHLHGG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-194 |
1.40e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLaGLLPPLSGSFSLgdgskDNAIGYLPQ------- 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRV-----EGRVEFFNQniyerrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 75 -LSEFDRQ----------FPISVRDLVLMGSLPhrgllrsihVNWHRK------ATDALDAVSMKDFADRHIGV----LS 133
Cdd:PRK14258 82 nLNRLRRQvsmvhpkpnlFPMSVYDNVAYGVKI---------VGWRPKleiddiVESALKDADLWDEIKHKIHKsaldLS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 134 GGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGR-TILAVLHDLELV 194
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQV 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-191 |
1.61e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDGskDNaigyLPQLSefdR 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDG--EN----IPAMS---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 QFPISVRDLVLM----GSL------------PHRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFAR 144
Cdd:PRK11831 77 SRLYTVRKRMSMlfqsGALftdmnvfdnvayPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLQIIEQL-HAEGRTILAVLHDL 191
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDV 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-193 |
1.74e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSG-------SFSLGDGSKDNAIGYLPQ-----LSEFDRQFPISVRDLVLMG 93
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlniagnHFDFSKTPSDKAIRELRRnvgmvFQQYNLWPHLTVQQNLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPHRGLLRSIHvnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQI 173
Cdd:PRK11124 107 PCRVLGLSKDQA---LARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSI 183
|
170 180
....*....|....*....|
gi 2316063307 174 IEQLHAEGRTILAVLHDLEL 193
Cdd:PRK11124 184 IRELAETGITQVIVTHEVEV 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-194 |
2.00e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSF------------SLGDGSKDnaIGYLPQLSEFdRQFPISVRDLVLMGs 94
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvKLSDIRKK--VGLVFQYPEY-QLFEETIEKDIAFG- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRSihvNWHRKATDALDAVSMK--DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:PRK13637 109 PINLGLSEE---EIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180
....*....|....*....|...
gi 2316063307 173 IIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK13637 186 KIKELHKEyNMTIILVSHSMEDV 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-222 |
2.25e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgdgsKDNAIGYL--PQLSEFDR------QFPIS-------VRDL 89
Cdd:PRK10419 36 KSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW----RGEPLAKLnrAQRKAFRRdiqmvfQDSISavnprktVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VlmgSLPHRGLLRSIHVNWHRKATDALDAVSMKD-FADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:PRK10419 112 I---REPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 169 ALLQIIEQLHAEGRT-ILAVLHDLELVgQHFPNILhLTPDGHRWGEAQPILHSLR 222
Cdd:PRK10419 189 GVIRLLKKLQQQFGTaCLFITHDLRLV-ERFCQRV-MVMDNGQIVETQPVGDKLT 241
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-194 |
2.65e-13 |
|
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: 66.74 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP--LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDGSK----DNA-----IG 70
Cdd:cd03252 1 ITFEHVRFRYKPDGPviLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHDlalaDPAwlrrqVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLSE-FDRqfpiSVRDLVLMGSlPHRGLLRSIHVnwhRKATDALDAVS-MKDFADRHIGV----LSGGQLQRVLFAR 144
Cdd:cd03252 80 VVLQENVlFNR----SIRDNIALAD-PGMSMERVIEA---AKLAGAHDFISeLPEGYDTIVGEqgagLSGGQRQRIAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAeGRTILAVLHDLELV 194
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-194 |
3.00e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.80 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDnaigyLPQLSEfdrqfpisvRDLvlmgslphRGLLRSI- 104
Cdd:COG1135 30 KGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV-DG-VD-----LTALSE---------REL--------RAARRKIg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 105 ----HVN-------------------WHRKATDA-----LDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:COG1135 86 mifqHFNllssrtvaenvalpleiagVPKAEIRKrvaelLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVV 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-175 |
3.50e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.04 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQlsefdrqfpisVRDlvlmgSL-PHRGLLRSI 104
Cdd:TIGR03719 347 PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---LAYVDQ-----------SRD-----ALdPNKTVWEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 105 hvnwhrkaTDALDAVSMKDF---------------AD--RHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTT 167
Cdd:TIGR03719 408 --------SGGLDIIKLGKReipsrayvgrfnfkgSDqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETL 479
|
....*...
gi 2316063307 168 QALLQIIE 175
Cdd:TIGR03719 480 RALEEALL 487
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-192 |
4.16e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 20 LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPpLSGSF--------SLGDGSKDNAIGYL---PQLsefdrqFPISVRD 88
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLkingielrELDPESWRKHLSWVgqnPQL------PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 LVLMGslphrgllrsihvnwHRKATD-----ALDAVSMKDFADRH-------IG----VLSGGQLQRVLFARLLLTQAPI 152
Cdd:PRK11174 442 NVLLG---------------NPDASDeqlqqALENAWVSEFLPLLpqgldtpIGdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLE 192
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLE 545
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-192 |
5.11e-13 |
|
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: 65.98 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPPLAtLSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIGylpqLSEF 78
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV-LKNIsfsIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDISKIG----LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQFPISVRDLVLMgslphRGLLRSiHVNWHRKATD-----ALDAVSMKDFADRHIG-----------VLSGGQLQRVLF 142
Cdd:cd03244 77 RSRISIIPQDPVLF-----SGTIRS-NLDPFGEYSDeelwqALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2316063307 143 ARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQlHAEGRTILAVLHDLE 192
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLD 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-185 |
5.94e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA-----IGYLPQL 75
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrsrfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 sefdrqfPISVRDLVLMGSLPHRGLLRSIHVnwHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILL 155
Cdd:PRK13543 91 -------PGLKADLSTLENLHFLCGLHGRRA--KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 156 DEPFTGIDSHTTQALLQIIE-QLHAEGRTIL 185
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISaHLRGGGAALV 192
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-191 |
7.32e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 65.98 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD---GSKDNAIGylpQLSEFDRQFPISVRDLVLM-----GSLP 96
Cdd:COG4598 32 RKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeiRLKPDRDG---ELVPADRRQLQRIRTRLGMvfqsfNLWS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSI-----HVNwHRKATDA-------LDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:COG4598 109 HMTVLENVieapvHVL-GRPKAEAieraealLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
170 180
....*....|....*....|....*..
gi 2316063307 165 HTTQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:COG4598 188 ELVGEVLKVMRDLAEEGRTMLVVTHEM 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-192 |
1.26e-12 |
|
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: 66.96 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAI-------GY 71
Cdd:TIGR01257 1937 ILRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIsdvhqnmGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 72 LPQLSEFDRqfpisvrdlvLMGSLPHRGL---LRSIHVNWHRKATD-ALDAVSMKDFADRHIGVLSGGQLQRVLFARLLL 147
Cdd:TIGR01257 2017 CPQFDAIDD----------LLTGREHLYLyarLRGVPAEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316063307 148 TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLE 192
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2131
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-192 |
1.58e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 64.66 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 15 PPLATLSGC---FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSG------------SFSLGDGSKDNAIGYLPQLSEFd 79
Cdd:cd03290 12 SGLATLSNInirIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnknesepSFEATRSRNRYSVAYAAQKPWL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 rqFPISVRDLVLMGSlphrgllrSIHVNWHRKATDA------LDAVSMKD---FADRHIGvLSGGQLQRVLFARLLLTQA 150
Cdd:cd03290 91 --LNATVEENITFGS--------PFNKQRYKAVTDAcslqpdIDLLPFGDqteIGERGIN-LSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQ--IIEQLHAEGRTILAVLHDLE 192
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
27-192 |
1.61e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.74 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDnaigyLPQLSEFDRQ----------FP-ISVRDLVLMGsl 95
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML-DG-QD-----ITHVPAENRHvntvfqsyalFPhMTVFENVAFG-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 96 phrglLRSIHVNWH---RKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:PRK09452 111 -----LRMQKTPAAeitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQN 185
|
170 180
....*....|....*....|.
gi 2316063307 173 IIEQLHAE-GRTILAVLHDLE 192
Cdd:PRK09452 186 ELKALQRKlGITFVFVTHDQE 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-195 |
1.66e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSK----------DNAIGYLpqlSEfDRQ-----FPISVRDL 89
Cdd:PRK10762 276 RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL-DGHEvvtrspqdglANGIVYI---SE-DRKrdglvLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VLMGSLPH--RGLLRSIHVNWHRKATDALDAVSMKD-FADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHT 166
Cdd:PRK10762 351 MSLTALRYfsRAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 167 TQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:PRK10762 431 KKEIYQLINQFKAEGLSIILVSSEMpEVLG 460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-200 |
1.72e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQelaFGyrSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQlsefDrQ 81
Cdd:PRK15064 7 ITMQ---FG--AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNER---LGKLRQ----D-Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 FP---ISVRDLVLMGslpHRGLLRsihVNWHRKATDALDAVSMKD----------FA----------------------D 126
Cdd:PRK15064 74 FAfeeFTVLDTVIMG---HTELWE---VKQERDRIYALPEMSEEDgmkvadlevkFAemdgytaearagelllgvgipeE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316063307 127 RHIGVLS----GGQLqRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAegrTILAVLHDlelvgQHFPN 200
Cdd:PRK15064 148 QHYGLMSevapGWKL-RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS---TMIIISHD-----RHFLN 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-208 |
2.58e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 32 IIGANGSGKSTLLKTLAGLLPP-LSGSFSL-----GDGS-----KDNaIGYLPQLSEFDRQFPISVRDLVLMGSLPHRGL 100
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGDHPQgYSNDLTLfgrrrGSGEtiwdiKKH-IGYVSSSLHLDYRVSTSVRNVILSGFFDSIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 LRSIHVNWHRKATDALDAVSM-KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHA 179
Cdd:PRK10938 370 YQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIS 449
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 180 EGRT-ILAVLHDLELVGQHFPNILHLTPDG 208
Cdd:PRK10938 450 EGETqLLFVSHHAEDAPACITHRLEFVPDG 479
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-165 |
2.64e-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: 65.74 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 12 RSQPP-LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSkdnaIGYLPQLSEFDRQfpiSVRDLV 90
Cdd:TIGR00957 648 RDLPPtLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KGS----VAYVPQQAWIQND---SLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LMGslphrgllRSIHVNWHRKATDA---LDAVSMKDFADR-HIGV----LSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:TIGR00957 720 LFG--------KALNEKYYQQVLEAcalLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
...
gi 2316063307 163 DSH 165
Cdd:TIGR00957 792 DAH 794
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-185 |
3.55e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKD-----------NAIGYLPQ-LSEFdRQfpISVRDlVLM 92
Cdd:COG1137 27 NQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG--EDithlpmhkrarLGIGYLPQeASIF-RK--LTVED-NIL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 GSLPHRGLLRSihvNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:COG1137 101 AVLELRKLSKK---EREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQK 177
|
170
....*....|...
gi 2316063307 173 IIEQLHAEGRTIL 185
Cdd:COG1137 178 IIRHLKERGIGVL 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-192 |
4.49e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.64 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTL--AGLLPP---LSGSFSLgdgsKDNAIgYLPQL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVY----NGHNI-YSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 76 SEFDRQ------------FPISVRDLVLMGslphrglLRSIHVnwhrKATDALDAV------------SMKD-FADRHIG 130
Cdd:PRK14239 80 DTVDLRkeigmvfqqpnpFPMSIYENVVYG-------LRLKGI----KDKQVLDEAvekslkgasiwdEVKDrLHDSALG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 131 vLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQallQIIEQLHA--EGRTILAVLHDLE 192
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG---KIEETLLGlkDDYTMLLVTRSMQ 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-191 |
4.56e-12 |
|
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: 63.33 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP---LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNA---------I 69
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL-DGVDIRDlnlrwlrsqI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 70 GYL---PQLsefdrqFPISVRDLVLMGSLPhrgllrsihvnwhRKATDALDA----------VSMKDFADRHIG----VL 132
Cdd:cd03249 80 GLVsqePVL------FDGTIAENIRYGKPD-------------ATDEEVEEAakkanihdfiMSLPDGYDTLVGergsQL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 133 SGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRL 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-188 |
5.32e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 23 CFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSlgdgskdnaigylpqlSEFDRQFPISVRDLVLMgslphrgllr 102
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ----------------SQFSHITRLSFEQLQKL---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 103 sIHVNWHRKATDAL----------------DAVS-------------MKDFADRHIGVLSGGQLQRVLFARLLLTQAPII 153
Cdd:PRK10938 79 -VSDEWQRNNTDMLspgeddtgrttaeiiqDEVKdparceqlaqqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2316063307 154 LLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVL 188
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSGITLVLVL 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-189 |
5.71e-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: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLL--------------PPLSGSFSlgdgskdNAIGYLPQLsefDRQF 82
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgvitggdrlvngRPLDSSFQ-------RSIGYVQQQ---DLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 83 PIS-VRDlvlmgSLPHRGLLR-SIHVNWHRK---ATDALDAVSMKDFADRHIGV----LSGGQLQRVLFA-RLLLTQAPI 152
Cdd:TIGR00956 849 PTStVRE-----SLRFSAYLRqPKSVSKSEKmeyVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGvELVAKPKLL 923
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 153 ILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLH 189
Cdd:TIGR00956 924 LFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-194 |
7.28e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.67 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDGsKDnaigyLPQLSEfdrqfpisvRDLVL----MGSL-PHRGL 100
Cdd:PRK11153 30 AGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDG-QD-----LTALSE---------KELRKarrqIGMIfQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 LRSIHV-----------NWHRKATDA-----LDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:PRK11153 94 LSSRTVfdnvalplelaGTPKAEIKArvtelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 165 HTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK11153 174 ATTRSILELLKDINRElGLTIVLITHEMDVV 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-192 |
8.98e-12 |
|
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: 64.26 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 14 QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgdGSKD---------NAIGYLPQLSEFDRQFPI 84
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV--GGKDietnldavrQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 85 SVRDLV---LMG------SLPHRGLLRSIHVNwHRKATDALDavsmkdfadrhigvLSGGQLQRVLFARLLLTQAPIILL 155
Cdd:TIGR01257 1021 AEHILFyaqLKGrsweeaQLEMEAMLEDTGLH-HKRNEEAQD--------------LSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 156 DEPFTGIDSHTTQALLQIIEQlHAEGRTILAVLHDLE 192
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMD 1121
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-191 |
1.06e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKDNAIGYLPQLSEFDR------------QFP--------- 83
Cdd:PRK11701 30 YPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM--RDGQLRDLYALSEAERrrllrtewgfvhQHPrdglrmqvs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 ----ISVRdlvLMGS-LPHRGLLRSIHVNWHRKATDALDAVsmkdfaDRHIGVLSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:PRK11701 108 aggnIGER---LMAVgARHYGDIRATAGDWLERVEIDAARI------DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
170 180 190
....*....|....*....|....*....|....
gi 2316063307 159 FTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDL 191
Cdd:PRK11701 179 TGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDL 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-170 |
1.09e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 32 IIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQlsefdrqfpisVRDlvlmgSL-PHRGLLRSIhvnwhr 110
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK---LAYVDQ-----------SRD-----ALdPNKTVWEEI------ 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 111 kaTDALDAVSMKDF---------------AD--RHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQAL 170
Cdd:PRK11819 410 --SGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-191 |
1.71e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.98 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGL--LPP---LSGSFSLGD----GSKDNA------IGYLPQLSefdRQFPISVRD 88
Cdd:COG1117 34 IPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGediyDPDVDVvelrrrVGMVFQKP---NPFPKSIYD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 LVLMG----SLPHRGLLRSIhVNWH-RKAtdAL-DAVsmKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:COG1117 111 NVAYGlrlhGIKSKSELDEI-VEESlRKA--ALwDEV--KDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSAL 185
|
170 180
....*....|....*....|....*....
gi 2316063307 163 DSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:COG1117 186 DPISTAKIEELILEL-KKDYTIVIVTHNM 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-192 |
2.10e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGdgskdnaiGYLP--QLSEFDRQfpISV----R-----DLVLMG 93
Cdd:COG4586 46 EPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL--------GYVPfkRRKEFARR--IGVvfgqRsqlwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPhrgLLRSIH---VNWHRKATDALDAV-SMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQA 169
Cdd:COG4586 116 SFR---LLKAIYripDAEYKKRLDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180
....*....|....*....|....
gi 2316063307 170 LLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:COG4586 193 IREFLKEYNRErGTTILLTSHDMD 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-209 |
2.51e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAG--LLPPLSGSFSLgDGSKDNA-----IGYLPQLsefDRQFPIS-VRD 88
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILI-NGRPLDKnfqrsTGYVEQQ---DVHSPNLtVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 lvlmgSLPHRGLLRSIHVNWHRKATdaldavsmkdfadrhIGVLsggqlqrvlfarlLLTQAPIILLDEPFTGIDSHTTQ 168
Cdd:cd03232 99 -----ALRFSALLRGLSVEQRKRLT---------------IGVE-------------LAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316063307 169 ALLQIIEQLHAEGRTILAVLHD-LELVGQHFPNILHLTPDGH 209
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIHQpSASIFEKFDRLLLLKRGGK 187
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-188 |
3.21e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.35 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 20 LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPP---LSGSFSLGDGSKDNAIGYLPQ----LSEFDRQFP-ISVRDLvl 91
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKYPGeiiyVSEEDVHFPtLTVRET-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 92 mgslphrgllrsihvnwhrkatdaLD-AVSMKdfADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQAL 170
Cdd:cd03233 104 ------------------------LDfALRCK--GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170
....*....|....*....
gi 2316063307 171 LQIIEQL-HAEGRTILAVL 188
Cdd:cd03233 158 LKCIRTMaDVLKTTTFVSL 176
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-209 |
3.60e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 60.23 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLlpPlsgSFSLGDGS---KDNAIGYLPqlsefdrqfpisVRDLVLMGslphrgl 100
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGH--P---KYEVTEGEilfKGEDITDLP------------PEERARLG------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 lrsIHVNWHRKAtdALDAVSMKDFAdRHIGV-LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHA 179
Cdd:cd03217 79 ---IFLAFQYPP--EIPGVKNADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE 152
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 180 EGRTILAVLHDLELVGQHFPNILHLTPDGH 209
Cdd:cd03217 153 EGKSVLIITHYQRLLDYIKPDRVHVLYDGR 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-187 |
4.55e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKD-----------NAI 69
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG--KDitdwqtakimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 70 GYLPqlsEFDRQFP-ISVRDLVLMGSL-------PHR-----GLLRSIHVNWHRKAtdaldavsmkdfadrhiGVLSGGQ 136
Cdd:PRK11614 83 AIVP---EGRRVFSrMTVEENLAMGGFfaerdqfQERikwvyELFPRLHERRIQRA-----------------GTMSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2316063307 137 LQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAV 187
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-194 |
6.82e-11 |
|
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: 61.38 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPplSGSFS---LGDGSKDNA----------IGYLPQlsEFDRQFPISVRDLVLMG 93
Cdd:TIGR02633 27 GECVGLCGENGAGKSTLMKILSGVYP--HGTWDgeiYWSGSPLKAsnirdteragIVIIHQ--ELTLVPELSVAENIFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 S-LPHRGLLRSIHVNWHRkATDALDAVSMKDFAD-RHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALL 171
Cdd:TIGR02633 103 NeITLPGGRMAYNAMYLR-AKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
170 180
....*....|....*....|...
gi 2316063307 172 QIIEQLHAEGRTILAVLHDLELV 194
Cdd:TIGR02633 182 DIIRDLKAHGVACVYISHKLNEV 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-192 |
7.07e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDGSkDNAIGYLPQLSEFDRQ-FPISVRDLVLMgslPHRGLLRSI 104
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGV-DIAKISDAELREVRRKkIAMVFQSFALM---PHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 105 HVNW----------HRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:PRK10070 128 AFGMelaginaeerREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170
....*....|....*....
gi 2316063307 175 EQLHAE-GRTILAVLHDLE 192
Cdd:PRK10070 208 VKLQAKhQRTIVFISHDLD 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-194 |
7.52e-11 |
|
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: 61.36 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGS--FSLGD-------------GSKDNAIGYLPQlsEFDRqfpisvrdlv 90
Cdd:TIGR03269 309 EGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewvdmtkpgpdgrGRAKRYIGILHQ--EYDL---------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 lmgsLPHRGLL----RSIHVNW-----HRKATDALDAVSM-----KDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:TIGR03269 377 ----YPHRTVLdnltEAIGLELpdelaRMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFV 491
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-196 |
8.84e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDG-------SKDNAIG-YL-PQLSEFdrqFP-ISVRDLVLMGS 94
Cdd:PRK15439 35 HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpAKAHQLGiYLvPQEPLL---FPnLSVKENILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLR---------SIHVNWHRKAtdaldavSMKDFADRhigvlsggqlQRVLFARLLLTQAPIILLDEPFTGIDSH 165
Cdd:PRK15439 112 PKRQASMQkmkqllaalGCQLDLDSSA-------GSLEVADR----------QIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 166 TTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQ 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
24-209 |
9.63e-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: 59.16 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGsLTAIIGANGSGKSTLLK----TLAGLLPPlsgsFSLGDGSKDNAIGYLPQLSEFDRQFPISVRDLVLmgslphrg 99
Cdd:cd03240 20 FFSP-LTLIVGQNGAGKTTIIEalkyALTGELPP----NSKGGAHDPKLIREGEVRAQVKLAFENANGKKYT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 100 LLRSIHVnwhrkatdaLDAV------SMKDFADRHIGVLSGGQlqRVLFA---RLLLTQA-----PIILLDEPFTGIDS- 164
Cdd:cd03240 87 ITRSLAI---------LENVifchqgESNWPLLDMRGRCSGGE--KVLASliiRLALAETfgsncGILALDEPTTNLDEe 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 165 HTTQALLQIIE-QLHAEGRTILAVLHDLELVgQHFPNILHLTPDGH 209
Cdd:cd03240 156 NIEESLAEIIEeRKSQKNFQLIVITHDEELV-DAADHIYRVEKDGR 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-194 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYR-SQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFsLGDG---SKDNA------IG 70
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGepiTKENIrevrkfVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 71 YLPQLSEfDRQFPISVRDLVLMGslPHRGLLRSIHVNwHRkATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQA 150
Cdd:PRK13652 82 LVFQNPD-DQIFSPTVEQDIAFG--PINLGLDEETVA-HR-VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2316063307 151 PIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLV 201
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-192 |
1.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.10 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGY------RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG--DGSKDNAIGYL 72
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 73 PQLSEFDRQFP-------ISVRDLVL----MGSLPHRglLRSihvnwhrKATDALDAVSMKDFADRHIGVLSGGQLQRVL 141
Cdd:PRK13633 84 RNKAGMVFQNPdnqivatIVEEDVAFgpenLGIPPEE--IRE-------RVDESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 142 FARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLE 192
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYME 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-194 |
2.08e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPplSGSFS---LGDGS-------KDN-----AIGY-----LPQLSefdrqfpisV 86
Cdd:PRK13549 31 GEIVSLCGENGAGKSTLMKVLSGVYP--HGTYEgeiIFEGEelqasniRDTeragiAIIHqelalVKELS---------V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 87 RDLVLMGSLPHRGLLrsihVNW---HRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGID 163
Cdd:PRK13549 100 LENIFLGNEITPGGI----MDYdamYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 164 SHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:PRK13549 176 ESETAVLLDIIRDLKAHGIACIYISHKLNEV 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-202 |
2.50e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLP--PLSGSFSLGDGskdnaigylpqlsEFDRQFPIsvrdlvlmgsLPHRGLLRS 103
Cdd:COG2401 55 PGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDN-------------QFGREASL----------IDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 104 IHVnwhrkATDAL------DAVSMKdfadRHIGVLSGGQLQRVLFARLLLTQAPIILLDEpFT-GIDSHTTQALLQIIEQ 176
Cdd:COG2401 112 FKD-----AVELLnavglsDAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCsHLDRQTAKRVARNLQK 181
|
170 180
....*....|....*....|....*..
gi 2316063307 177 LHAE-GRTILAVLHDLELVGQHFPNIL 202
Cdd:COG2401 182 LARRaGITLVVATHHYDVIDDLQPDLL 208
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-194 |
3.37e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.81 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRSQPP--LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIGylpqLSEFD 79
Cdd:cd03369 7 IEVENLSVRYAPDLPpvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIP----LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFPISVRDLVLMGslphrGLLRSiHVNWHRKATDA--LDAVSMKDFADRhigvLSGGQLQRVLFARLLLTQAPIILLDE 157
Cdd:cd03369 82 SSLTIIPQDPTLFS-----GTIRS-NLDPFDEYSDEeiYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 158 PFTGIDSHTTQALLQIIEQLHAeGRTILAVLHDLELV 194
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-195 |
4.46e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 14 QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDN-----AIGYLPQLSEFDR-------Q 81
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneAINHGFALVTEERrstgiyaY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 82 FPISVRDLV--LMGSLPHRGLLRSIhvnwhRKATDA---LDAVSMKDFADR-HIGVLSGGQLQRVLFARLLLTQAPIILL 155
Cdd:PRK10982 341 LDIGFNSLIsnIRNYKNKVGLLDNS-----RMKSDTqwvIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2316063307 156 DEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLG 456
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-189 |
4.85e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSefdrqfPISVRDLVLM-----GSLPH-------- 97
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVD------PIEVRREVGMvfqypNPFPHltiydnva 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 -----RGLLRSIH-----VNWHRKATDALDAVsmKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTT 167
Cdd:PRK14267 108 igvklNGLVKSKKelderVEWALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180
....*....|....*....|..
gi 2316063307 168 QALLQIIEQLHAEgRTILAVLH 189
Cdd:PRK14267 186 AKIEELLFELKKE-YTIVLVTH 206
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-191 |
6.44e-10 |
|
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: 58.68 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG---------SKDNAIGYLPQlsefdrqfpisvrDLVLMGSlph 97
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-DGqdirdvtqaSLRAAIGIVPQ-------------DTVLFND--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 rgllrSIHVN-----WHrkATD-----ALDAVSMKDFAD------------RhiGV-LSGGQLQRVLFARLLLTQAPIIL 154
Cdd:COG5265 447 -----TIAYNiaygrPD--ASEeeveaAARAAQIHDFIEslpdgydtrvgeR--GLkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRL 553
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-194 |
7.43e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY-RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGskdnaigylpqlsefdr 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DG----------------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 qfpISVRDLVLmGSLPHR--------GLL-RSIHVNWH---RKATD-----ALDAVSMKDFADR-------HIG----VL 132
Cdd:PRK13657 397 ---TDIRTVTR-ASLRRNiavvfqdaGLFnRSIEDNIRvgrPDATDeemraAAERAQAHDFIERkpdgydtVVGergrQL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 133 SGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDLELV 194
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTV 533
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-204 |
7.46e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.96 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 30 TAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD------GSKDN------AIGYLPQLSefdRQFP-ISVRdlvlmGSLp 96
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGIClppekrRIGYVFQDA---RLFPhYKVR-----GNL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSIHVNWhrkaTDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQ 176
Cdd:PRK11144 98 RYGMAKSMVAQF----DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180
....*....|....*....|....*....
gi 2316063307 177 LHAEGRT-ILAVLHDLElvgqhfpNILHL 204
Cdd:PRK11144 174 LAREINIpILYVSHSLD-------EILRL 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-194 |
7.74e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYlpqlseFDRqfpisvrdlvlmgslphrgllrsihvnwHR 110
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLE---VAY------FDQ----------------------------HR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 111 KATDALDAVsMKDFAD-----------RHI------------------GVLSGGQLQRVLFARLLLTQAPIILLDEPFTG 161
Cdd:PRK11147 392 AELDPEKTV-MDNLAEgkqevmvngrpRHVlgylqdflfhpkramtpvKALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190
....*....|....*....|....*....|....
gi 2316063307 162 IDSHTtqalLQIIEQLHAEGR-TILAVLHDLELV 194
Cdd:PRK11147 471 LDVET----LELLEELLDSYQgTVLLVSHDRQFV 500
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-191 |
9.25e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFS-LG-----DGSKDN---AIGYLPQlsEFDRQFPISVRDLVLMGSLPH 97
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGkevtfNGPKSSqeaGIGIIHQ--ELNLIPQLTIAENIFLGREFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 RGLLRsihVNW---HRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQII 174
Cdd:PRK10762 108 NRFGR---IDWkkmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVI 184
|
170
....*....|....*..
gi 2316063307 175 EQLHAEGRTILAVLHDL 191
Cdd:PRK10762 185 RELKSQGRGIVYISHRL 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-189 |
1.08e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 28 SLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEFDR------QFP-----ISVRDLVLMGSLP 96
Cdd:PRK14247 30 TITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIELRRrvqmvfQIPnpipnLSIFENVALGLKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRgLLRS-----IHVNWHRKATDALDAVsmKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALL 171
Cdd:PRK14247 110 NR-LVKSkkelqERVRWALEKAQLWDEV--KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIE 186
|
170
....*....|....*...
gi 2316063307 172 QIIEQLHAEgRTILAVLH 189
Cdd:PRK14247 187 SLFLELKKD-MTIVLVTH 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-192 |
1.13e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNA---------IGYLPQlsefDRQ-------FpiSVRD 88
Cdd:COG3845 282 RAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsprerrrlgVAYIPE----DRLgrglvpdM--SVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 LVLMGSLPHRGLLRSIHVNWHRKATDALDAvsMKDF------ADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:COG3845 356 NLILGRYRRPPFSRGGFLDRKAIRAFAEEL--IEEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGL 433
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 163 DSHTTQALLQIIEQLHAEGRTILAVLHDLE 192
Cdd:COG3845 434 DVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-192 |
1.24e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGS---------FSLGDGSKDNAIGYLPQlsEFDRQFPISVRDLVLMGSLPH 97
Cdd:PRK10982 24 HSIHALMGENGAGKSTLLKCLFGIYQKDSGSilfqgkeidFKSSKEALENGISMVHQ--ELNLVLQRSVMDNMWLGRYPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 RGLLRSiHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQL 177
Cdd:PRK10982 102 KGMFVD-QDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL 180
|
170
....*....|....*
gi 2316063307 178 HAEGRTILAVLHDLE 192
Cdd:PRK10982 181 KERGCGIVYISHKME 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-193 |
1.46e-09 |
|
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: 55.06 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKtlagllpplsgsfslgdgskdnAIGYLpqlsEFDRQFPISVRDLVLMGslphrgllrs 103
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILD----------------------AIGLA----LGGAQSATRRRSGVKAG---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 104 ihvnwHRKATDALDAVSMkdfadrhIGVLSGGQLQRV----LFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHA 179
Cdd:cd03227 62 -----CIVAAVSAELIFT-------RLQLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLV 129
|
170
....*....|....
gi 2316063307 180 EGRTILAVLHDLEL 193
Cdd:cd03227 130 KGAQVIVITHLPEL 143
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-192 |
1.53e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.63 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 32 IIGANGSGKSTLLKTLAGLLPPLSGSFSLGDgsKDnaigyLPQLSEFDR--------QFPisvrdlvLMGSLPH------ 97
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPPDSGSILIDG--KD-----VTKLPEYKRakyigrvfQDP-------MMGTAPSmtieen 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 ------RGLLR--SIHVNWHRKA--TDALDAVSMkDFADR---HIGVLSGGQLQRV--LFArlLLTQAPIILLDEPFTGI 162
Cdd:COG1101 103 lalayrRGKRRglRRGLTKKRRElfRELLATLGL-GLENRldtKVGLLSGGQRQALslLMA--TLTKPKLLLLDEHTAAL 179
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 163 DSHTTQALLQIIEQLHAEGR-TILAVLHDLE 192
Cdd:COG1101 180 DPKTAALVLELTEKIVEENNlTTLMVTHNME 210
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-194 |
1.62e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPP----LSGSFSLgDGSKDNAIGYLPQLSEFDRQFPISVRDLVL-MGS-----LP 96
Cdd:PRK10418 29 GRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLL-DGKPVAPCALRGRKIATIMQNPRSAFNPLHtMHTharetCL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSihvnwHRKATDALDAVSMKD---FADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQI 173
Cdd:PRK10418 108 ALGKPAD-----DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDL 182
|
170 180
....*....|....*....|..
gi 2316063307 174 IEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK10418 183 LESIVQKrALGMLLVTHDMGVV 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
22-204 |
2.63e-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: 54.89 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 22 GCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKdnaIGYLPQLSEfdrqfpisvrdlvlmgslphrgll 101
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGIT---PVYKPQYID------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 102 rsihvnwhrkatdaldavsmkdfadrhigvLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEG 181
Cdd:cd03222 72 ------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....
gi 2316063307 182 -RTILAVLHDLeLVGQHFPNILHL 204
Cdd:cd03222 122 kKTALVVEHDL-AVLDYLSDRIHV 144
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-213 |
3.27e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.56 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 29 LTAIIGANGSGKSTLLKT---LAGLLPPLSGSFSLGDGSKDNaigYLPQL--SEFDRQ----------FPISVRDLVLMG 93
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNL---YAPDVdpVEVRRRigmvfqkpnpFPKSIYDNIAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SlphrgllrsiHVNWHRKATDALDAVSMKDFA------D--RHIGV-LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:PRK14243 115 A----------RINGYKGDMDELVERSLRQAAlwdevkDklKQSGLsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 165 HTTQALLQIIEQLhAEGRTILAVLHDLELVGQ-----HFPNIlHLTPDGHRWGE 213
Cdd:PRK14243 185 ISTLRIEELMHEL-KEQYTIIIVTHNMQQAARvsdmtAFFNV-ELTEGGGRYGY 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-194 |
5.37e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAgllpplsGSFSLGDGS--KDNAIGYLPQlsefdrQFPI---SVRDLVLMGSlphrgl 100
Cdd:PTZ00243 685 RGKLTVVLGATGSGKSTLLQSLL-------SQFEISEGRvwAERSIAYVPQ------QAWImnaTVRGNILFFD------ 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 lrsihvnwHRKATDALDAVSM----KDFA------DRHIGV----LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHT 166
Cdd:PTZ00243 746 --------EEDAARLADAVRVsqleADLAqlggglETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180
....*....|....*....|....*...
gi 2316063307 167 TQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVV 845
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-191 |
1.06e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGY--RSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGskDNAIGYlpQLSEFD 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DG--HDLRDY--TLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 RQFPISVRDLVLMGSLPHRGLLRSIHVNWHR-------KATDALDAVS-MKDFADRHIG----VLSGGQLQRVLFARLLL 147
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIAYARTEQYSReqieeaaRMAYAMDFINkMDNGLDTVIGengvLLSGGQRQRIAIARALL 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 148 TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEgRTILAVLHDL 191
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRL 539
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-195 |
1.14e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG------SKDNAIGYLPQLSEFDRQF----PI-SVRDLVLMG 93
Cdd:PRK11288 277 RAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL-DGkpidirSPRDAIRAGIMLCPEDRKAegiiPVhSVADNINIS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPHrgllrsihvnwHRKATDALDAVSMKDFADRH--------------IGVLSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:PRK11288 356 ARRH-----------HLRAGCLINNRWEAENADRFirslniktpsreqlIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 160 TGIDSHTTQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLG 461
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-205 |
1.16e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPP--LSGSFSLGDGSKDNAI----GYLPQlseFDRQFP-ISVRDL 89
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPTKQIlkrtGFVTQ---DDILYPhLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VLMGSLPH--RGLLRSIHVnwhRKATDALDAVSMKDFADRHIGV-----LSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:PLN03211 161 LVFCSLLRlpKSLTKQEKI---LVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2316063307 163 DSHTTQALLQIIEQLHAEGRTILAVLHD-LELVGQHFPNILHLT 205
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLS 281
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
31-194 |
1.72e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.97 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGsKDnaIGYLP--QLSEFDRQFPI-------------SVRD-----LV 90
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILF-DG-QD--ITGLSgrELRPLRRRMQMvfqdpyaslnprmTVGDiiaepLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LMGSLPHRGLLRsihvnwhrKATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGID-ShtTQ 168
Cdd:COG4608 124 IHGLASKAERRE--------RVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvS--IQ 193
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 169 AllQII---EQLHAE-GRTILAVLHDLELV 194
Cdd:COG4608 194 A--QVLnllEDLQDElGLTYLFISHDLSVV 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-193 |
2.56e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.94 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLagllpplsgsfslgdGSKDNAIGYLPQLSEFDRQFPISVRDLVLMgslphrgllrsIHV 106
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLVNEG---------------LYASGKARLISFLPKFSRNKLIFIDQLQFL-----------IDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 107 NwhrkatdaLDAVSMkdfaDRHIGVLSGGQLQRVLFARLLLTQAP--IILLDEPFTGIDSHTTQALLQIIEQLHAEGRTI 184
Cdd:cd03238 75 G--------LGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV 142
|
....*....
gi 2316063307 185 LAVLHDLEL 193
Cdd:cd03238 143 ILIEHNLDV 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-194 |
2.67e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPL-ATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaigylpqLSEFD 79
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR---------MAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 80 rQFPISVRDLvlmGSLPHRGLLRSIHVNWHRKATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEP 158
Cdd:PLN03073 579 -QHHVDGLDL---SSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190
....*....|....*....|....*....|....*.
gi 2316063307 159 FTGIDSHTTQALLQIIEQLHAegrTILAVLHDLELV 194
Cdd:PLN03073 655 SNHLDLDAVEALIQGLVLFQG---GVLMVSHDEHLI 687
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-190 |
2.92e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.65 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDG---SKDNAIGYLPQLSE-------FDRqfpisvrdlvLMG 93
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL-DGqpvTADNREAYRQLFSAvfsdfhlFDR----------LLG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPH------RGLLRSIHVNwhrkatdalDAVSMKD--FADRHigvLSGGQLQRV--LFArlLLTQAPIILLDE------ 157
Cdd:COG4615 424 LDGEadparaRELLERLELD---------HKVSVEDgrFSTTD---LSQGQRKRLalLVA--LLEDRPILVFDEwaadqd 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316063307 158 P-----FTgidshttqalLQIIEQLHAEGRTILAVLHD 190
Cdd:COG4615 490 PefrrvFY----------TELLPELKARGKTVIAISHD 517
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-189 |
2.98e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGllpPLSGSFSLGDGSkdnaIGYLPQLSE-FDR------QFPISVRDL 89
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIR----ISGFPKKQEtFARisgyceQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VLMGSLPHRGLLR-SIHVNWHRK---ATDALDAVSMKDFADRHIGV-----LSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:PLN03140 969 TVRESLIYSAFLRlPKEVSKEEKmmfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180
....*....|....*....|....*....
gi 2316063307 161 GIDSHTTQALLQIIEQLHAEGRTILAVLH 189
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-163 |
3.07e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.87 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKSTLLKTLAGLLPPLSGS-------FSLGDGS----KDNAIGYLPQLSEFDRQFPISVRDLVLMGSLPHRG 99
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGElliddhpLHFGDYSyrsqRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEP 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 100 LLRSIHVNwhrkatDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGID 163
Cdd:PRK15112 123 EQREKQII------ETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-197 |
3.10e-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: 51.22 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaigylpqlsefdrqfpisvrdlvlmgslphrgllrsih 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 106 vnwhrKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIE------QLHA 179
Cdd:smart00382 40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSE 114
|
170
....*....|....*...
gi 2316063307 180 EGRTILAVLHDLELVGQH 197
Cdd:smart00382 115 KNLTVILTTNDEKDLGPA 132
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-194 |
3.56e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKdnaIGYLPQLS-EFDRQFPISVRDLVLMGSLPHRGLLRsih 105
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIK---LGYFAQHQlEFLRADESPLQHLARLAPQELEQKLR--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 106 vnwhrkatDALDAVSMK-DFADRHIGVLSGGQLQRVLFArLLLTQAP-IILLDEPFTGIDSHTTQALLQIIeqLHAEGrT 183
Cdd:PRK10636 412 --------DYLGGFGFQgDKVTEETRRFSGGEKARLVLA-LIVWQRPnLLLLDEPTNHLDLDMRQALTEAL--IDFEG-A 479
|
170
....*....|.
gi 2316063307 184 ILAVLHDLELV 194
Cdd:PRK10636 480 LVVVSHDRHLL 490
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-190 |
3.88e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.11 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDG------SKDNAIGYLPQLSEFdrqFP-ISVRDLVLMGslph 97
Cdd:PRK11000 27 HEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvpPAERGVGMVFQSYAL---YPhLSVAENMSFG---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 RGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDshttqALLQI---- 173
Cdd:PRK11000 100 LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD-----AALRVqmri 174
|
170
....*....|....*....
gi 2316063307 174 -IEQLHAE-GRTILAVLHD 190
Cdd:PRK11000 175 eISRLHKRlGRTMIYVTHD 193
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-194 |
8.24e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPP---LSGSfSLGDGskdNAIGYLPQlSEFDR----------QFPIS------ 85
Cdd:PRK09473 40 RAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGS-ATFNG---REILNLPE-KELNKlraeqismifQDPMTslnpym 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 86 -VRDL---VLMgslPHRGLLRSIHVNwhrKATDALDAVSMKDfADRHIGV----LSGGQLQRVLFARLLLTQAPIILLDE 157
Cdd:PRK09473 115 rVGEQlmeVLM---LHKGMSKAEAFE---ESVRMLDAVKMPE-ARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 2316063307 158 PFTGIDShTTQA-LLQIIEQLHAEGRT-ILAVLHDLELV 194
Cdd:PRK09473 188 PTTALDV-TVQAqIMTLLNELKREFNTaIIMITHDLGVV 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-196 |
8.62e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 28 SLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGS-----KD----NAIGY-------------LPQLSEFDR-QFPI 84
Cdd:PRK14246 37 SIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV-DGKvlyfgKDifqiDAIKLrkevgmvfqqpnpFPHLSIYDNiAYPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 85 SVRDL--------VLMGSLPHRGLLRSIHvnwhrkatDALDAVSMKdfadrhigvLSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:PRK14246 116 KSHGIkekreikkIVEECLRKVGLWKEVY--------DRLNSPASQ---------LSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLHAEgRTILAVLHDLELVGQ 196
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVAR 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-157 |
9.80e-08 |
|
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: 52.06 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgdgSKDNAIGYLPQLSEFDRQfpiSVRDLVL--MGSLP--HRGL-- 100
Cdd:TIGR00954 478 GNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---PAKGKLFYVPQRPYMTLG---TLRDQIIypDSSEDmkRRGLsd 551
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 101 ------LRSIHVNWHRKATDALDAVsmKDFADrhigVLSGGQLQRVLFARLLLTQAPIILLDE 157
Cdd:TIGR00954 552 kdleqiLDNVQLTHILEREGGWSAV--QDWMD----VLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-191 |
1.35e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLG----------DGSKdNAIGYLPQ-------LSEFDRQFPISVRD 88
Cdd:PRK09700 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkdisprsplDAVK-KGMAYITEsrrdngfFPNFSIAQNMAISR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 89 LVLMGSLphRGLLRSIHVNWHRK-ATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHT 166
Cdd:PRK09700 367 SLKDGGY--KGAMGLFHEVDEQRtAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGA 444
|
170 180
....*....|....*....|....*
gi 2316063307 167 TQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:PRK09700 445 KAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-197 |
1.58e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.26 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 2 IALQELAFGYRS-QPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIGY--LPQLSEF 78
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSLSHsvLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 79 DRQFPISVRDLVLMGSLPHRGLlrSIHVNWHrkatdALDAVSMKDFADR-------HIG----VLSGGQLQRVLFARLLL 147
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDI--SEEQVWQ-----ALETVQLAELARSlpdglytPLGeqgnNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 148 TQAPIILLDEPFTGIDSHTTQAL---LQIIEQ-------LH-----AEGRTILaVLHDLELV--GQH 197
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIqqaLAAVREhttlvviAHrlstiVEADTIL-VLHRGQAVeqGTH 558
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
103-208 |
1.75e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 103 SIHVNWHRKATDALDAVSMkdfaDRHIGVLSGGQLQRVLFARLLLTQAP---IILLDEPFTGIDSHTTQALLQIIEQLHA 179
Cdd:PRK00635 785 SIHEKIHALCSLGLDYLPL----GRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTH 860
|
90 100
....*....|....*....|....*....
gi 2316063307 180 EGRTILAVLHDLELVgQHFPNILHLTPDG 208
Cdd:PRK00635 861 QGHTVVIIEHNMHVV-KVADYVLELGPEG 888
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-194 |
1.90e-07 |
|
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: 50.31 E-value: 1.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 132 LSGGQLQRVLFARLLLTQAP---IILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI 235
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-208 |
2.42e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.78 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 132 LSGGQLQRVLFARLLL---TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHfPNILHLTPDG 208
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTA-DYIIDLGPEG 908
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-196 |
2.67e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSkdnaigyLPQLSEFDR------------QFPISVRDLVLMGSLPHR 98
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-------LHQMDEEARaklrakhvgfvfQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 99 GLLRSIHVNWHRK-ATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQL 177
Cdd:PRK10584 113 ALLRGESSRQSRNgAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170 180
....*....|....*....|
gi 2316063307 178 HAE-GRTILAVLHDLELVGQ 196
Cdd:PRK10584 193 NREhGTTLILVTHDLQLAAR 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-196 |
4.94e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIG----------YLPQlsefDRQF-------PIS--VR 87
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLYGLRPARGGRIML-NGKEINALStaqrlarglvYLPE----DRQSsglyldaPLAwnVC 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 88 DLV--LMGSLPHRGLLRSIHVNWHRkatdaldAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:PRK15439 364 ALThnRRGFWIKPARENAVLERYRR-------ALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190
....*....|....*....|....*....|..
gi 2316063307 165 HTTQALLQIIEQLHAEGRTILAVLHDLELVGQ 196
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
129-195 |
5.63e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 5.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316063307 129 IGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLG 468
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-174 |
5.86e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYrSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAigYLPQLSEFDR 80
Cdd:PRK13541 1 MLSLHQLQFNI-EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 QFPISVrDLVLMGSLphrgLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFT 160
Cdd:PRK13541 78 NLGLKL-EMTVFENL----KFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170
....*....|....
gi 2316063307 161 GIDSHTTQALLQII 174
Cdd:PRK13541 153 NLSKENRDLLNNLI 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-190 |
8.16e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAigylPQLSEFDRQFPISVRDLVLMGSL-------PH 97
Cdd:PRK10522 347 KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTA----EQPEDYRKLFSAVFTDFHLFDQLlgpegkpAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 RGLLRSihvnWhrkatdaLDAVSMKD---FADRHIGV--LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQ 172
Cdd:PRK10522 422 PALVEK----W-------LERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170
....*....|....*....
gi 2316063307 173 -IIEQLHAEGRTILAVLHD 190
Cdd:PRK10522 491 vLLPLLQEMGKTIFAISHD 509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-196 |
1.07e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLAT----LSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD-------------- 62
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTvvndVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDirfhgesllhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 63 ---GSKDNAIGYLPQ--------LSEFDRQfpisvrdLVLMGSLpHRGLLRSIHvnwHRKATDALDAVSMKDFADR---- 127
Cdd:PRK15134 85 tlrGVRGNKIAMIFQepmvslnpLHTLEKQ-------LYEVLSL-HRGMRREAA---RGEILNCLDRVGIRQAAKRltdy 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 128 -HigVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDShTTQA-LLQIIEQLHAE-GRTILAVLHDLELVGQ 196
Cdd:PRK15134 154 pH--QLSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAqILQLLRELQQElNMGLLFITHNLSIVRK 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-194 |
1.25e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.53 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPlSGSFSLGDgskdNAIGYLP--QLSEFDRQFPI-------------SVRDL 89
Cdd:COG4172 310 RRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDG----QDLDGLSrrALRPLRRRMQVvfqdpfgslsprmTVGQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 90 VLMGSLPHR-GLLRSIHvnwHRKATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDsHTT 167
Cdd:COG4172 385 IAEGLRVHGpGLSAAER---RARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSV 460
|
170 180 190
....*....|....*....|....*....|.
gi 2316063307 168 QAllQIIE---QLHAE-GRTILAVLHDLELV 194
Cdd:COG4172 461 QA--QILDllrDLQREhGLAYLFISHDLAVV 489
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-194 |
1.69e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.78 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFS-LGdgsKDnaigyLPQLSEFDRQfpiSVRDLVLM------GSLPH 97
Cdd:PRK15079 45 YEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLG---KD-----LLGMKDDEWR---AVRSDIQMifqdplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 98 RGL--------LRSIHVNWHRKAT-DALDAVSMK-----DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGID 163
Cdd:PRK15079 114 RMTigeiiaepLRTYHPKLSRQEVkDRVKAMMLKvgllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|..
gi 2316063307 164 SHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVV 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-191 |
1.77e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPplSGSFSlGDgskdnaIGYLPQLSEFDrqfpiSVRD--------------LV 90
Cdd:NF040905 25 REGEIHALCGENGAGKSTLMKVLSGVYP--HGSYE-GE------ILFDGEVCRFK-----DIRDsealgiviihqelaLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 LMGSLP----------HRGLlrsihVNW---HRKATDALDAVSMKDFAD---RHIGVlsgGQLQRVLFARLLLTQAPIIL 154
Cdd:NF040905 91 PYLSIAeniflgneraKRGV-----IDWnetNRRARELLAKVGLDESPDtlvTDIGV---GKQQLVEIAKALSKDVKLLI 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2316063307 155 LDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL 191
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKL 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-194 |
1.83e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPplsgSFSLGDGSKDNAIGYLPQ------------LSEFDRQFP- 83
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTD----GFHIGVEGVITYDGITPEeikkhyrgdvvyNAETDVHFPh 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 84 ISVRDLV----LMGSLPHRGLLRSIHVnWHRKATDaldaVSMKDFADRHI-----------GVlSGGQLQRVLFARLLLT 148
Cdd:TIGR00956 153 LTVGETLdfaaRCKTPQNRPDGVSREE-YAKHIAD----VYMATYGLSHTrntkvgndfvrGV-SGGERKRVSIAEASLG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2316063307 149 QAPIILLDEPFTGIDSHTTqalLQIIEQLhaegRTILAVLHDLELV 194
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATA---LEFIRAL----KTSANILDTTPLV 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
129-195 |
1.98e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 1.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316063307 129 IGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELpEVLG 470
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
130-191 |
2.12e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 2.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 130 GV-LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLHDL 191
Cdd:PRK10789 449 GVmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRL 510
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-194 |
3.29e-06 |
|
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: 46.48 E-value: 3.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 126 DRHIGVLSGGQLQRVLFARLL---LTQApIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-190 |
4.51e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDnaigylpQLSEFDR------Q----FP-ISVRDLvlM 92
Cdd:PRK11650 27 VADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-------ELEPADRdiamvfQnyalYPhMSVREN--M 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 93 G-SLPHRGLLRSiHVNwhRKATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDshttqALL 171
Cdd:PRK11650 98 AyGLKIRGMPKA-EIE--ERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-----AKL 169
|
170 180
....*....|....*....|....*
gi 2316063307 172 QI-----IEQLHAE-GRTILAVLHD 190
Cdd:PRK11650 170 RVqmrleIQRLHRRlKTTSLYVTHD 194
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-194 |
1.10e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316063307 126 DRHIGVLSGGQLQRVLFARLLLTQAPII--LLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI 541
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-189 |
1.19e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 132 LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEG-RTILAVLH 189
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
130-195 |
2.50e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316063307 130 GVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDL-ELVG 195
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELpELLG 469
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-192 |
2.97e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.07 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPpLSGSFSLgDGSKDNAIgylpQLSEFDRQFPIsVRDLVLMGSLP 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNSV----PLQKWRKAFGV-IPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSIHVNWHRKATDALDAVSMKDFADRHIG-----------VLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSH 165
Cdd:cd03289 93 FRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180
....*....|....*....|....*..
gi 2316063307 166 TTQALLQIIEQLHAeGRTILAVLHDLE 192
Cdd:cd03289 173 TYQVIRKTLKQAFA-DCTVILSEHRIE 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-186 |
3.43e-05 |
|
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: 44.52 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPlSGSFSLgDGSKDNAIgylpQLSEFDRQFPISVRDLVLMGSLP 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQI-DGVSWNSV----TLQTWRKAFGVIPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLlrSIHVNWHR----KATDALDAVSM-------KDFADRHIG-VLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:TIGR01271 1309 RKNL--DPYEQWSDeeiwKVAEEVGLKSVieqfpdkLDFVLVDGGyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180
....*....|....*....|..
gi 2316063307 165 HTTQALLQIIEQLHAEGRTILA 186
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCTVILS 1408
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-194 |
3.98e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 21 SGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSkdNAIGYlpqlsefDRQFPISVRDLVLM------GS 94
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQ--DLLKA-------DPEAQKLLRQKIQIvfqnpyGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRS-------IHVNWHR-----KATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTG 161
Cdd:PRK11308 105 LNPRKKVGQileepllINTSLSAaerreKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190
....*....|....*....|....*....|....
gi 2316063307 162 IDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVV 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
127-194 |
6.23e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 6.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316063307 127 RHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDsHTTQA----LLQIIEQLHAegrtiLAVL---HDLELV 194
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAqilaLLKSLQQKHQ-----LAYLfisHDLHVV 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-208 |
7.61e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.71 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 23 CFHQGSLTAIIGANGSGKSTLLKTLAGllpplSGSFSLGDGS---KDNAIGYLP-----QLSEF-DRQFPISVrdlvlmG 93
Cdd:CHL00131 29 SINKGEIHAIMGPNGSGKSTLSKVIAG-----HPAYKILEGDilfKGESILDLEpeeraHLGIFlAFQYPIEI------P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 94 SLPHRGLLRSIHvNWHRKA---------------TDALDAVSMKD-FADRHIGV-LSGGQLQRVLFARLLLTQAPIILLD 156
Cdd:CHL00131 98 GVSNADFLRLAY-NSKRKFqglpeldplefleiiNEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 157 EPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHLTPDG 208
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNG 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
109-196 |
8.89e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 109 HRKATDALDAVSMKDFADRhIGV----LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDShTTQAllQIIEQL----HAE 180
Cdd:PRK11022 128 RQRAIDLLNQVGIPDPASR-LDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQA--QIIELLlelqQKE 203
|
90
....*....|....*.
gi 2316063307 181 GRTILAVLHDLELVGQ 196
Cdd:PRK11022 204 NMALVLITHDLALVAE 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-208 |
1.66e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 1 MIALQELAFGYRSQPPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGllpplSGSFSLGDGSKDNAIGYLPQLSEFDR 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-----REDYEVTGGTVEFKGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 ---------QFPISVRdlvlmgSLPHRGLLRSiHVNWHRK--ATDALDAVSMKDFADRHIGVL---------------SG 134
Cdd:PRK09580 76 agegifmafQYPVEIP------GVSNQFFLQT-ALNAVRSyrGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 135 GQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHLTPDG 208
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQG 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-196 |
1.95e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSL-GDGS--KDNAiGYLPQLSEFDR-QFpisvrDLVLMGslphrgl 100
Cdd:PRK13546 48 YEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRnGEVSviAISA-GLSGQLTGIENiEF-----KMLCMG------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 101 lrsihvnWHRKATDAL-----DAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIE 175
Cdd:PRK13546 115 -------FKRKEIKAMtpkiiEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180
....*....|....*....|.
gi 2316063307 176 QLHAEGRTILAVLHDLELVGQ 196
Cdd:PRK13546 188 EFKEQNKTIFFVSHNLGQVRQ 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-197 |
2.00e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.98 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 31 AIIGANGSGKS-TLLKTLaGLLPP----LSGSFSLGDgsKDnaigyLPQLSEFDRQfpiSVR--DLVL-----MGSL-P- 96
Cdd:COG4172 40 ALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDG--QD-----LLGLSERELR---RIRgnRIAMifqepMTSLnPl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 -------------HRGLLRSihvNWHRKATDALDAVSMKDfADRHIGV----LSGGQLQRVLFARLLLTQAPIILLDEPF 159
Cdd:COG4172 109 htigkqiaevlrlHRGLSGA---AARARALELLERVGIPD-PERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2316063307 160 TGIDShTTQA-LLQIIEQLHAE-GRTILAVLHDLELVGQH 197
Cdd:COG4172 185 TALDV-TVQAqILDLLKDLQRElGMALLLITHDLGVVRRF 223
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-62 |
2.35e-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: 41.61 E-value: 2.35e-04
10 20 30
....*....|....*....|....*....|....
gi 2316063307 29 LTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGD 62
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTD 34
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
111-196 |
2.80e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 111 KATDALDAVSMKDFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHD 190
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY 203
|
....*.
gi 2316063307 191 LELVGQ 196
Cdd:NF000106 204 MEEAEQ 209
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
106-196 |
3.67e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 106 VNW-HRKATDALDAVSMKDFADRHIGV---LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDShTTQAllQIIEQL---- 177
Cdd:PRK15093 129 FGWrKRRAIELLHRVGIKDHKDAMRSFpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEP-TTQA--QIFRLLtrln 205
|
90
....*....|....*....
gi 2316063307 178 HAEGRTILAVLHDLELVGQ 196
Cdd:PRK15093 206 QNNNTTILLISHDLQMLSQ 224
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
126-176 |
4.38e-04 |
|
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: 38.37 E-value: 4.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 126 DRHIGVLSGGQLQR----VLFARL--LLTQAP-------IILLDEPFTGIDSHTTQALLQIIEQ 176
Cdd:pfam13558 27 YRRSGGLSGGEKQLlaylPLAAALaaQYGSAEgrppaprLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-194 |
4.81e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 7 LAFGYRSQ--PPLATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEFDRQFPI 84
Cdd:PRK10261 20 IAFMQEQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 85 SVR--DLVL-----MGSLP---------------HRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGVLSGGQLQRVLF 142
Cdd:PRK10261 100 HVRgaDMAMifqepMTSLNpvftvgeqiaesirlHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2316063307 143 ARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHAE-GRTILAVLHDLELV 194
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVV 232
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
29-63 |
6.28e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 6.28e-04
10 20 30
....*....|....*....|....*....|....*
gi 2316063307 29 LTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDG 63
Cdd:COG1106 31 VNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDK 65
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-194 |
6.93e-04 |
|
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: 40.70 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 17 LATLSGCFHQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgDGSKDNAIGylpqLSEFDRQFPISVRDLVLM-GSL 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGLNIAKIG----LHDLRFKITIIPQDPVLFsGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 96 phRGLLRSIHVNWHRKATDALDAVSMKDFADRHIGV-----------LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDS 164
Cdd:TIGR00957 1377 --RMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190
....*....|....*....|....*....|
gi 2316063307 165 HTTQaLLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:TIGR00957 1455 ETDN-LIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-65 |
7.06e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.98 E-value: 7.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2316063307 25 HQGSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSK 65
Cdd:COG3950 23 NPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRK 63
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-53 |
7.07e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 7.07e-04
10 20 30
....*....|....*....|....*....|
gi 2316063307 24 FHQGSLTAIIGANGSGKSTLLKTLAGLLPP 53
Cdd:pfam13555 19 IDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
24-189 |
1.11e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 39.11 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 24 FHQGsLTAIIGANGSGKSTLLKTLAGLL---------------PPLSGSFSLGDGSKD----NAIGYLPQLSEFDR---- 80
Cdd:cd03241 19 FEEG-LTVLTGETGAGKSILLDALSLLLggrasadlirsgaekAVVEGVFDISDEEEAkallLELGIEDDDDLIIRreis 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 81 ----------QFPISVRDLVLMGSL--------PHRGLLRSIHvnwHRKATDA-LDAVSMkdFADRHIG--------VLS 133
Cdd:cd03241 98 rkgrsryfinGQSVTLKLLRELGSLlvdihgqhDHQNLLNPER---QLDLLDGgLDDVEF--LFSTNPGeplkplakIAS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 134 GGQLQRVLFA-RLLLTQ---APIILLDEPFTGIDSHTTQALLQIIEQLhAEGRTILAVLH 189
Cdd:cd03241 173 GGELSRLMLAlKAILARkdaVPTLIFDEIDTGISGEVAQAVGKKLKEL-SRSHQVLCITH 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
27-196 |
1.64e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.73 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPP----LSGSFSLGDgsKDnaigyLPQLSEFDR------------QFPISVRDLV 90
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNG--ID-----LLKLSPRERrkiigreiamifQEPSSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 91 ------LMGSLPHRGLLRSIhvnWHRK------ATDALDAVSMKDfadrHIGV-------LSGGQLQRVLFARLLLTQAP 151
Cdd:COG4170 106 akigdqLIEAIPSWTFKGKW---WQRFkwrkkrAIELLHRVGIKD----HKDImnsypheLTEGECQKVMIAMAIANQPR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316063307 152 IILLDEPFTGIDShTTQA----LLQIIEQLHaeGRTILAVLHDLELVGQ 196
Cdd:COG4170 179 LLIADEPTNAMES-TTQAqifrLLARLNQLQ--GTSILLISHDLESISQ 224
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
24-78 |
1.88e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 24 FHQGsLTAIIGANGSGKSTLLK--TLA--GLLPPLSGSFSLGDGSKDNAIGYLPQLSEF 78
Cdd:pfam13476 16 FSKG-LTLITGPNGSGKTTILDaiKLAlyGKTSRLKRKSGGGFVKGDIRIGLEGKGKAY 73
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-202 |
1.90e-03 |
|
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: 39.02 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGL--LPPLSGS--FSLGDGSKdnaIGYLPQLSEFDRQFPI-------SVRDLVLMGS 94
Cdd:TIGR03269 25 EGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiYHVALCEK---CGYVERPSKVGEPCPVcggtlepEEVDFWNLSD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 95 LPHRGLLRSIHVNWHR--------------------------KATD-ALDAVSMKDFADR--HIGV-LSGGQLQRVLFAR 144
Cdd:TIGR03269 102 KLRRRIRKRIAIMLQRtfalygddtvldnvlealeeigyegkEAVGrAVDLIEMVQLSHRitHIARdLSGGEKQRVVLAR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 145 LLLTQAPIILLDEPFTGIDSHTTQALLQ-IIEQLHAEGRTIlavlhdleLVGQHFPNIL 202
Cdd:TIGR03269 182 QLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISM--------VLTSHWPEVI 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-194 |
2.15e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.86 E-value: 2.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2316063307 132 LSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIEQLHA-EGRTILAVLHDLELV 194
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTI 643
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-190 |
2.45e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316063307 126 DRHIGVLSGGQLQRVLFARLL---LTQApIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHD 190
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD 549
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
132-195 |
2.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 132 LSGGQlqRVLFA--------RLLLT----QAPI--ILLDEPFTGIDS-HTTQaLLQIIEQLHAEG-RTILAVLHDLELVG 195
Cdd:PRK02224 782 LSGGE--RALFNlslrcaiyRLLAEgiegDAPLppLILDEPTVFLDSgHVSQ-LVDLVESMRRLGvEQIVVVSHDDELVG 858
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-57 |
2.95e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.57 E-value: 2.95e-03
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-194 |
3.06e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 38.30 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLGDGSKDNAIGYLPQLSEFDRQF----------PISVRDLVLMGSLP 96
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFifqdpyasldPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 97 HRGLLRSIHVnwHRKATDALDAVSMK-DFADRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHTTQALLQIIE 175
Cdd:PRK10261 430 VHGLLPGKAA--AARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180
....*....|....*....|
gi 2316063307 176 QLHAE-GRTILAVLHDLELV 194
Cdd:PRK10261 508 DLQRDfGIAYLFISHDMAVV 527
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
26-62 |
3.16e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.06 E-value: 3.16e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2316063307 26 QGSLTAIIGANGSGKSTLLKTLAGLLPPLSG-SFSLGD 62
Cdd:COG3593 22 SDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEED 59
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-204 |
3.34e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316063307 133 SGGQLQRVLFARLLLTQAPIILLDEPFTGIDSHttqALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH---AVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
27-48 |
3.63e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 3.63e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
132-194 |
3.99e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 3.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 132 LSGGQLQRVLFARLLLTQA---PIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVI 896
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-194 |
4.04e-03 |
|
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: 37.75 E-value: 4.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316063307 129 IGVLSGGQLQRVLFARLLLTQAP---IILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-194 |
4.85e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 4.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316063307 132 LSGGQLQRVLFARLLL---TQAPIILLDEPFTGIDSHTTQALLQIIEQLHAEGRTILAVLHDLELV 194
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVI 892
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-204 |
8.91e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.07 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 27 GSLTAIIGANGSGKSTLLKTLAGLLPPLSGSFSLgdgSKDNAIGYLPQLSEfdrQFPISVRDLVLMGSLPHRGLLRSIHV 106
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQLAWVNQETP---ALPQPALEYVIDGDREYRQLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316063307 107 -----NWHRKAT-----DALDAVSMKDFA--------------DRHIGVLSGGQLQRVLFARLLLTQAPIILLDEPFTGI 162
Cdd:PRK10636 101 anernDGHAIATihgklDAIDAWTIRSRAasllhglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2316063307 163 DshtTQALLQIIEQLHAEGRTILAVLHDLELVGQHFPNILHL 204
Cdd:PRK10636 181 D---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
22-47 |
9.47e-03 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 36.12 E-value: 9.47e-03
10 20
....*....|....*....|....*.
gi 2316063307 22 GCFHQgSLTAIIGANGSGKSTLLKTL 47
Cdd:cd03274 21 GPFHK-SFSAIVGPNGSGKSNVIDSM 45
|
|
| |
