|
Name |
Accession |
Description |
Interval |
E-value |
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-248 |
4.27e-145 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 405.76 E-value: 4.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 5 MQLTDVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVP 84
Cdd:COG4138 1 LQLNDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 PFAMPVWHYLMLHLHDKHSTA----LLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPAGNPHGRMLLLDEP 160
Cdd:COG4138 81 PFAMPVFQYLALHQPAGASSEaveqLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTINPEGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 161 MSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMSFRRLDIE 240
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVE 240
|
....*...
gi 495776072 241 GHKMLIST 248
Cdd:COG4138 241 GHRWLIPT 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-248 |
5.37e-142 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 397.77 E-value: 5.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 5 MQLTDVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVP 84
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 PFAMPVWHYLMLHLHDKHSTA----LLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPAGNPHGRMLLLDEP 160
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEavasALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 161 MSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMSFRRLDIE 240
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDVE 240
|
....*...
gi 495776072 241 GHKMLIST 248
Cdd:PRK03695 241 GHPMLIST 248
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-232 |
2.73e-61 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 193.41 E-value: 2.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYL 94
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 ML-----HLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPAGNPHGRMLLLDEPMSGLDVAQQ 169
Cdd:COG4559 97 ALgraphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGPRWLFLDEPTSALDLAHQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNM 232
Cdd:COG4559 177 HAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGA 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-246 |
1.35e-60 |
|
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: 191.41 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYL 94
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 ML----HLH-----DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLD 165
Cdd:COG1120 97 ALgrypHLGlfgrpSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ-----EP--PLLLLDEPTSHLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 166 VAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMSFRRLDIE--GH 242
Cdd:COG1120 170 LAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARVIEDPvtGR 249
|
....
gi 495776072 243 KMLI 246
Cdd:COG1120 250 PLVL 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-215 |
2.14e-54 |
|
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: 173.01 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQqqvppfampvwhy 93
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 lmlhlhdkhstalltdVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAALD 173
Cdd:cd03214 81 ----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ-----EP--PILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495776072 174 TLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03214 138 ELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-230 |
4.23e-49 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 162.25 E-value: 4.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPV---------- 90
Cdd:PRK13548 24 TLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVeevvamgrap 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 WHylmlhLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPAGNPhGRMLLLDEPMSGLDVAQQA 170
Cdd:PRK13548 104 HG-----LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGP-PRWLLLDEPTSALDLAHQH 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 171 ALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:PRK13548 178 HVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-238 |
8.34e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 158.33 E-value: 8.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLehtlaeWSPVSLAHRR-SYLVQQ-QVPP------- 85
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlPPTSGTVRLF------GKPPRRARRRiGYVPQRaEVDWdfpitvr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 86 --FAMPVWHYL-MLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMS 162
Cdd:COG1121 96 dvVLMGRYGRRgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ-----DP--DLLLLDEPFA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 163 GLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGkMIASGTRDQVLTPPNLARAYNMSFRRLD 238
Cdd:COG1121 169 GVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGGPVALLA 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
16-221 |
2.68e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.95 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG-EGQIMLLEHTLAEwSPVSLAHRRSYLVQQQVPPFAMPVWHYL 94
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLH-----LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDVAQQ 169
Cdd:COG1131 95 RFFarlygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL-----HDP--ELLILDEPTSGLDPEAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG1131 168 RELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-215 |
3.00e-37 |
|
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: 130.35 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEhtlaewSPVSLAHRR-SYLVQQQVPPFAMPV--- 90
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGlLKPTSGSIRVFG------KPLEKERKRiGYVPQRRSIDRDFPIsvr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 -------WHYLMLHLHDKHSTALLTDVA-AALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMS 162
Cdd:cd03235 89 dvvlmglYGHKGLFRRLSKADKAKVDEAlERVGLSELADRQIGELSGGQQQRVLLARALVQ-----DP--DLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495776072 163 GLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSqGKMIASG 215
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-210 |
3.24e-36 |
|
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: 127.58 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQ---QQvppFAMP-- 89
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLlGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQnpdDQ---FFGPtv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 ----VWHYLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLD 165
Cdd:cd03225 94 eeevAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL-----AMDP--DILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495776072 166 VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-222 |
5.12e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 127.45 E-value: 5.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQ---QQVppFAMPVW 91
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQnpdDQL--FAPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYLM-----LHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLDV 166
Cdd:COG1122 95 EDVAfgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA-MEP------EVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 167 AQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLT 222
Cdd:COG1122 168 RGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-211 |
8.79e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 8.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG-EGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFAM 88
Cdd:COG4619 10 VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAY-VPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYL---MLHLHDKHSTALLTDVAAALGL-EDKLSRHVSQLSGGEWQRVRLAAVIvQIHPagnphgRMLLLDEPMSGL 164
Cdd:COG4619 89 TVRDNLpfpFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRAL-LLQP------DVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495776072 165 DVAQQAALDTLLSALS-RKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:COG4619 162 DPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-224 |
1.90e-33 |
|
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: 121.00 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHR---RSYlvqQQVPPFA-MPVWHYLMLH 97
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLISGFlRPTSGSVLFDGEDITGLPPHEIARLgigRTF---QIPRLFPeLTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHDKHSTALLT---------------DVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMS 162
Cdd:cd03219 100 AQARTGSGLLLararreereareraeELLERVGLADLADRPAGELSYGQQRRLEIARAL-----ATDP--KLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 163 GLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:cd03219 173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-224 |
8.37e-32 |
|
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: 121.93 E-value: 8.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSY--LVQQQvpPFA-----MPVWHYL 94
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGLlRPTSGSILFDGKDLTKLSRRSLRELRRRvqMVFQD--PYSslnprMTVGDII 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 M--LHLHDKHSTALLTDVAAAL----GL-EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVA 167
Cdd:COG1123 366 AepLRLHGLLSRAERRERVAELlervGLpPDLADRYPHELSGGQRQRVAIARAL-----ALEP--KLLILDEPTSALDVS 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 168 QQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG1123 439 VQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-238 |
4.29e-31 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 115.69 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 3 LLMQLTDVAEKGR--LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAG--------EGQIMLLEHTLAEWSPVSL 71
Cdd:PRK13547 2 LTADHLHVARRHRaiLRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 72 AHRRSYLVQQQVPPFAMPVWHYLML--HLHDKHSTAL------LTDVAAALGLEDKL-SRHVSQLSGGEWQRVRLAAVIV 142
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLgrYPHARRAGALthrdgeIAWQALALAGATALvGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 143 QIHPAGN--PHGRMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQ 219
Cdd:PRK13547 162 QLWPPHDaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250
....*....|....*....
gi 495776072 220 VLTPPNLARAYNMSFRRLD 238
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVD 260
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-210 |
2.73e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.41 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVSLAHRRSYlvqqqvppfampvwhyl 94
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEELRRRIGY----------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 mlhlhdkhstalltdvaaalgledklsrhVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd00267 78 -----------------------------VPQLSGGQRQRVALARALLL-----NP--DLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 495776072 175 LLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:cd00267 122 LLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-220 |
4.14e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.67 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLaRMA-G-MTAGEGQIMLLEHtlaewsPVSLAHRRS--YLvqqqvP------PfAMPVWH 92
Cdd:COG4152 24 VPKGEIFGLLGPNGAGKTTTI-RIIlGiLAPDSGEVLWDGE------PLDPEDRRRigYL-----PeerglyP-KMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 ---YL-MLHLHDKH-STALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqIHpagNPhgRMLLLDEPMSGLD-V 166
Cdd:COG4152 91 qlvYLaRLKGLSKAeAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL--LH---DP--ELLILDEPFSGLDpV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 167 AQQAALDTLLsALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQV 220
Cdd:COG4152 164 NVELLKDVIR-ELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-244 |
4.22e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.48 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLvqQQVPPFAM------ 88
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRlLPPDSGEVLVDGLDVATTPSRELAKRLAIL--RQENHINSrltvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 -------PvwhylmlhlhdkHSTALLTD-----VAAA---LGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGR 153
Cdd:COG4604 95 lvafgrfP------------YSKGRLTAedreiIDEAiayLDLEDLADRYLDELSGGQRQRAFIAMVLAQ-------DTD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 154 MLLLDEPMSGLDVAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNM 232
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDT 235
|
250
....*....|..
gi 495776072 233 SFRRLDIEGHKM 244
Cdd:COG4604 236 DIEVEEIDGKRI 247
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-230 |
6.75e-30 |
|
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: 112.05 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHR---RSYlvqQQVPPFA-MPVWHYLML 96
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGFyRPTSGRILFDGRDITGLPPHRIARLgiaRTF---QNPRLFPeLTVLENVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HLHDKHSTALLT--------------------DVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLL 156
Cdd:COG0411 103 AAHARLGRGLLAallrlprarreereareraeELLERVGLADRADEPAGNLSYGQQRRLEIARAL-----ATEP--KLLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 157 LDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEAY 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-232 |
1.05e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.64 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLL---ARMagMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPV----------W 91
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLkcfARL--LTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVrelvaygrspW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 --HYLMLHLHDKHstaLLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQ 169
Cdd:PRK11231 105 lsLWGRLSAEDNA---RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP-------VVLLDEPTTYLDINHQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNM 232
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDV 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-205 |
7.13e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 108.34 E-value: 7.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEwSPVSLAHRRSYLVQQQVPPFAMPVWHYL 94
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGlLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLH---LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAA 171
Cdd:COG4133 97 RFWaalYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS-------PAPLWLLDEPFTALDAAGVAL 169
|
170 180 190
....*....|....*....|....*....|....
gi 495776072 172 LDTLLSALSRKGIAVVMSSHDLnHTLRHAHRVWL 205
Cdd:COG4133 170 LAELIAAHLARGGAVLLTTHQP-LELAAARVLDL 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
16-220 |
1.76e-28 |
|
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: 107.65 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLL---ARMAGMTAG---EGQIMLLEHTLAEWSPVSLAHRRSY-LVQQQVPPFAM 88
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllNRLNDLIPGapdEGEVLLDGKDIYDLDVDVLELRRRVgMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVwhY----LMLHLHDKHSTALLTD-VAAAL---GLEDKLSR--HVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLD 158
Cdd:cd03260 96 SI--YdnvaYGLRLHGIKLKEELDErVEEALrkaALWDEVKDrlHALGLSGGQQQRLCLARAL-----ANEP--EVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 159 EPMSGLDVAQQAALDTLLSALSRKgIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQV 220
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-230 |
3.97e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.95 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLaRMAG--MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFA 87
Cdd:PRK10575 21 VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGrhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPV----------WHYlMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLL 157
Cdd:PRK10575 100 MTVrelvaigrypWHG-ALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ-------DSRCLLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 158 DEPMSGLDVAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-211 |
5.01e-28 |
|
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: 105.17 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEwSPVSLAHRRSYLVQQQVPPFAMPVWHYL 94
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGlLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 mlhlhdkhstalltdvaaalgledklsrhvsQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03230 95 -------------------------------KLSGGMKQRLALAQALL-----HDP--ELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 495776072 175 LLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:cd03230 137 LLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
25-230 |
9.70e-28 |
|
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: 106.44 E-value: 9.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAhRRSYLVQQQVPPfAMPVW-----------H 92
Cdd:TIGR03873 26 PGSLTGLLGPNGSGKSTLLRLLAGaLRPDAGTVDLAGVDLHGLSRRARA-RRVALVEQDSDT-AVPLTvrdvvalgripH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVAQQAAL 172
Cdd:TIGR03873 104 RSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQ-----EPK--LLLLDEPTNHLDVRAQLET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 173 DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:TIGR03873 177 LALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVY 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-229 |
9.91e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 110.38 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG----EGQIMLLEHTLAEWSPVSLAHRRSYLVQ----QQVPpfa 87
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggriSGEVLLDGRDLLELSEALRGRRIGMVFQdpmtQLNP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVWHYLM-----LHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMS 162
Cdd:COG1123 99 VTVGDQIAealenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL-----ALDP--DLLIADEPTT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 163 GLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARA 229
Cdd:COG1123 172 ALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-221 |
4.93e-27 |
|
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: 104.17 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslAHRR--SYLVQQQVPPFAMPVWH 92
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPDSGSILIDGEDVRKEPR---EARRqiGVLPDERGLYDRLTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YL----MLH-LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVA 167
Cdd:COG4555 94 NIryfaELYgLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH-----DP--KVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 168 QQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG4555 167 ARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-205 |
5.42e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.70 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGegqimllehTLAewspVSLAHRRSYLVQQQVPPFAMPV-- 90
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVlrpTSG---------TVR----RAGGARVAYVPQRSEVPDSLPLtv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 --------W-HYLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPM 161
Cdd:NF040873 75 rdlvamgrWaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ-------EADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495776072 162 SGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWL 205
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-230 |
2.70e-26 |
|
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: 102.26 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG-EGQIMLLEHTLAEWSPVSL-AHRR--SYLVQQQ--VPPF-- 86
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKGKALrQLRRqiGMIFQQFnlIERLsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 ----------AMPVWHYL--MLHLHDKH-STALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgR 153
Cdd:cd03256 96 lenvlsgrlgRRSTWRSLfgLFPKEEKQrALAALERV----GLLDKAYQRADQLSGGQQQRVAIARALMQ-----QP--K 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 154 MLLLDEPMSGLDVA-QQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQvLTPPNLARAY 230
Cdd:cd03256 165 LILADEPVASLDPAsSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-215 |
3.58e-26 |
|
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: 101.12 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEwSPVSLAHRRSYLVQQQVPPFAMPVWHYL-----MLHLHDKHST 104
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTpPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPNFTVREFLdyiawLKGIPSKEVK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 105 ALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGI 184
Cdd:cd03264 109 ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV-----GDP--SILIVDEPTAGLDPEERIRFRNLLSELGEDRI 181
|
170 180 190
....*....|....*....|....*....|.
gi 495776072 185 aVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03264 182 -VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-230 |
4.71e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.37 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPvslaHRR--SYLVQQQvPPFA-MPVWHYLMLH 97
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTALPP----AERpvSMLFQEN-NLFPhLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHD--KHSTALLTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQAAL 172
Cdd:COG3840 96 LRPglKLTAEQRAQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP-------ILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 173 DTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL--TPPNLARAY 230
Cdd:COG3840 169 LDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgEPPPALAAY 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-232 |
5.38e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 101.70 E-value: 5.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEgQIMLLEHTLAEWSPVSLAHRRSYL---VQQQVPPfAMP 89
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlppTYGN-DVRLFGERRGGEDVWELRKRIGLVspaLQLRFPR-DET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWH------YLMLHLHDKHS---TALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLA-AVIvqihpaGNPhgRMLLLDE 159
Cdd:COG1119 97 VLDvvlsgfFDSIGLYREPTdeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIArALV------KDP--ELLILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRKG-IAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNM 232
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGL 242
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-215 |
1.13e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.05 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQImllehtLAEWSPVSLAHRRS--YL--------- 78
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpDSGEV------LFDGKPLDIAARNRigYLpeerglypk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 79 --VQQQVPPFAmpvwhylmlHLHD-KHSTAL--LTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqIHpagNPhgR 153
Cdd:cd03269 85 mkVIDQLVYLA---------QLKGlKKEEARrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV--IH---DP--E 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 154 MLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-216 |
1.48e-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: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAewSPVSLAHRR-SYLVQQQVPPFAMPVWHYLMLH-- 97
Cdd:cd03263 24 NVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYINGYSIR--TDRKAARQSlGYCPQFDALFDELTVREHLRFYar 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 ---LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPHgrMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03263 102 lkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI-----GGPS--VLLLDEPTSGLDPASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495776072 175 LLSALsRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:cd03263 175 LILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-221 |
1.58e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 104.45 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQ-QVPP---- 85
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNpYLFAgtir 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 86 ----FAMP------VWHYLMLhlhdkhstALLTDVAAAL--GLEDKLSRHVSQLSGGEWQRVRLAAVIvqIHPAgnphgR 153
Cdd:COG4988 429 enlrLGRPdasdeeLEAALEA--------AGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALARAL--LRDA-----P 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 154 MLLLDEPMSGLDVAQQAALDTLLSALSrKGIAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-221 |
2.67e-25 |
|
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: 104.15 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFAMPVWHYLMLHlHDK 101
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLGLyEPTSGRILIDGIDLRQIDPASLRRQIGV-VLQDVFLFSGTIRENITLG-DPD 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 102 HSTALLTDVAAALGLEDKLSRHV-----------SQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQA 170
Cdd:COG2274 576 ATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLR-----NP--RILILDEATSALDAETEA 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495776072 171 ALDTLLSALsRKGIAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG2274 649 IILENLRRL-LKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
23-213 |
3.69e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAH-RRSYL--VQQQ---VPPF------AMP 89
Cdd:COG1136 31 IEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDGQDISSLSERELARlRRRHIgfVFQFfnlLPELtalenvALP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VwhyLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLA-AVIvqihpaGNPhgRMLLLDEPMSGLDVAQ 168
Cdd:COG1136 111 L---LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIArALV------NRP--KLILADEPTGNLDSKT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495776072 169 QAALDTLLSALSRK-GIAVVMSSHDLnHTLRHAHRVWLLSQGKMIA 213
Cdd:COG1136 180 GEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-225 |
7.56e-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: 98.34 E-value: 7.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAH--RRSYLVQQQVPPF-AMPVW 91
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPDSGEVLIDGEDISGLSEAELYRlrRRMGMLFQSGALFdSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 H--YLMLHLHDKHSTALLTDVA----AALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLD 165
Cdd:cd03261 96 EnvAFPLREHTRLSEEEIREIVleklEAVGLRGAEDLYPAELSGGMKKRVALARALA-LDP------ELLLYDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 166 VAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:cd03261 169 PIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-217 |
3.66e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYL--------------VQQQVppfA 87
Cdd:COG2884 25 IEKGEFVFLTGPSGAGKSTLLKLLYGEeRPTSGQVLVNGQDLSRLKRREIPYLRRRIgvvfqdfrllpdrtVYENV---A 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPvwhylmLHLHDKHSTALLTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLA-AVIvqihpaGNPhgRMLLLDEPMSG 163
Cdd:COG2884 102 LP------LRVTGKSRKEIRRRVREVLdlvGLSDKAKALPHELSGGEQQRVAIArALV------NRP--ELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 164 LDvaQQAALD--TLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTR 217
Cdd:COG2884 168 LD--PETSWEimELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-225 |
5.82e-24 |
|
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: 96.20 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRR---SYLVQQQvppfA---- 87
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPDSGEILVDGQDITGLSEKELYELRrriGMLFQGG----Alfds 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVWHYLMLHL--HDKHSTALLTDVA----AALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPM 161
Cdd:COG1127 97 LTVFENVAFPLreHTDLSEAEIRELVleklELVGLPGAADKMPSELSGGMRKRVALARAL-----ALDP--EILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 162 SGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:COG1127 170 AGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-230 |
1.17e-23 |
|
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: 95.30 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWsPVslaHRR-----SYLVQQQVPPFAMPVWH 92
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGQDITKL-PM---HKRarlgiGYLPQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLML-----HLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVA 167
Cdd:cd03218 95 NILAvleirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT-----NP--KFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 168 QQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-215 |
1.97e-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: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIML--LEHTLAEWS--PVSLAHRRSYL-----VQQQVPPFAMPvw 91
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFeTPQSGRVLIngVDVTAAPPAdrPVSMLFQENNLfahltVEQNVGLGLSP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 hylMLHLHDKHSTALlTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQAA 171
Cdd:cd03298 98 ---GLKLTAEDRQAI-EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP-------VLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495776072 172 LDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03298 167 MLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
23-215 |
2.92e-23 |
|
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: 94.11 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIMLLEHTLAEWSPVSLAHRRSYLvqQQVP--PFA-----MPVWHYL 94
Cdd:cd03257 28 IKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLSRRLRKIRRKEI--QMVFqdPMSslnprMTIGEQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 M--LHLHDKHSTALLTDVAAALGL------EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDV 166
Cdd:cd03257 106 AepLRIHGKLSKKEARKEAVLLLLvgvglpEEVLNRYPHELSGGQRQRVAIARAL-----ALNP--KLLIADEPTSALDV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495776072 167 AQQAA-LDTLLSALSRKGIAVVMSSHDLnHTLRH-AHRVWLLSQGKMIASG 215
Cdd:cd03257 179 SVQAQiLDLLKKLQEELGLTLLFITHDL-GVVAKiADRVAVMYAGKIVEEG 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-230 |
3.66e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVW---------H 92
Cdd:PRK09536 26 VREGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRqvvemgrtpH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQAAL 172
Cdd:PRK09536 106 RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP-------VLLLDEPTASLDINHQVRT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 173 DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:PRK09536 179 LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-229 |
3.98e-23 |
|
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: 95.94 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAE-----WSPVslaHRRS--YLVQQqvppfampvwHY 93
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGlERPDSGRIRLGGEVLQDsargiFLPP---HRRRigYVFQE----------AR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLHL-------------HDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLA-AVivqihpAGNPhgRMLLLDE 159
Cdd:COG4148 88 LFPHLsvrgnllygrkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGrAL------LSSP--RLLLMDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARA 229
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
4.44e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPP---FAMPV- 90
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDdqlFAPTVe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 ----WHYLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDV 166
Cdd:PRK13639 98 edvaFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL-----AMKP--EIIVLDEPTSGLDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 167 AQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMsfrRLDIEGH 242
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANL---RLPRVAH 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-210 |
5.19e-23 |
|
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: 91.68 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFAMPVWHYL 94
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIDGVDLRDLDLESLRKNIAY-VPQDPFLFSGTIRENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 mlhlhdkhstalltdvaaalgledklsrhvsqLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03228 97 --------------------------------LSGGQRQRIAIARALLR-----DP--PILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 495776072 175 LLSALsRKGIAVVMSSHDLnHTLRHAHRVWLLSQGK 210
Cdd:cd03228 138 ALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-160 |
7.60e-23 |
|
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: 90.78 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG-EGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYL 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 95 ML-----HLHDKHSTALLTDVAAALGLEDKLSRHV----SQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEP 160
Cdd:pfam00005 81 RLglllkGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLT-------KPKLLLLDEP 148
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
23-210 |
8.28e-23 |
|
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: 92.55 E-value: 8.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAH-RRSYL--VQQQ---VPPF------AMP 89
Cdd:cd03255 27 IEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELAAfRRRHIgfVFQSfnlLPDLtalenvELP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 vwhylmLHLHDKHSTALLTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLA-AVIvqihpaGNPhgRMLLLDEPMSGLD 165
Cdd:cd03255 107 ------LLLAGVPKKERRERAEELLervGLGDRLNHYPSELSGGQQQRVAIArALA------NDP--KIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495776072 166 VAQQAALDTLLSALSRK-GIAVVMSSHDLNhTLRHAHRVWLLSQGK 210
Cdd:cd03255 173 SETGKEVMELLRELNKEaGTTIVVVTHDPE-LAEYADRIIELRDGK 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-232 |
1.08e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.51 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 17 EPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVW---- 91
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQelva 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 -----HYLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDV 166
Cdd:PRK10253 104 rgrypHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-------ETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 167 AQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNM 232
Cdd:PRK10253 177 SHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-222 |
1.20e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIML--LEHTLAEWS--PVSLAHRRSYLvqqqvppFA-MPVWHYLML 96
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLngQDHTTTPPSrrPVSMLFQENNL-------FShLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HLH-----DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQAA 171
Cdd:PRK10771 95 GLNpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP-------ILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495776072 172 LDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLT 222
Cdd:PRK10771 168 MLTLVSQVCQeRQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
1.31e-22 |
|
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: 90.57 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSlahrrsylvqqqvppfampvwhyl 94
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlYKPDSGEILVDGKEVSFASPRD------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 mlhlhdkhstalltdvAAALGLEdklsrHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03216 72 ----------------ARRAGIA-----MVYQLSVGERQMVEIARAL-----ARNA--RLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495776072 175 LLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIAS 214
Cdd:cd03216 124 VIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-223 |
2.89e-22 |
|
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: 91.45 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIMLlehtlAEWSPVSLAHRRSYLVQQQVPPFAMP--VWHYLM---- 95
Cdd:TIGR03771 3 ADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKV-----AGASPGKGWRHIGYVPQRHEFAWDFPisVAHTVMsgrt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 --LHLHDKHSTALLTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVAQQA 170
Cdd:TIGR03771 78 ghIGWLRRPCVADFAAVRDALrrvGLTELADRPVGELSGGQRQRVLVARAL-----ATRP--SVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495776072 171 ALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSqGKMIASGTRDQVLTP 223
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQDP 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-230 |
3.74e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGR--LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRS--YLVQQQVPPF 86
Cdd:PRK10895 12 AYKGRrvVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGigYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMPVWHYLM--LHLHDKHSTALLTDVAAALGLE---DKLSRHVSQ-LSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEP 160
Cdd:PRK10895 92 RLSVYDNLMavLQIRDDLSAEQREDRANELMEEfhiEHLRDSMGQsLSGGERRRVEIARAL-----AANP--KFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 161 MSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-215 |
4.04e-22 |
|
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: 90.66 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPvslaHRR--SYLVQQqvppFAMpvWH 92
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGEILIDGRDVTGVPP----ERRniGMVFQD----YAL--FP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YL-----------MLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPM 161
Cdd:cd03259 86 HLtvaeniafglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR-----EP--SLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 162 SGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03259 159 SALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-251 |
8.81e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.10 E-value: 8.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLL-ARMAGMTAGEGQIMLLEHtlaewsPVSLAHRRS---YLVQQQVPPFAMPVW 91
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFkALMGFVRLASGKISILGQ------PTRQALQKNlvaYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 -----------HYLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEP 160
Cdd:PRK15056 97 vedvvmmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ-------QGQVILLDEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 161 MSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVwLLSQGKMIASGTRDQVLTPPNLARAYNMSFRRLDIE 240
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFSGVLRHVALN 248
|
250
....*....|.
gi 495776072 241 GHKMLISTGQE 251
Cdd:PRK15056 249 GSEESIITDDE 259
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-224 |
1.18e-21 |
|
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: 90.25 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMTAG-EGQIMLLEHTLAEWSPVSLAHRRSYLVQQqvpPFA-----MPVWHYLM 95
Cdd:COG1124 27 EVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKAFRRRVQMVFQD---PYAslhprHTVDRILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 --LHLHDK-HSTALLTDVAAALGL-EDKLSRHVSQLSGGEWQRVRLA-AVIVQihPagnphgRMLLLDEPMSGLDVAQQA 170
Cdd:COG1124 104 epLRIHGLpDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIArALILE--P------ELLLLDEPTSALDVSVQA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 171 ALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG1124 176 EILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-224 |
2.12e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVslaHRRS--YLVQqqvppfampvwHY-LMLHL 98
Cdd:COG1118 25 IASGELVALLGPSGSGKTTLLRIIAGLeTPDSGRIVLNGRDLFTNLPP---RERRvgFVFQ-----------HYaLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 -----------HDKHSTALLTDVAAAL-------GLEDklsRHVSQLSGGEWQRVRLA-AVIVQihPagnphgRMLLLDE 159
Cdd:COG1118 91 tvaeniafglrVRPPSKAEIRARVEELlelvqleGLAD---RYPSQLSGGQRQRVALArALAVE--P------EVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 160 PMSGLDVAQQAALDTLLSAL-SRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
23-210 |
2.37e-21 |
|
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: 87.63 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRS--YLVQQQVPPFAMPVWHYLMLhlh 99
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSILIDGEDLTDLEDELPPLRRRigMVFQDFALFPHLTVLENIAL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 dkhstalltdvaaalgledklsrhvsQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVAQQAALDTLLSAL 179
Cdd:cd03229 100 --------------------------GLSGGQQQRVALARALAM-----DPD--VLLLDEPTSALDPITRREVRALLKSL 146
|
170 180 190
....*....|....*....|....*....|..
gi 495776072 180 -SRKGIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:cd03229 147 qAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-221 |
2.53e-21 |
|
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: 92.52 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFAMPVWHYL 94
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFlDPQSGSITLGGVDLRDLDEDDLRRRIAV-VPQRPHLFDTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 ML--------HLHDKHSTALLTDVAAAL--GLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGL 164
Cdd:COG4987 430 RLarpdatdeELWAALERVGLGDWLAALpdGLDTWLGEGGRRLSGGERRRLALARALLRDAP-------ILLLDEPTEGL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 165 DVA-QQAALDTLLSALSRKgiAVVMSSHDLNHtLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG4987 503 DAAtEQALLADLLEALAGR--TVLLITHRLAG-LERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-221 |
2.94e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 88.65 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPvslaHRRSYLVQQQVPP----FA-MPVWHYLML 96
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPP----HERARAGIGYVPEgrriFPeLTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HLHDKHSTALLTDVAAALG----LEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGL--DVAQQa 170
Cdd:cd03224 99 GAYARRRAKRKARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARALM-----SRP--KLLLLDEPSEGLapKIVEE- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495776072 171 aLDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:cd03224 171 -IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
23-216 |
9.21e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.39 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLaRM-AGM-TAGEGQIMLLEHTLAEWSPvslaHRRsylvqqqvpPFAMpVW-HY-LMLHL 98
Cdd:COG3842 28 IEPGEFVALLGPSGCGKTTLL-RMiAGFeTPDSGRILLDGRDVTGLPP----EKR---------NVGM-VFqDYaLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 -----------HDKHSTALLTD-VAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSG 163
Cdd:COG3842 93 tvaenvafglrMRGVPKAEIRArVAELLelvGLEGLADRYPHQLSGGQQQRVALARALA-PEP------RVLLLDEPLSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 164 LDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:COG3842 166 LDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
25-210 |
1.97e-20 |
|
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: 85.77 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEhtlaEWSPVSLAHRRSYLVQQQVPP--FAMPVWHYLMLHLHDK 101
Cdd:cd03226 25 AGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNG----KPIKAKERRKSIGYVMQDVDYqlFTDSVREELLLGLKEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 102 H-STALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAALDTLLSALS 180
Cdd:cd03226 101 DaGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS-----GK--DLLIFDEPTSGLDYKNMERVGELIRELA 173
|
170 180 190
....*....|....*....|....*....|
gi 495776072 181 RKGIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:cd03226 174 AQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-225 |
2.76e-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: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVSlaHRRSYLVQQQVPPFAMPVWH---YLMLHL 98
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKniaYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 HDKHST--ALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLDVAQQAALDTLL 176
Cdd:cd03299 100 KVDKKEieRKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALV-VNP------KILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495776072 177 SALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:cd03299 173 KKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-211 |
5.17e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 85.15 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEW--SPVSLAHRRSYLVQQQvppfampvwH 92
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLrgRAIPYLRRKIGVVFQD---------F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLHDKHSTAL---LTD---------VAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLL 157
Cdd:cd03292 88 RLLPDRNVYENVAFaleVTGvppreirkrVPAALelvGLSHKHRALPAELSGGEQQRVAIARAIVN-----SP--TILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 158 DEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-192 |
6.12e-20 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 84.40 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRS---YLVQ---QQVppFAMP 89
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQrvgLVFQdpdDQL--FAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWH-----YLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGL 164
Cdd:TIGR01166 86 VDQdvafgPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAV-----AMRP--DVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*...
gi 495776072 165 DVAQQAALDTLLSALSRKGIAVVMSSHD 192
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
16-225 |
1.27e-19 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 84.21 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAewsPVSLAHRRSYLVQQQVPPFA-MPVWHY 93
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDIT---NLPPHKRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LM--LHLHDKHSTALLTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpagnPHGRMLLLDEPMSGLDVAQ 168
Cdd:cd03300 93 IAfgLRLKKLPKAEIKERVAEALdlvQLEGYANRKPSQLSGGQQQRVAIARALV-------NEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 169 QAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:cd03300 166 RKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
23-216 |
1.48e-19 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 85.52 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMLLEHTlaewSPVSLAHRRSYLVQQQVPPF-AMPVWHYLMLH- 97
Cdd:TIGR01188 16 VREGEVFGFLGPNGAGKTTTIRMLTTLlrpTSGTARVAGYDVV----REPRKVRRSIGIVPQYASVDeDLTGRENLEMMg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 --------LHDKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLDVAQQ 169
Cdd:TIGR01188 92 rlyglpkdEAEERAEELLELF----ELGEAADRPVGTYSGGMRRRLDIAASLI-HQP------DVLFLDEPTTGLDPRTR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGT 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
23-210 |
1.55e-19 |
|
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: 83.84 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslAHRRSYLVQQQvppFA----MPVWHYLMLH 97
Cdd:cd03301 23 IADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYIGGRDVTDLPP---KDRDIAMVFQN---YAlyphMTVYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHDKHS-----TALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDVAQQAAL 172
Cdd:cd03301 97 LKLRKVpkdeiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIV-----REP--KVFLMDEPLSNLDAKLRVQM 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 495776072 173 DTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:cd03301 170 RAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-224 |
2.27e-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: 83.78 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRR--------------SYLVQ 80
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGTDLTLLSGKELRKARrrigmifqhfnllsSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 81 QQVpPFAMPVWHYLMLHLHDKhSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEP 160
Cdd:cd03258 101 ENV-ALPLEIAGVPKAEIEER-VLELLELV----GLEDKADAYPAQLSGGQKQRVGIARAL-----ANNPK--VLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 161 MSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:cd03258 168 TSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-209 |
4.58e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.22 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLaRM-AG-MTAGEGQIMLLEHTLAEWSPvslahRRSYLVQQqvppFA-MP--- 89
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLL-RLiAGlEKPTSGEVLVDGKPVTGPGP-----DRGVVFQE----PAlLPwlt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWHYLMLHLHDKH-STALLTDVAAAL----GLEDKLSRHVSQLSGGEWQRVRLA-AVIVQihPagnphgRMLLLDEPMSG 163
Cdd:COG1116 97 VLDNVALGLELRGvPKAERRERARELlelvGLAGFEDAYPHQLSGGMRQRVAIArALAND--P------EVLLMDEPFGA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495776072 164 LDVAQQAAL-DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQG 209
Cdd:COG1116 169 LDALTRERLqDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-230 |
5.59e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWsPVslaHRR-----SYLVQQqvppfA-----MPVW 91
Cdd:COG1137 26 VNQGEIVGLLGPNGAGKTTTFYMIVGLvKPDSGRIFLDGEDITHL-PM---HKRarlgiGYLPQE-----AsifrkLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYLM--LHLHDKHST-------ALLTDvaaaLGLEDKLSRHVSQLSGGEWQRVRLA-AVivqihpAGNPhgRMLLLDEPM 161
Cdd:COG1137 97 DNILavLELRKLSKKereerleELLEE----FGITHLRKSKAYSLSGGERRRVEIArAL------ATNP--KFILLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 162 SGLD---VA--QQaaldtLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:COG1137 165 AGVDpiaVAdiQK-----IIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVY 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-226 |
7.85e-19 |
|
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: 84.01 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWS-PVSL-AHRR--SYLVQQqvppfAMPVWH----- 92
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNGRTLFDSRkGIFLpPEKRriGYVFQE-----ARLFPHlsvrg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 ---YLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQ 169
Cdd:TIGR02142 95 nlrYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLS-----SP--RLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 170 AALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNL 226
Cdd:TIGR02142 168 YEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-230 |
1.11e-18 |
|
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: 81.95 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQ--QVppFA-MPVWHYLML-- 96
Cdd:COG0410 26 VEEGEIVALLGRNGAGKTTLLKAISGLLpPRSGSIRFDGEDITGLPPHRIARLGIGYVPEgrRI--FPsLTVEENLLLga 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 -HLHDKHSTAllTDVAAALG----LEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGL------D 165
Cdd:COG0410 104 yARRDRAEVR--ADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALM-----SRP--KLLLLDEPSLGLapliveE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 166 VAQqaaldtLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:COG0410 175 IFE------IIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-224 |
2.10e-18 |
|
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: 83.97 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYL--VQQQvpPFA-----MPVWHYL 94
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMqvVFQD--PFGslsprMTVGQII 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 M--LHLHDKHSTALLTD--VAAAL---GL-EDKLSRHVSQLSGGEWQRVRLA-AVIVQihpagnPhgRMLLLDEPMSGLD 165
Cdd:COG4172 386 AegLRVHGPGLSAAERRarVAEALeevGLdPAARHRYPHEFSGGQRQRIAIArALILE------P--KLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 166 VAQQAALDTLLSALSRK-GIAVVMSSHDLnHTLRH-AHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG4172 458 VSVQAQILDLLRDLQREhGLAYLFISHDL-AVVRAlAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-224 |
4.05e-18 |
|
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: 80.42 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLaRMAG--MTAGEGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFA-MPVWHYLML--- 96
Cdd:cd03295 24 IAKGEFLVLIGPSGSGKTTTM-KMINrlIEPTSGEIFIDGEDIREQDPVELRRKIGY-VIQQIGLFPhMTVEENIALvpk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 ------HLHDKHSTALLTDVaaalGLEDK--LSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVAQ 168
Cdd:cd03295 102 llkwpkEKIRERADELLALV----GLDPAefADRYPHELSGGQQQRVGVARAL-----AADP--PLLLMDEPFGALDPIT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 169 QAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:cd03295 171 RDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-207 |
4.17e-18 |
|
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: 79.82 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslahRRSYLVQQqvpPFAMP---VW 91
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVDGEPVTGPGP-----DRGYVFQQ---DALLPwltVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYLMLHL-HDKHSTALLTDVAAAL----GLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDV 166
Cdd:cd03293 92 DNVALGLeLQGVPKAEARERAEELlelvGLSGFENAYPHQLSGGMRQRVALARALAV-----DP--DVLLLDEPFSALDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495776072 167 AQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLS 207
Cdd:cd03293 165 LTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-236 |
4.40e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 80.77 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQImllehtlaEWSPVSlAHRRSYLVQQQVPPFAMPVWHY-LMLH 97
Cdd:cd03294 46 DVREGEIFVIMGLSGSGKSTLLRCINRLiepTSGKVLI--------DGQDIA-AMSRKELRELRRKKISMVFQSFaLLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHDKHSTALLTDVA---------------AALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEPMS 162
Cdd:cd03294 117 RTVLENVAFGLEVQgvpraereeraaealELVGLEGWEHKYPDELSGGMQQRVGLARAL-----AVDPD--ILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 163 GLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPnlARAYNMSFRR 236
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP--ANDYVREFFR 262
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-215 |
4.48e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 79.65 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSL---AHRR--SYLVQQQVPPFAMPVWH---YLMLH 97
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlpPQQRkiGLVFQQYALFPHLNVREnlaFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVAQQAALDTLL- 176
Cdd:cd03297 103 KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARAL-----AAQP--ELLLLDEPFSALDRALRLQLLPELk 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 495776072 177 SALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-221 |
6.41e-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: 82.49 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYLvQQQVPPFAMPVwhylmlh 97
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwPPTAGSVRLDGADLSQWDREELGRHIGYL-PQDVELFDGTI------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 lhdKHSTALLTD------VAAA---------LGLED----KLSRHVSQLSGGEWQRVRLA-AVivqihpAGNPhgRMLLL 157
Cdd:COG4618 423 ---AENIARFGDadpekvVAAAklagvhemiLRLPDgydtRIGEGGARLSGGQRQRIGLArAL------YGDP--RLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 158 DEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-225 |
6.54e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAewspvslahrrsylvqqQVPPFAMPV-----WHYLML 96
Cdd:PRK11607 42 IYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLS-----------------HVPPYQRPInmmfqSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HL-----------HDKHSTALLTD-VAAALGL---EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPM 161
Cdd:PRK11607 105 HMtveqniafglkQDKLPKAEIASrVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSL-----AKRP--KLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 162 SGLDVAQQAALD-TLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:PRK11607 178 GALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-168 |
7.10e-18 |
|
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: 80.14 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEgqimllehtlAEWSPVSLahrrSYLVQQQVPPFAMPVW 91
Cdd:cd03237 14 TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVlkpDEGD----------IEIELDTV----SYKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 92 HYLMLHLHDKHSTALL-TDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihPAGnphgrMLLLDEPMSGLDVAQ 168
Cdd:cd03237 80 DLLSSITKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSK--DAD-----IYLLDEPSAYLDVEQ 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-221 |
1.23e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 81.75 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKST---LLARMagMTAGEGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFAMPVWHYLMLHLH 99
Cdd:COG1132 363 IPPGETVALVGPSGSGKSTlvnLLLRF--YDPTSGRILIDGVDIRDLTLESLRRQIGV-VPQDTFLFSGTIRENIRYGRP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 DkhstALLTDVAAAL----------GLEDKLSRHVSQ----LSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLD 165
Cdd:COG1132 440 D----ATDEEVEEAAkaaqahefieALPDGYDTVVGErgvnLSGGQRQRIAIARALLK-----DP--PILILDEATSALD 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 166 V----AQQAALDTLlsalsRKGIAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG1132 509 TeteaLIQEALERL-----MKGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-215 |
2.34e-17 |
|
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: 78.53 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMllehTLAEWSPVSLAHRRSYLV--QQQVPPFAMPV 90
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlqpTSGEVRVA----GLVPWKRRKKFLRRIGVVfgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 WHYLMLHLH-----DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqIHpagNPhgRMLLLDEPMSGLD 165
Cdd:cd03267 113 IDSFYLLAAiydlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAAL--LH---EP--EILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495776072 166 VAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03267 186 VVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-229 |
2.70e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKST---LLARMAGMTAgeGQIMLLEHTLAEWSPVSLaHRRSYLVQQQVPPFAMPVWH 92
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTG--GQVLLDGVPLVQYDHHYL-HRQVALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLhDKHSTALLTDVAAALGLEDKLSR-----------HVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPM 161
Cdd:TIGR00958 574 NIAYGL-TDTPDEEIMAAAKAANAHDFIMEfpngydtevgeKGSQLSGGQKQRIAIARALVR-----KP--RVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 162 SGLDVAQQAALDTLlsaLSRKGIAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARA 229
Cdd:TIGR00958 646 SALDAECEQLLQES---RSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-206 |
5.15e-17 |
|
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: 79.64 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQqvpPFAMP--VW 91
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH---PFLFAgtIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYLMLHLHDKHSTAL--------LTDVAAAL--GLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPM 161
Cdd:TIGR02857 414 ENIRLARPDASDAEIrealeragLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP-------LLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495776072 162 SGLDVAQQAALDTLLSALSRkGIAVVMSSHDLnHTLRHAHRVWLL 206
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ-GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-218 |
5.52e-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: 77.09 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYLV----Q--QQVPpfAM 88
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGQDLFALDEDARARLRARHVgfvfQsfQLLP--TL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYLMLHLH---DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLA-AVIVQihPAgnphgrMLLLDEPMSGL 164
Cdd:COG4181 106 TALENVMLPLElagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALArAFATE--PA------ILFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 165 DVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRhAHRVWLLSQGKMIASGTRD 218
Cdd:COG4181 178 DAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
23-215 |
6.14e-17 |
|
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: 76.49 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVsLAHRRSYLvqqQVPPF--AMPVWHYLMLHL- 98
Cdd:cd03268 23 VKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGKSYQKNIEA-LRRIGALI---EAPGFypNLTARENLRLLAr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 -----HDKHSTALLTdvaaaLGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPHgrMLLLDEPMSGLDVAQQAALD 173
Cdd:cd03268 99 llgirKKRIDEVLDV-----VGLKDSAKKKVKGFSLGMKQRLGIALALL-----GNPD--LLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495776072 174 TLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03268 167 ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-194 |
9.59e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.98 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG----EGQIMLLEHTLAEWSPvslAHRRSYLVQQQVPPFA-MPV 90
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsaSGEVLLNGRRLTALPA---EQRRIGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 WHYLMLHLHDKHSTALLTD-VAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIVQiHPagnphgRMLLLDEPMSGLDV 166
Cdd:COG4136 94 GENLAFALPPTIGRAQRRArVEQALeeaGLAGFADRDPATLSGGQRARVALLRALLA-EP------RALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*....
gi 495776072 167 AQQAALDTL-LSALSRKGIAVVMSSHDLN 194
Cdd:COG4136 167 ALRAQFREFvFEQIRQRGIPALLVTHDEE 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-216 |
9.71e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGEgqIMLLEHTlaewsPVslAHRRSYLVQ--------QQVPpFAMPVW 91
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLTGIlvpTSGE--VRVLGYV-----PF--KRRKEFARRigvvfgqrSQLW-WDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYLMLH--LHD------KHSTALLTDVaaaLGLEDKLSRHVSQLSGGewQRVR--LAAVIvqIHpagNPhgRMLLLDEPM 161
Cdd:COG4586 115 DSFRLLkaIYRipdaeyKKRLDELVEL---LDLGELLDTPVRQLSLG--QRMRceLAAAL--LH---RP--KILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 162 SGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-219 |
1.03e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLA-----RMAGMTaGEGQIMLLEHTLAEWSpvslAHRRSYLVQQQ---V 83
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNalafrSPKGVK-GSGSVLLNGMPIDAKE----MRAISAYVQQDdlfI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 84 PpfAMPVWHYLMLHLH---DKHST-----ALLTDVAAALGLED------KLSRHVSQLSGGEWQRVRLAAVIVQihpagN 149
Cdd:TIGR00955 112 P--TLTVREHLMFQAHlrmPRRVTkkekrERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLT-----D 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 150 PHgrMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTL-RHAHRVWLLSQGKMIASGTRDQ 219
Cdd:TIGR00955 185 PP--LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-219 |
1.10e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTAG----EGQIMLLEHTLAEWSPVSLAHRRS-----YLVQQ-----------Q 82
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGdksaGSHIELLGRTVQREGRLARDIRKSrantgYIFQQfnlvnrlsvleN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 83 VPPFAM---PVWHYLM---LHLHDKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLL 156
Cdd:PRK09984 107 VLIGALgstPFWRTCFswfTREQKQRALQALTRV----GMVHFAHQRVSTLSGGQQQRVAIARALMQ-------QAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 157 LDEPMSGLDV-AQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQ 219
Cdd:PRK09984 176 ADEPIASLDPeSARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-215 |
1.26e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 75.87 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSlAHRRSYLVQQQVPPFA-MPVW----HYLMLH-LH 99
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRLGFVSDSTGLYDrLTARenleYFAGLYgLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqiHPAGNphgrmLLLDEPMSGLDVAQQAALDTLLSAL 179
Cdd:cd03266 110 GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV--HDPPV-----LLLDEPTTGLDVMATRALREFIRQL 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 495776072 180 SRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03266 183 RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-215 |
1.74e-16 |
|
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: 75.70 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYlVQQQVPPFAMP 89
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDIRQLDPADLRRNIGY-VPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWHYLMLHLHDkHSTALLTDVAAALGLEDKLSRHV-----------SQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLD 158
Cdd:cd03245 94 LRDNITLGAPL-ADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLN-----DP--PILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 159 EPMSGLDVAQQAALDTLLSALsRKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
19-219 |
2.08e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 75.51 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEgqIMLLEHtlaEWSPVSLaHRRSYLVQQqvPPF--------A 87
Cdd:TIGR03740 19 ISLTVPKNSVYGLLGPNGAGKSTLLKMITGIlrpTSGE--IIFDGH---PWTRKDL-HKIGSLIES--PPLyenltareN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVwHYLMLHLHDKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIVQiHPagnphgRMLLLDEPMSGLDVA 167
Cdd:TIGR03740 91 LKV-HTTLLGLPDSRIDEVLNIV----DLTNTGKKKAKQFSLGMKQRLGIAIALLN-HP------KLLILDEPTNGLDPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495776072 168 QQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQ 219
Cdd:TIGR03740 159 GIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-221 |
2.79e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 75.27 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKST---LLARMAGMTagEGQIMLLEHTLAEwspVSLAHRRSY--LVQQQVPPFAMPVWHYLMLH 97
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTvvsLLERFYDPT--SGEILLDGVDIRD---LNLRWLRSQigLVSQEPVLFDGTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHDKHSTallTDVAAA---------LGLEDKLSRHV----SQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGL 164
Cdd:cd03249 101 KPDATDE---EVEEAAkkanihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLR-----NP--KILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 165 DVAQ----QAALDTLlsalsRKGIAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:cd03249 171 DAESeklvQEALDRA-----MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-193 |
3.60e-16 |
|
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: 75.48 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLArmagMTAGEGQIMLLEHT-LAEWSPVSLAHRRSYL-------VQQQVPPFAMPvwHYLML- 96
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALK----ILAGKLKPNLGKFDdPPDWDEILDEFRGSELqnyftklLEGDVKVIVKP--QYVDLi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 ----------HLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDV 166
Cdd:cd03236 100 pkavkgkvgeLLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALAR-------DADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 495776072 167 AQQAALDTLLSALSRKGIAVVMSSHDL 193
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-215 |
3.78e-16 |
|
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: 74.12 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE---GQIMLLEHTLAEWSPvslaHRRSYLVQQQvppfampvwhyLM 95
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvsGEVLINGRPLDKRSF----RKIIGYVPQD-----------DI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 LHLHdkhstalLTdVAAALgledKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVAQQAALDTL 175
Cdd:cd03213 93 LHPT-------LT-VRETL----MFAAKLRGLSGGERKRVSIALELVS-----NPS--LLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495776072 176 LSALSRKGIAVVMSSHDLNHTLRHA-HRVWLLSQGKMIASG 215
Cdd:cd03213 154 LRRLADTGRTIICSIHQPSSEIFELfDKLLLLSQGRVIYFG 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
23-226 |
3.95e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.52 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIML----LEHTLAEwspvslaHRRSYLVQQQVPPFA-MPVWHYLML 96
Cdd:PRK09452 37 INNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLdgqdITHVPAE-------NRHVNTVFQSYALFPhMTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HLHDKHSTA--LLTDVAAALG---LEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAA 171
Cdd:PRK09452 110 GLRMQKTPAaeITPRVMEALRmvqLEEFAQRKPHQLSGGQQQRVAIARAVVN-----KP--KVLLLDESLSALDYKLRKQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 172 LDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT-RDQVLTPPNL 226
Cdd:PRK09452 183 MQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTpREIYEEPKNL 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-234 |
5.30e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.16 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHtlaEWSPVSLAHRRSY--LVQQ----QVppFAMPVWH-----YLMLHL 98
Cdd:PRK13647 36 LLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGR---EVNAENEKWVRSKvgLVFQdpddQV--FSSTVWDdvafgPVNMGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 HDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVAQQAALDTLLSA 178
Cdd:PRK13647 111 DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL-----AMDP--DVIVLDEPMAYLDPRGQETLMEILDR 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 179 LSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRdQVLTPPNLARAYNMSF 234
Cdd:PRK13647 184 LHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRL 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-216 |
9.66e-16 |
|
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: 73.56 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKST---LLARMAGMTAGEGQIMLLEhtlAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYLMLH-- 97
Cdd:cd03265 23 VRRGEIFGLLGPNGAGKTTtikMLTTLLKPTSGRATVAGHD---VVREPREVRRRIGIVFQDLSVDDELTGWENLYIHar 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 ---LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQiHPagnphgRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03265 100 lygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH-RP------EVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495776072 175 LLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:cd03265 173 YIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-211 |
1.08e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEW--SPVSLAHRRSYLVQQQvppfampvwH 92
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIWFSGHDITRLknREVPFLRRQIGMIFQD---------H 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLH--LHDKHSTALLTD----------VAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIVQiHPAgnphgrMLLL 157
Cdd:PRK10908 89 HLLMDrtVYDNVAIPLIIAgasgddirrrVSAALdkvGLLDKAKNFPIQLSGGEQQRVGIARAVVN-KPA------VLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 158 DEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-221 |
1.17e-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: 73.80 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKST---LLARMAGMTagEGQIMLLEHTLAEwspVSLAHRRSY--LVQQQVPPFAMPV 90
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTlvnLIPRFYDVD--SGRILIDGHDVRD---YTLASLRRQigLVSQDVFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 WHYLMLHLHDkhstALLTDVAAAL--------------GLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLL 156
Cdd:cd03251 93 AENIAYGRPG----ATREEVEEAAraanahefimelpeGYDTVIGERGVKLSGGQRQRIAIARALLK-----DP--PILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 157 LDEPMSGLDV----AQQAALDTLLSalSRKGIAVvmsSHDLNhTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:cd03251 162 LDEATSALDTeserLVQAALERLMK--NRTTFVI---AHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
16-216 |
1.22e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.11 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLaRM-AG-MTAGEGQIMLLEHTLAEWSPvslAHRRSYLVQQQvppFAmpvwhy 93
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLL-RMiAGlEDPTSGEILIGGRDVTDLPP---KDRNIAMVFQS---YA------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLHL--------------HDKHS-TALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLD 158
Cdd:COG3839 86 LYPHMtvyeniafplklrkVPKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR-----EP--KVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 159 EPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-227 |
1.54e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLA---RMAGMTAG---EGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVP 84
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRtlnRMNDKVSGyrySGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 PFAMPVWHYLMLHLHDKH----------STALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRM 154
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKlvprkefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL-----AVNP--EV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 155 LLLDEPMSGLDVAQQAALDTLLSALSRKgIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLA 227
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-191 |
1.62e-15 |
|
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: 72.53 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYLMLhLHDK 101
Cdd:cd03231 22 TLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF-WHAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 102 HSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALDTLLSALSR 181
Cdd:cd03231 101 HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLS-------GRPLWILDEPTTALDKAGVARFAEAMAGHCA 173
|
170
....*....|
gi 495776072 182 KGIAVVMSSH 191
Cdd:cd03231 174 RGGMVVLTTH 183
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-229 |
1.93e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.10 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEwSPVSLAHRRSYL--VQQQVPPFA-MPVWHYL 94
Cdd:COG1126 20 ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTITVDGEDLTD-SKKDINKLRRKVgmVFQQFNLFPhLTVLENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 ML---HLHdKHSTALLTDVAAAL----GLEDKLSRHVSQLSGGEWQRVRLA-AVivqihpAGNPhgRMLLLDEPMSGLD- 165
Cdd:COG1126 99 TLapiKVK-KMSKAEAEERAMELlervGLADKADAYPAQLSGGQQQRVAIArAL------AMEP--KVMLFDEPTSALDp 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 166 -----VaqqaaLDTLLSaLSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARA 229
Cdd:COG1126 170 elvgeV-----LDVMRD-LAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-224 |
2.12e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-------AGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQ 82
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 83 VPPFAMPVWHYLMLHLHD------KHSTALLTDVAAALGL----EDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphg 152
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKShgikekREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALA-LKP------ 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 153 RMLLLDEPMSGLDVAQQAALDTLLSALsRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-222 |
2.19e-15 |
|
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: 73.62 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLlARM--AGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQ------------ 81
Cdd:TIGR04520 18 LKNVSLSIEKGEFVAIIGHNGSGKSTL-AKLlnGLLLPTSGKVTVDGLDTLDEENLWEIRKKVGMVFQnpdnqfvgatve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 82 ----------QVPPFAMPvwhylmlhlhdkhstALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPh 151
Cdd:TIGR04520 97 ddvafglenlGVPREEMR---------------KRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL-----AMRP- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 152 gRMLLLDEPMSGLD-VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLrHAHRVWLLSQGKMIASGTRDQVLT 222
Cdd:TIGR04520 156 -DIIILDEATSMLDpKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFS 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
26-224 |
2.24e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.42 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAG-MTAGEGQIM--LLEHTLAEWSPVSLAHRRSYL------VQQ--------QVPPFAm 88
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSArLAPDAGEVHyrMRDGQLRDLYALSEAERRRLLrtewgfVHQhprdglrmQVSAGG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYLML----HLHDKHSTAL--LTDVAAALGLEDKLSRhvsQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMS 162
Cdd:PRK11701 111 NIGERLMAvgarHYGDIRATAGdwLERVEIDAARIDDLPT---TFSGGMQQRLQIARNLV-THP------RLVFMDEPTG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 163 GLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDP 243
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-169 |
2.95e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQimllehtlaewspVSLAHRRSYLVQQQVPPFAMPVWHY 93
Cdd:PRK13409 354 SLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDEGE-------------VDPELKISYKPQYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 94 LMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQ 169
Cdd:PRK13409 421 LRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSR-------DADLYLLDEPSAHLDVEQR 489
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-231 |
3.23e-15 |
|
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: 72.37 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLlehTLAEWSPVSLAHRRSYLVQQQVPPFA-MPVWHYLMLHLHDKH- 102
Cdd:cd03296 28 GELVALLGPSGSGKTTLLRLIAGLeRPDSGTILF---GGEDATDVPVQERNVGFVFQHYALFRhMTVFDNVAFGLRVKPr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 103 ----STALLTDVAAAL----GLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03296 105 serpPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALA-VEP------KVLLLDEPFGALDAKVRKELRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 175 LLSAL-SRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYN 231
Cdd:cd03296 178 WLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-224 |
3.95e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 1 MSLLMQLTDVA----EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLaewspvslahRRS 76
Cdd:PRK09544 1 MTSLVSLENVSvsfgQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL----------RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 77 YLVQQQV--PPFAMPVWHYLMLHLHDKHSTAL--LTDVAAALGLEDKLSRhvsqLSGGEWQRVRLAAVIVQihpagnpHG 152
Cdd:PRK09544 71 YVPQKLYldTTLPLTVNRFLRLRPGTKKEDILpaLKRVQAGHLIDAPMQK----LSGGETQRVLLARALLN-------RP 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 153 RMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQgKMIASGTRDQVLTPP 224
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-238 |
4.05e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQImLLEHTLAEWSPVSLAHRRS-YLVQQQ---VPpfAMPVWHYLMLH 97
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGVyQPDSGEI-LLDGEPVRFRSPRDAQAAGiAIIHQElnlVP--NLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 --------LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQ 169
Cdd:COG1129 104 reprrgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR-------DARVLILDEPTASLTEREV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQvLTPPNLARAynMSFRRLD 238
Cdd:COG1129 177 ERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE-LTEDELVRL--MVGRELE 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-230 |
4.91e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGEgqIMLLEHTLAEWSPVSLAhrRSYLVQ--QQVPPF-AMPVWHYLML 96
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFykpTGGT--ILLRGQHIEGLPGHQIA--RMGVVRtfQHVRLFrEMTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HLHDKHSTALLT----------------DVAA----ALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLL 156
Cdd:PRK11300 104 AQHQQLKTGLFSgllktpafrraesealDRAAtwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVT-----QP--EILM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 157 LDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAY 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-228 |
5.44e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.91 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslAHRRSY---LVQQQ---VPPFamPVWHYLM 95
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGLyQPDSGEILIDGKPVRIRSP---RDAIALgigMVHQHfmlVPNL--TVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 LHLHDKHSTAL--------LTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVA 167
Cdd:COG3845 103 LGLEPTKGGRLdrkaararIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR-----GA--RILILDEPTAVLTPQ 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 168 QQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVlTPPNLAR 228
Cdd:COG3845 176 EADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET-SEEELAE 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-210 |
8.63e-15 |
|
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: 69.40 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQImllehtlaewspvslahrrsylvqqqvppfampvwhyl 94
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIV-------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 mlHLHDKHSTAlltdvaaalgledklsrHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03221 58 --TWGSTVKIG-----------------YFEQLSGGEKMRLALAKLLLE-----NPN--LLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 495776072 175 LLSALSRkgiAVVMSSHD---LNHTlrhAHRVWLLSQGK 210
Cdd:cd03221 112 ALKEYPG---TVILVSHDryfLDQV---ATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-212 |
1.09e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIML----------------LEHTLAEWspVSLAHRRSYL 78
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPDSGEVSIpkglrigylpqeppldDDLTVLDT--VLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 79 VQQQ---------VPPFAMPVWHYLMLHLHDKHSTALLTDVAAAL-GL---EDKLSRHVSQLSGGEWQRVRLAAVIVQih 145
Cdd:COG0488 92 LEAEleeleaklaEPDEDLERLAELQEEFEALGGWEAEARAEEILsGLgfpEEDLDRPVSELSGGWRRRVALARALLS-- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 146 pagNPHgrMLLLDEPMSGLDVAQQAALDTLLSalSRKGiAVVMSSHD---LNHTlrhAHRVWLLSQGKMI 212
Cdd:COG0488 170 ---EPD--LLLLDEPTNHLDLESIEWLEEFLK--NYPG-TVLVVSHDryfLDRV---ATRILELDRGKLT 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
23-210 |
1.42e-14 |
|
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: 70.25 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIML----LEHTLAEWSPVslahrRSYL--VQQQVPPFA-MPVWHYL 94
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTIIIdglkLTDDKKNINEL-----RQKVgmVFQQFNLFPhLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHL----------HDKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEPMSGL 164
Cdd:cd03262 98 TLAPikvkgmskaeAEERALELLEKV----GLADKADAYPAQLSGGQQQRVAIARAL-----AMNPK--VMLFDEPTSAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495776072 165 D---VAQqaALDTLLSaLSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:cd03262 167 DpelVGE--VLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-193 |
1.72e-14 |
|
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: 72.51 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 21 GAVNAGEILHLVGPNGAGKSTllarMAGMTAGEgqimlLEHTLAEwspVSLAHRRSYLVQQQVPPFAMPVWHYLMLHLHD 100
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTT----FAKILAGV-----LKPDEGE---VDEDLKISYKPQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 101 KHSTALL-TDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihPAGnphgrMLLLDEPMSGLDVAQQAALDTLLSAL 179
Cdd:COG1245 429 DFGSSYYkTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR--DAD-----LYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170
....*....|....*
gi 495776072 180 SR-KGIAVVMSSHDL 193
Cdd:COG1245 502 AEnRGKTAMVVDHDI 516
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-221 |
1.84e-14 |
|
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: 69.86 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMLLEHTLAEWSPVSLAhRRSYLVQQQVPPf 86
Cdd:cd03217 10 VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyEVTEGEILFKGEDITDLPPEERA-RLGIFLAFQYPP- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMPvwhylmlhlhdkhstalltdvaaALGLEDKLsRHVSQ-LSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLD 165
Cdd:cd03217 88 EIP-----------------------GVKNADFL-RYVNEgFSGGEKKRNEILQLLLL-----EP--DLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 166 VAQQAALDTLLSALSRKGIAVVMSSHD---LNHTlrHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHYqrlLDYI--KPDRVHVLYDGRIVKSGDKELAL 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-215 |
2.02e-14 |
|
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: 69.99 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG----EGQIMLLEHtlaEWSPVSLAHRRSYLVQQQ--VPPF-AMPVW 91
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttSGQILFNGQ---PRKPDQFQKCVAYVRQDDilLPGLtVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HY-LMLHLHDKHSTALLTDVAAALGLEDKLSRHV-----SQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLD 165
Cdd:cd03234 103 TYtAILRLPRKSSDAIRKKRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLW-----DP--KVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 166 VAQQAALDTLLSALSRKGIAVVMSSH----DLnhtLRHAHRVWLLSQGKMIASG 215
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-194 |
2.78e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 7 LTDVaekgrLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRS------YLV 79
Cdd:PRK11629 21 QTDV-----LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAELRNqklgfiYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 80 QQQVPPF------AMPVwhyLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgR 153
Cdd:PRK11629 96 HHLLPDFtalenvAMPL---LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN-----NP--R 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495776072 154 MLLLDEPMSGLDVAQQAALDTLLSALS-RKGIAVVMSSHDLN 194
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQ 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-215 |
2.98e-14 |
|
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: 68.49 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSpvslAHRRSYL--VQQQVppfampvwhylmlHLH 99
Cdd:cd03247 25 LKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE----KALSSLIsvLNQRP-------------YLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 DkhsTALLTDVAAalgledklsrhvsQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLD-VAQQAALDTLLSA 178
Cdd:cd03247 88 D---TTLRNNLGR-------------RFSGGERQRLALARILLQDAP-------IVLLDEPTVGLDpITERQLLSLIFEV 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 495776072 179 LsrKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03247 145 L--KDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-220 |
3.44e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 33 GPNGAGKSTLLARMAGMT-AGEGQIMLLEHTL--AEwSPVSLA--HRRSYLVQQQVPPFAmpvwHY-LMLHLH---DKHS 103
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTrPQKGRIVLNGRVLfdAE-KGICLPpeKRRIGYVFQDARLFP----HYkVRGNLRygmAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 104 TALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLaavivqihpagnphGR-------MLLLDEPMSGLDVAQQAALDTLL 176
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAI--------------GRalltapeLLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495776072 177 SALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQV 220
Cdd:PRK11144 172 ERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-211 |
5.55e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 67.63 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQqqvppfamp 89
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 vwhylmlhlhdkhstalltdvaaalglEDKL-SRHVSQ--LSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDV 166
Cdd:cd03246 84 ---------------------------DDELfSGSIAEniLSGGQRQRLGLARALY-----GNP--RILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495776072 167 AQQAALDTLLSALSRKGIAVVMSSHDLNhTLRHAHRVWLLSQGKM 211
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
5.75e-14 |
|
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: 67.84 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 4 LMQLTDVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSP-VSLAHRRSYlvqq 81
Cdd:cd03215 4 VLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRSPrDAIRAGIAY---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 82 qVPpfampvwhylmlhlHDKHSTALLTD--VAAALGLEdklsrhvSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDE 159
Cdd:cd03215 80 -VP--------------EDRKREGLVLDlsVAENIALS-------SLLSGGNQQKVVLARWL-----ARDP--RVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-215 |
6.34e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.24 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIMLLEHTLAewSPVSLAHRRSYLVQQ---QVPPFAmpVWHYLMLH- 97
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVP--ARARLARARIGVVPQfdnLDLEFT--VRENLLVFg 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 ----LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVAQQAALD 173
Cdd:PRK13536 140 ryfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN-----DPQ--LLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495776072 174 TLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:PRK13536 213 ERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-207 |
6.67e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 2 SLLMQLTDV----AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRS 76
Cdd:PRK10247 5 SPLLQLQNVgylaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 77 YLVQQQVpPFAMPVWHYLMLHLHDKHST----ALLTDVaAALGL-EDKLSRHVSQLSGGEWQRVRLAAVIvQIHPagnph 151
Cdd:PRK10247 85 YCAQTPT-LFGDTVYDNLIFPWQIRNQQpdpaIFLDDL-ERFALpDTILTKNIAELSGGEKQRISLIRNL-QFMP----- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 152 gRMLLLDEPMSGLDVAQQAALDTLLSALSR-KGIAVVMSSHDLNHtLRHAHRVWLLS 207
Cdd:PRK10247 157 -KVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDE-INHADKVITLQ 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-212 |
9.20e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQImllehtlaEWSP-VSLAhrrsYLVQQQ--VPPfAMPVW 91
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTV--------KLGEtVKIG----YFDQHQeeLDP-DKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYLMlHLHDKHSTALLTDVAAALGL-EDKLSRHVSQLSGGEWQRVRLAAVIVQihpAGNphgrMLLLDEPMSGLDVaqqA 170
Cdd:COG0488 398 DELR-DGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS---PPN----VLLLDEPTNHLDI---E 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495776072 171 ALDTLLSALSR-KGiAVVMSSHDlnhtlRH-----AHRVWLLSQGKMI 212
Cdd:COG0488 467 TLEALEEALDDfPG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-224 |
1.06e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVS-LAHRRSYLVQQQVPPFAM 88
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQlLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 -PVWHYLM-----LHLHDKHSTAL-----LTDVAAALGLeDKLSRH--VSQLSGGEWQRVRLA-AVIVQihpagnphGRM 154
Cdd:PRK15134 376 nPRLNVLQiieegLRVHQPTLSAAqreqqVIAVMEEVGL-DPETRHryPAEFSGGQRQRIAIArALILK--------PSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 155 LLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-218 |
1.49e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.78 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-----MTagEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFA-MPVWHYLML 96
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGhpkyeVT--SGSILLDGEDILELSPDERARAGIFLAFQYPVEIPgVSVSNFLRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 --------HLHDKHSTALLTDVAAALGL-EDKLSRHVSQ-LSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDV 166
Cdd:COG0396 101 alnarrgeELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLL-----EP--KLAILDETDSGLDI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 167 aqqAALDTL---LSALSRKGIAVVMSSHD---LNHTlrHAHRVWLLSQGKMIASGTRD 218
Cdd:COG0396 174 ---DALRIVaegVNKLRSPDRGILIITHYqriLDYI--KPDFVHVLVDGRIVKSGGKE 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-221 |
1.57e-13 |
|
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: 69.47 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG--EGQIMLLEHTLAEWSPVSLAHRRSYLVQQQ------VPpf 86
Cdd:TIGR02633 275 RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGkfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDrkrhgiVP-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMPVWHYLMLHLHDKHSTALLTDVAAALG-LEDKLSR----------HVSQLSGGEWQRVRLAAVIVQihpagNPhgRML 155
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELQiIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLLT-----NP--RVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 156 LLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG-----TRDQVL 221
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFvnhalTQEQVL 496
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-193 |
2.36e-13 |
|
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: 68.93 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYLM 95
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 LHLHDKhSTALLTDVAAALGLEDKLSR-----------HVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGL 164
Cdd:TIGR02868 431 LARPDA-TDEELWAALERVGLADWLRAlpdgldtvlgeGGARLSGGERQRLALARALLADAP-------ILLLDEPTEHL 502
|
170 180 190
....*....|....*....|....*....|
gi 495776072 165 DVAQQAA-LDTLLSALSRKgiAVVMSSHDL 193
Cdd:TIGR02868 503 DAETADElLEDLLAALSGR--TVVLITHHL 530
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-220 |
2.92e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.73 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSpVSLAHRRSYLVqqqvppFAMP 89
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVLSEET-VWDVRRQVGMV------FQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWHYLMLHLHDKHSTAL----------LTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLL 156
Cdd:PRK13635 91 DNQFVGATVQDDVAFGLenigvpreemVERVDQALrqvGMEDFLNREPHRLSGGQKQRVAIAGVL-----ALQP--DIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 157 LDEPMSGLD-VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRhAHRVWLLSQGKMIASGTRDQV 220
Cdd:PRK13635 164 LDEATSMLDpRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-215 |
3.03e-13 |
|
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: 66.79 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGE----GQImllehtlaewspvslahrrsylvqqqVPPFAM-----P- 89
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIyppDSGTvtvrGRV--------------------------SSLLGLgggfnPe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 ------VWHYLMLH-LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGewQRVRLA-AVIVQIHPagnphgRMLLLDEPM 161
Cdd:cd03220 99 ltgrenIYLNGRLLgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG--MKARLAfAIATALEP------DILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 162 SGLDVA-QQAALDtLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:cd03220 171 AVGDAAfQEKCQR-RLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-251 |
3.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAG-MTAGEGQImllehtLAEWSPVSLAHRR------------------SYLVQQQVP--PFAMP 89
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGiLKPTSGSV------LIRGEPITKENIRevrkfvglvfqnpddqifSPTVEQDIAfgPINLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWHYLMLHlhdKHSTALLTdvaaaLGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVAQQ 169
Cdd:PRK13652 109 LDEETVAH---RVSSALHM-----LGLEELRDRVPHHLSGGEKKRVAIAGVI-----AMEP--QVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 170 AALDTLLSALS-RKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLaraynMSFRRLDIEGHKMLIST 248
Cdd:PRK13652 174 KELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL-----LARVHLDLPSLPKLIRS 248
|
...
gi 495776072 249 GQE 251
Cdd:PRK13652 249 LQA 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-239 |
3.94e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.14 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKST---LLARMAGMTagEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAmpvwhyLMLHL 98
Cdd:PRK10070 50 AIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPT--RGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFA------LMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 HDKHSTAL---LTDVAAA------------LGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEPMSG 163
Cdd:PRK10070 122 TVLDNTAFgmeLAGINAEerrekaldalrqVGLENYAHSYPDELSGGMRQRVGLARAL-----AINPD--ILLMDEAFSA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 164 LD-VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP--NLARAYnmsFRRLDI 239
Cdd:PRK10070 195 LDpLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPanDYVRTF---FRGVDI 270
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-224 |
4.74e-13 |
|
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: 67.39 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTL------LARMAGMTAGEgqIMLLEHTLAEWSPVSLAHRRSYLVQ---QQvpPFA-----M 88
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLarailgLLPPPGITSGE--ILFDGEDLLKLSEKELRKIRGREIQmifQD--PMTslnpvM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYLM--LHLHDKHSTALLTDVAAAL----GL---EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDE 159
Cdd:COG0444 104 TVGDQIAepLRIHGGLSKAEARERAIELlervGLpdpERRLDRYPHELSGGMRQRVMIARAL-----ALEP--KLLIADE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNhTLRH-AHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG0444 177 PTTALDVTIQAQILNLLKDLQRElGLAILFITHDLG-VVAEiADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-224 |
5.03e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLaewSPVSLAHRRSYLVQQQVPPFA-MPVWHY 93
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDV---SRLHARDRKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 L-----MLHLHDKHSTALLTDVAAAL----GLEDKLSRHVSQLSGGEWQRVRLA---AVIVQIhpagnphgrmLLLDEPM 161
Cdd:PRK10851 95 IafgltVLPRRERPNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALAralAVEPQI----------LLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 162 SGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-221 |
5.32e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRsylvQQQVPPFAMPVWHYLMlhlhdkhsTALLTDV 110
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALR----QQVATVFQDPEQQIFY--------TDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 111 AAAL---GL-EDKLSRHVSQ-----------------LSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQ 169
Cdd:PRK13638 100 AFSLrnlGVpEAEITRRVDEaltlvdaqhfrhqpiqcLSHGQKKRVAIAGALVL-------QARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-194 |
5.44e-13 |
|
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: 65.46 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYLM 95
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 LhLHDKHSTALLT--DVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALD 173
Cdd:TIGR01189 96 F-WAAIHGGAQRTieDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLS-------RRPLWILDEPTTALDKAGVALLA 167
|
170 180
....*....|....*....|..
gi 495776072 174 TLLSA-LSRKGIAVVMSSHDLN 194
Cdd:TIGR01189 168 GLLRAhLARGGIVLLTTHQDLG 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-224 |
7.28e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.40 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKS-TLLARM----AGMTAGEGQIMLLEHTLAEWSPVSLAHRRS-----------------YLV 79
Cdd:COG4172 32 DIAAGETLALVGESGSGKSvTALSILrllpDPAAHPSGSILFDGQDLLGLSERELRRIRGnriamifqepmtslnplHTI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 80 QQQVppfampvwhYLMLHLHDKHSTA--------LLTDVaaalGL---EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAG 148
Cdd:COG4172 112 GKQI---------AEVLRLHRGLSGAaararaleLLERV----GIpdpERRLDAYPHQLSGGQRQRVMIAMAL-----AN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 149 NPhgRMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG4172 174 EP--DLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-225 |
8.65e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLA---RMAGMTAGEgqimLLEHTLAEWSP---VSLAHRRSYLVQQQVppfamp 89
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinKLEEITSGD----LIVDGLKVNDPkvdERLIRQEAGMVFQQF------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 vwhYLMLHLH--------------------DKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagn 149
Cdd:PRK09493 87 ---YLFPHLTalenvmfgplrvrgaskeeaEKQARELLAKV----GLAERAHHYPSELSGGQQQRVAIARALA-VKP--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 150 phgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLT-PPN 225
Cdd:PRK09493 156 ---KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKnPPS 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-212 |
8.91e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSL-AHRRSYLVQQQVPPFAM----- 88
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLNRAQRkAFRRDIQMVFQDSISAVnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 -------PVWHYLMLHLHDKHSTA--LLTDVAAALGLEDKLSrhvSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDE 159
Cdd:PRK10419 108 vreiirePLRHLLSLDKAERLARAseMLRAVDLDDSVLDKRP---PQLSGGQLQRVCLARAL-----AVEP--KLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMI 212
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-215 |
9.09e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE---GQIMLLEHTLAEwspvSLAHRRSYLVQQQVPPFAM 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftGTILANNRKPTK----QILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYLML--------HLHDKHSTALLTDVAAALGL---EDKL--SRHVSQLSGGEWQRVRLAAVIVqIHPAgnphgrML 155
Cdd:PLN03211 156 TVRETLVFcsllrlpkSLTKQEKILVAESVISELGLtkcENTIigNSFIRGISGGERKRVSIAHEML-INPS------LL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 156 LLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHD-LNHTLRHAHRVWLLSQGKMIASG 215
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-221 |
1.47e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGE----GQI-MLLEHTLAewspvslahrrsylvqqqvppFaMP----- 89
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLIAGIlepTSGRvevnGRVsALLELGAG---------------------F-HPeltgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 --VWHYLMLHLHDKHST-ALLTDVAAALGLEDKLSRHVSQLSGGewQRVRLA-AVIVQIHPagnphgRMLLLDEPMSGLD 165
Cdd:COG1134 107 enIYLNGRLLGLSRKEIdEKFDEIVEFAELGDFIDQPVKTYSSG--MRARLAfAVATAVDP------DILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 166 VA-QQAALDtLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:COG1134 179 AAfQKKCLA-RIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-234 |
2.07e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVS-LAHRRSYLVQ--QQVPPF--AMPVW- 91
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLrPARGGRIMLNGKEINALSTAQrLARGLVYLPEdrQSSGLYldAPLAWn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 ------HYLMLHLHDKHSTALLTDVAAALGLedKLSrHVSQ----LSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPM 161
Cdd:PRK15439 362 vcalthNRRGFWIKPARENAVLERYRRALNI--KFN-HAEQaartLSGGNQQKVLIAKCL-----EASP--QLLIVDEPT 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 162 SGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVltppNLARAYNMSF 234
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI----NVDTIMRLAF 500
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-218 |
2.25e-12 |
|
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: 66.00 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMLLEHTL-------AEWSPVSLAHRRSYLVQQqvpp 85
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphGTWDGEIYWSGSPLkasnirdTERAGIVIIHQELTLVPE---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 86 faMPVWHYLMLHLHDKHSTALLTDVAAALGLEDKL----------SRHVSQLSGGEWQrvrlaavIVQIHPAGNPHGRML 155
Cdd:TIGR02633 93 --LSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLrelqldadnvTRPVGDYGGGQQQ-------LVEIAKALNKQARLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495776072 156 LLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIasGTRD 218
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV--ATKD 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-210 |
3.65e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAGM-TAGEGQImllehtLAEWSPVSLAHRRSYLVQQQVPpfAMPvWHYLM----LHLH 99
Cdd:PRK11247 37 AGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGEL------LAGTAPLAEAREDTRLMFQDAR--LLP-WKKVIdnvgLGLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 DKHSTALLtDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqIHpagnpHGRMLLLDEPMSGLDVAQQAALDTLLSAL 179
Cdd:PRK11247 108 GQWRDAAL-QALAAVGLADRANEWPAALSGGQKQRVALARAL--IH-----RPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|..
gi 495776072 180 SRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGK 210
Cdd:PRK11247 180 WQQhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-229 |
5.49e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 4 LMQLTDVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPV-SLAH-------- 73
Cdd:COG1129 256 VLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADpADSGEIRLDGKPVRIRSPRdAIRAgiayvped 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 74 RRSY-LVQQqvppfaMPVWHYLMLHLHDKHSTALLTD----VAAALGLEDKLS-------RHVSQLSGGEWQRVRLAAVI 141
Cdd:COG1129 336 RKGEgLVLD------LSIRENITLASLDRLSRGGLLDrrreRALAEEYIKRLRiktpspeQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 142 vqihpAGNPhgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQvL 221
Cdd:COG1129 410 -----ATDP--KVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREE-A 481
|
....*...
gi 495776072 222 TPPNLARA 229
Cdd:COG1129 482 TEEAIMAA 489
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-224 |
6.08e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.52 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLA---RMAGMTAG---EGQIMLLEHTL--AEWSPVSLAhRRSYLVQQQVPPFA 87
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRclnRMNDLIPGarvEGEILLDGEDIydPDVDVVELR-RRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVWH---YLmLHLHDKHSTALLTDV------AAALGLE--DKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLL 156
Cdd:COG1117 106 KSIYDnvaYG-LRLHGIKSKSELDEIveeslrKAALWDEvkDRLKKSALGLSGGQQQRLCIARAL-----AVEP--EVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 157 LDEPMSGLDVAQQAALDTLLSALSRKgIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-224 |
8.08e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFA-----MPVWHYLMLHL 98
Cdd:PRK15079 46 EGETLGVVGESGCGKSTFARAIIGLvKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLAslnprMTIGEIIAEPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 ---HDKHSTALLTDVAAAL----GL-EDKLSRHVSQLSGGEWQRVRLA-AVIVQihpagnPhgRMLLLDEPMSGLDVAQQ 169
Cdd:PRK15079 126 rtyHPKLSRQEVKDRVKAMmlkvGLlPNLINRYPHEFSGGQCQRIGIArALILE------P--KLIICDEPVSALDVSIQ 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 170 AALDTLLSALSRK-GIAVVMSSHDLNhTLRH-AHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK15079 198 AQVVNLLQQLQREmGLSLIFIAHDLA-VVKHiSDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-221 |
8.35e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 63.02 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKST---LLARMAGMTagEGQIMLLEHTLAEWSPVSLahRRSY-LVQQQVPPFAMPVWH---YLM 95
Cdd:cd03253 24 IPAGKKVAIVGPSGSGKSTilrLLFRFYDVS--SGSILIDGQDIREVTLDSL--RRAIgVVPQDTVLFNDTIGYnirYGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 L--------------HLHDKhstalltdvaaALGLEDKLSRHVSQ----LSGGEWQRVRLAAVIVQihpagNPhgRMLLL 157
Cdd:cd03253 100 PdatdeevieaakaaQIHDK-----------IMRFPDGYDTIVGErglkLSGGEKQRVAIARAILK-----NP--PILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 158 DEPMSGLDV-AQQAALDTLLSALSRKgiAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:cd03253 162 DEATSALDThTEREIQAALRDVSKGR--TTIVIAHRL-STIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-220 |
8.99e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.60 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTL---LARMAGMTAGEgqIMLLEHTLAEWSPVSLAHRRSYLvqQQV--PPFA-----MPVWH 92
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLgrlLLRLEEPTSGE--ILFDGQDITGLSGRELRPLRRRM--QMVfqDPYAslnprMTVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLM--LHLHDKHSTALLTDVAAAL----GL-EDKLSRHVSQLSGGEWQRVRLA-AVIVqihpagNPhgRMLLLDEPMSGL 164
Cdd:COG4608 117 IIAepLRIHGLASKAERRERVAELlelvGLrPEHADRYPHEFSGGQRQRIGIArALAL------NP--KLIVCDEPVSAL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 165 DVAQQAALDTLLSALSRK-GIAVVMSSHDLNhTLRH-AHRVWLLSQGKMIASGTRDQV 220
Cdd:COG4608 189 DVSIQAQVLNLLEDLQDElGLTYLFISHDLS-VVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-218 |
9.61e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMLLEHTLA-------EWSPVSLAHRRSYLVQQ---- 81
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphGTYEGEIIFEGEELQasnirdtERAGIAIIHQELALVKElsvl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 82 -------QVPPFAmpVWHYLMLHLHdkhSTALLtdvaAALGLEDKLSRHVSQLSGGEWQrvrlaavIVQIHPAGNPHGRM 154
Cdd:PRK13549 101 eniflgnEITPGG--IMDYDAMYLR---AQKLL----AQLKLDINPATPVGNLGLGQQQ-------LVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 155 LLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIasGTRD 218
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI--GTRP 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-211 |
1.16e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 62.49 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKST---LLARMAGMTagEGQIMLLEHTLAEWSPVSLaHRRSYLVQQQVPPFAMPVWH 92
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTvvaLLENFYQPQ--GGQVLLDGKPISQYEHKYL-HSKVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLHDKhSTALLTDVAAA-------LGLEDKLSRHV----SQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPM 161
Cdd:cd03248 107 NIAYGLQSC-SFECVKEAAQKahahsfiSELASGYDTEVgekgSQLSGGQKQRVAIARALIR-----NP--QVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495776072 162 SGLDVAQQAALDTLLS-ALSRKGIAVVmsSHDLNhTLRHAHRVWLLSQGKM 211
Cdd:cd03248 179 SALDAESEQQVQQALYdWPERRTVLVI--AHRLS-TVERADQILVLDGGRI 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-216 |
1.31e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 24 NAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSY-----LVQQQV---PPFAM------ 88
Cdd:COG4161 26 PSGETLVLLGPSGAGKSSLLRVLNLLeTPDSGQLNIAGHQFDFSQKPSEKAIRLLrqkvgMVFQQYnlwPHLTVmenlie 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 -PVWhylMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVA 167
Cdd:COG4161 106 aPCK---VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM-----EP--QVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495776072 168 QQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:COG4161 176 ITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-246 |
1.48e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.94 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPP---FAMPVW 91
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDnqlFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 H-----YLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLD- 165
Cdd:PRK13636 102 QdvsfgAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV-MEP------KVLVLDEPTAGLDp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 166 VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMSFRRLdieGHKML 245
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLPRI---GHLME 251
|
.
gi 495776072 246 I 246
Cdd:PRK13636 252 I 252
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-209 |
2.07e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslahRRSYLVQ----QQVppfAMPv 90
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIARPAGARVLFLP-----QRPYLPLgtlrEAL---LYP- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 91 whylmlHLHDKHSTALLTDVAAALGLEDKLSR-HVSQ-----LSGGEWQRVRLAAVIVQiHPagnphgRMLLLDEPMSGL 164
Cdd:COG4178 450 ------ATAEAFSDAELREALEAVGLGHLAERlDEEAdwdqvLSLGEQQRLAFARLLLH-KP------DWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495776072 165 DVAQQAALDTLLSAlSRKGIAVVMSSHDlnHTLRHAH-RVWLLSQG 209
Cdd:COG4178 517 DEENEAALYQLLRE-ELPGTTVISVGHR--STLAAFHdRVLELTGD 559
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-221 |
2.12e-11 |
|
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: 61.73 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPpFAMPVWHYL 94
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVDGHDLALADPAWLRRQVGVVLQENVL-FNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 ML-----HLHDKHSTALLTDVAA-----ALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGL 164
Cdd:cd03252 97 ALadpgmSMERVIEAAKLAGAHDfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIH-----NP--RILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 165 DVAQQAALDTLLSALSrKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:cd03252 170 DYESEHAIMRNMHDIC-AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-222 |
2.43e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.92 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMA-GMTAGEGQIMLLEHTLAEWSPVSLAHRRSyLVQQQVPPFAMPVWHYL 94
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAALRQAIS-VVSQRVHLFSATLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHLHDKhSTALLTDVAAALGLEDKLSRHVS----------QLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGL 164
Cdd:PRK11160 435 LLAAPNA-SDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAP-------LLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 165 DVAQQAALDTLLSALSrKGIAVVMSSHDLnHTLRHAHRVWLLSQGKMIASGTRDQVLT 222
Cdd:PRK11160 507 DAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-250 |
2.51e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVsLAHRRS-YLVQQQVPPFA-MPVWH 92
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLTPA-KAHQLGiYLVPQEPLLFPnLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLhDKHSTAL--LTDVAAALGLEDKLSRHVSQLSGGEWQrvrlaavIVQIHPAGNPHGRMLLLDEPMSGLDVAQQA 170
Cdd:PRK15439 106 NILFGL-PKRQASMqkMKQLLAALGCQLDLDSSAGSLEVADRQ-------IVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 171 ALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRD--------QVLTPpnLARAYNMSFRR---LDI 239
Cdd:PRK15439 178 RLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAdlstddiiQAITP--AAREKSLSASQklwLEL 255
|
250
....*....|.
gi 495776072 240 EGHKMLISTGQ 250
Cdd:PRK15439 256 PGNRRQQAAGA 266
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-224 |
2.64e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 28 ILHLVGPNGAGKSTLL------------ARMAGMTAGEGQIMLLehtlaewSPVSLAHRRSYLVQQQVPPFA-MPVWHYL 94
Cdd:PRK14247 31 ITALMGPSGSGKSTLLrvfnrlielypeARVSGEVYLDGQDIFK-------MDVIELRRRVQMVFQIPNPIPnLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHLH----DKHSTALLTDVAAAL-------GLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSG 163
Cdd:PRK14247 104 ALGLKlnrlVKSKKELQERVRWALekaqlwdEVKDRLDAPAGKLSGGQQQRLCIARAL-----AFQP--EVLLADEPTAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 164 LDVAQQAALDTLLSALsRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK14247 177 LDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-224 |
2.71e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.40 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLaRMAGM--TAGEGQIMLLEHTLAEWSPVSL-AHRR-------------SYLVQQQVppf 86
Cdd:COG1135 28 IEKGEIFGIIGYSGAGKSTLI-RCINLleRPTSGSVLVDGVDLTALSERELrAARRkigmifqhfnllsSRTVAENV--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMP--VWHYlmlhlhDKHSTA-----LLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLA-AVivqihpAGNPhgRMLLLD 158
Cdd:COG1135 104 ALPleIAGV------PKAEIRkrvaeLLELV----GLSDKADAYPSQLSGGQKQRVGIArAL------ANNP--KVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 159 EPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLnHTLRH-AHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRElGLTIVLITHEM-DVVRRiCDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-225 |
2.74e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLA---RMAGMTAG---EGQIMLLEHTLaeWSP----VSLahRRSY-LVQ 80
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRsinRMNDLNPEvtiTGSIVYNGHNI--YSPrtdtVDL--RKEIgMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 81 QQVPPFAMPVWHYLM--LHLHDKHSTALLTDV------AAALGLEDKLSRHVSQ--LSGGEWQRVRLAAVIvqihpAGNP 150
Cdd:PRK14239 93 QQPNPFPMSIYENVVygLRLKGIKDKQVLDEAvekslkGASIWDEVKDRLHDSAlgLSGGQQQRVCIARVL-----ATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 151 hgRMLLLDEPMSGLDVAQQAALDTLLSALsRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG-TRDQVLTPPN 225
Cdd:PRK14239 168 --KIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNdTKQMFMNPKH 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-215 |
3.18e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.13 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVslAHRRSYLVQQ---QVPPFAmpVWHYLMLH- 97
Cdd:PRK13537 30 VQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCGEPVPSRARH--ARQRVGVVPQfdnLDPDFT--VRENLLVFg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 ----LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLD-VAQQAAL 172
Cdd:PRK13537 106 ryfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN-----DPD--VLVLDEPTTGLDpQARHLMW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495776072 173 DTLLSALSRkGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:PRK13537 179 ERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-237 |
3.56e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLleHTLAEWSPVSLAHRRSYL--VQQQVP-----P--F 86
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRV--EGRVEFFNQNIYERRVNLnrLRRQVSmvhpkPnlF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMPV------------WHyLMLHLHDKHSTALltdVAAAL--GLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphg 152
Cdd:PRK14258 101 PMSVydnvaygvkivgWR-PKLEIDDIVESAL---KDADLwdEIKHKIHKSALDLSGGQQQRLCIARALA-VKP------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 153 RMLLLDEPMSGLDVAQQAALDTLLSALS-RKGIAVVMSSHDLNHTLRHAHRVWLLSQ-----GKMIASGTRDQVLTPPNL 226
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHD 249
|
250
....*....|.
gi 495776072 227 ARAYNMSFRRL 237
Cdd:PRK14258 250 SRTREYVLSRL 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-224 |
3.82e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKS-TLLARMaGMTAGEGQIML--LEHTLAEWSPVSLAHRRSYLVQQQVPPFAMP------ 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLIDYPGRVMAekLEFNGQDLQRISEKERRNLVGAEVAMIFQDPmtslnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 ---VWHYLM--LHLHDKHSTA--------LLTDVaaalGLEDKLSR---HVSQLSGGEWQRVRLAAVIvqihpAGNPhgR 153
Cdd:PRK11022 105 cytVGFQIMeaIKVHQGGNKKtrrqraidLLNQV----GIPDPASRldvYPHQLSGGMSQRVMIAMAI-----ACRP--K 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 154 MLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-209 |
4.16e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.42 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIML----------------LEHTLAEW----SPVSLAhr 74
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApSSGEITLdgvpvtgpgadrgvvfQKDALLPWlnvlDNVAFG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 75 rsyLVQQQVPPfampvwhylmlhlHDKHSTALltDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRM 154
Cdd:COG4525 101 ---LRLRGVPK-------------AERRARAE--ELLALVGLADFARRRIWQLSGGMRQRVGIARAL-----AADP--RF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 155 LLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQG 209
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-230 |
4.24e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFA-MPVWHYLMLHLHD 100
Cdd:PRK11614 28 INQGEIVTLIGANGAGKTTLLGTLCGDPrATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrMTVEENLAMGGFF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 101 KHSTALLTDVAAALGLEDKLSRHVSQ----LSGGEWQrvrlaavIVQIHPAGNPHGRMLLLDEPMSGL-DVAQQAALDTl 175
Cdd:PRK11614 108 AERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQ-------MLAIGRALMSQPRLLLLDEPSLGLaPIIIQQIFDT- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 176 LSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAY 230
Cdd:PRK11614 180 IEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-191 |
5.52e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVSLAHrrsYLVQQQVPPFAMPVWHYLML--HL 98
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIKLDGGDIDDPDVAEACH---YLGHRNAMKPALTVAENLEFwaAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 HDKHSTALlTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpAGNPhgrMLLLDEPMSGLDVAQQAALDTLLSA 178
Cdd:PRK13539 101 LGGEELDI-AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLV----SNRP---IWILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|...
gi 495776072 179 LSRKGIAVVMSSH 191
Cdd:PRK13539 173 HLAQGGIVIAATH 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-209 |
6.05e-11 |
|
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: 60.56 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVSLAHRRSY------LVQQQVppfAM 88
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAqPTSGGVILEGKQITEPGPDRMVVFQNYsllpwlTVRENI---AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVwHYLMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvQIHPagnphgRMLLLDEPMSGLDVAQ 168
Cdd:TIGR01184 78 AV-DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARAL-SIRP------KVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495776072 169 QAAL-DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQG 209
Cdd:TIGR01184 150 RGNLqEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-221 |
6.48e-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: 61.74 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMLLEhtlaEWspVSLAHRRSYLVQQQVPPFAMPVWHYLMLhlh 99
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVlepTSGEVNVRVGD----EW--VDMTKPGPDGRGRAKRYIGILHQEYDLY--- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 dKHSTAL--LTD-----------------VAAALGLEDK-----LSRHVSQLSGGEWQRVRLAAVIVQiHPagnphgRML 155
Cdd:TIGR03269 378 -PHRTVLdnLTEaiglelpdelarmkaviTLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIK-EP------RIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 156 LLDEPMSGLD-VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:TIGR03269 450 ILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-226 |
7.45e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSpvslAHRRSYLVQQ--QVP-----PfAMPVWHYL 94
Cdd:COG1101 29 IEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILIDGKDVTKLP----EYKRAKYIGRvfQDPmmgtaP-SMTIEENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHLH-----------DKHSTALLTDVAAAL--GLEDKLSRHVSQLSGGEWQRVRLA-AVIVQIhpagnphgRMLLLDEP 160
Cdd:COG1101 104 ALAYRrgkrrglrrglTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLmATLTKP--------KLLLLDEH 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 161 MsgldvaqqAALDTLLSAL---------SRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMI--ASGTRDQVLTPPNL 226
Cdd:COG1101 176 T--------AALDPKTAALvleltekivEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIldVSGEEKKKLTVEDL 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-232 |
1.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM------TAGEGQIMLLEHT-LAEWSPVslahRRSYLVQQQVPP---FAMPVWH 92
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLlqptegKVTVGDIVVSSTSkQKEIKPV----RKKVGVVFQFPEsqlFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLH-----LHDKHSTALLTDVAAALGLEDKL-SRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEPMSGLDV 166
Cdd:PRK13643 105 DVAFGpqnfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL-----AMEPE--VLVLDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 167 AQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNM 232
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL 243
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
10-215 |
1.13e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 59.97 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG---MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQ----- 81
Cdd:TIGR01978 10 VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsYEVTSGTILFKGQDLLELEPDERARAGLFLAFQypeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 82 --------------------QVPPFAMPVWHylmlhlhdkhstALLTDVAAALGL-EDKLSRHVSQ-LSGGEWQRVRLAA 139
Cdd:TIGR01978 90 pgvsnleflrsalnarrsarGEEPLDLLDFE------------KLLKEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 140 VIVqIHPagnphgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNhTLRHAH--RVWLLSQGKMIASG 215
Cdd:TIGR01978 158 MAL-LEP------KLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR-LLNYIKpdYVHVLLDGRIVKSG 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-215 |
1.22e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKS-TLLARM----AGMTAGEGQImllehtLAEWSPVSLAHRRSYLVQ--QQVPPFAMPVWHYL 94
Cdd:PRK10418 25 TLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAGRV------LLDGKPVAPCALRGRKIAtiMQNPRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHLHD------KHST-ALLTDVAAALGLEDK---LSRHVSQLSGGEWQRVRLAAVIVqihpAGNPhgrMLLLDEPMSGL 164
Cdd:PRK10418 99 HTHAREtclalgKPADdATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALL----CEAP---FIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495776072 165 D-VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:PRK10418 172 DvVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-221 |
1.34e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLlARmagmtAGEGQIMLLEHTLAewSPVSLAHRRSYLVQQQV-----------------P 84
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSAL-AR-----ALAGELPLLSGERQ--SQFSHITRLSFEQLQKLvsdewqrnntdmlspgeD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 PFAMPVWHYLMLHLHDkhsTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGL 164
Cdd:PRK10938 97 DTGRTTAEIIQDEVKD---PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMS-----EPD--LLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 165 DVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-193 |
1.37e-10 |
|
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: 59.37 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLaRM--AGMTAGEGQImLLEHT-----LAEWSPVS-LAHRRSYL--VQQqvppF--AMP 89
Cdd:COG4778 33 SVAAGECVALTGPSGAGKSTLL-KCiyGNYLPDSGSI-LVRHDggwvdLAQASPREiLALRRRTIgyVSQ----FlrVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 -VwhylmlhlhdkhsTALltDVAAALGLEDKLSRHVSQ-----------------------LSGGEWQRVRLAAVIVQIH 145
Cdd:COG4778 107 rV-------------SAL--DVVAEPLLERGVDREEARararellarlnlperlwdlppatFSGGEQQRVNIARGFIADP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495776072 146 PAgnphgrmLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDL 193
Cdd:COG4778 172 PL-------LLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDE 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
115-226 |
1.74e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 115 GL-EDKLSRHVSQLSGGEWQRVRLAAvIVQIHPagnphgRMLLLDEPMSGLD-VAQQAALDtLLSALSRKGIAVVMSSHD 192
Cdd:PRK13651 153 GLdESYLQRSPFELSGGQKRRVALAG-ILAMEP------DFLVFDEPTAGLDpQGVKEILE-IFDNLNKQGKTIILVTHD 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 495776072 193 LNHTLRHAHRVWLLSQGKMIASGT-----------RDQVLTPPNL 226
Cdd:PRK13651 225 LDNVLEWTKRTIFFKDGKIIKDGDtydilsdnkflIENNMEPPKL 269
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
107-193 |
2.04e-10 |
|
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: 60.18 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 107 LTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAV 186
Cdd:COG1245 193 LDELAEKLGLENILDRDISELSGGELQRVAIAAALLR-------DADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV 265
|
....*..
gi 495776072 187 VMSSHDL 193
Cdd:COG1245 266 LVVEHDL 272
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-219 |
2.29e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMA-GMTAGEGQIMLLEHTLAEWSPVSLahRRSY-LVQQQVPPFAMPVWHY 93
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQSGRILIDGTDIRTVTRASL--RRNIaVVFQDAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLHLHDKHSTALL--TDVAAALGL----EDKLSRHV----SQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSG 163
Cdd:PRK13657 429 IRVGRPDATDEEMRaaAERAQAHDFierkPDGYDTVVgergRQLSGGERQRLAIARALLKDPP-------ILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 164 LDVAQ----QAALDTLlsalsRKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGTRDQ 219
Cdd:PRK13657 502 LDVETeakvKAALDEL-----MKGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDE 555
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-233 |
2.61e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 19 ITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVS----LAHRRSY-LVQQQvppfaMPVWH 92
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSGTLNIAGNHFDFSKTPSdkaiRELRRNVgMVFQQ-----YNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YL------------MLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLA-AVIVQihPAgnphgrMLLLDE 159
Cdd:PRK11124 96 HLtvqqnlieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIArALMME--PQ------VLLFDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMS 233
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEAFKNYLS 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-222 |
2.62e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.23 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLaewSPVSLAHRRSY------------ 77
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlKPQSGEIKIDGITI---SKENLKEIRKKigiifqnpdnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 78 ------------LVQQQVPPFAMPvwhylmlhlhdkhstALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqih 145
Cdd:PRK13632 97 igatveddiafgLENKKVPPKKMK---------------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL---- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 146 pAGNPhgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMS-SHDLNHTLRhAHRVWLLSQGKMIASGTRDQVLT 222
Cdd:PRK13632 158 -ALNP--EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-222 |
2.80e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 14 GRLEPITGA---VNAGEILHLVGPNGAG--KSTLLARMAGMTAGE---------GQIMLLEHTLAEWSPVSLAHRRSYLV 79
Cdd:NF000106 24 GEVKAVDGVdldVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRrpwrf*twcANRRALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 80 QQQVppfampvwhYLM---LHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLL 156
Cdd:NF000106 104 RENL---------YMIgr*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI-----GRP--AVLY 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 157 LDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLT 222
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-226 |
3.05e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEwspVSLAHRRSYL--VQQQVPPFAMPVWHY 93
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRE---LDPESWRKHLswVGQNPQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LML---HLHDKHSTALLTDVAA-------ALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSG 163
Cdd:PRK11174 443 VLLgnpDASDEQLQQALENAWVseflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQ-------PCQLLLLDEPTAS 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 164 LDV-AQQAALDTLLSALSRKgiAVVMSSHDLNHtLRHAHRVWLLSQGKMIASGTRDQVLTPPNL 226
Cdd:PRK11174 516 LDAhSEQLVMQALNAASRRQ--TTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-192 |
3.47e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.25 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGMTAG-EGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAM-PVWHY------- 93
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGsSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLiPTLNAlenvelp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 -LMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAvivqihpAGNPHGRMLLLDEPMSGLDVAQQAAL 172
Cdd:PRK10584 113 aLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR-------AFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|.
gi 495776072 173 DTLLSALSRK-GIAVVMSSHD 192
Cdd:PRK10584 186 ADLLFSLNREhGTTLILVTHD 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-209 |
4.94e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLlehtlaEWSPVS-LAHRRSYLVQQQvppfAMPVWHY 93
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITL------DGKPVEgPGAERGVVFQNE----GLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LM------LHLH---DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGL 164
Cdd:PRK11248 87 VQdnvafgLQLAgveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARAL-----AANP--QLLLLDEPFGAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495776072 165 DVAQQAALDTLLSAL-SRKGIAVVMSSHDLNHTLRHAHRVWLLSQG 209
Cdd:PRK11248 160 DAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-222 |
5.18e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMTAG--EGQIMLLEHTLAEWSPV-SLAHRRSYLVQQQ-----VPpfAMPVWHY 93
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYPGrwEGEIFIDGKPVKIRNPQqAIAQGIAMVPEDRkrdgiVP--VMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLHLHDKHSTALLTDVAAALG-LEDKLSR----------HVSQLSGGEWQRVRLAAVIVqihpagnPHGRMLLLDEPMS 162
Cdd:PRK13549 362 ITLAALDRFTGGSRIDDAAELKtILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLL-------LNPKILILDEPTR 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 163 GLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIAS-----GTRDQVLT 222
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDlinhnLTQEQVME 499
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
114-226 |
5.43e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 114 LGL-EDKLSRHVSQLSGGEWQRVRLAAvIVQIHPagnphgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHD 192
Cdd:PRK13631 163 MGLdDSYLERSPFGLSGGQKRRVAIAG-ILAIQP------EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
90 100 110
....*....|....*....|....*....|....
gi 495776072 193 LNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNL 226
Cdd:PRK13631 236 MEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
12-225 |
5.88e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.11 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTL-AEWSPVSLAHRR-----------SYL 78
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPTSGTVTIGERVItAGKKNKKLKPLRkkvgivfqfpeHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 79 VQQQVPP--------FAMPvwhylmlhlhDKHSTALLTDVAAALGL-EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGN 149
Cdd:PRK13634 99 FEETVEKdicfgpmnFGVS----------EEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL-----AME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 150 PhgRMLLLDEPMSGLDVAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:PRK13634 164 P--EVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-239 |
8.50e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.89 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLaRMAGM--TAGEGQIMLLEHTLAEWSPVSLAHRR--------------SYLV 79
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLI-RCINLleRPTSGRVLVDGQDLTALSEKELRKARrqigmifqhfnllsSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 80 QQQVppfAMPvwhylmLHLH-------DKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhg 152
Cdd:PRK11153 100 FDNV---ALP------LELAgtpkaeiKARVTELLELV----GLSDKADRYPAQLSGGQKQRVAIARAL-----ASNP-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 153 RMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN--LARA 229
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKhpLTRE 239
|
250
....*....|
gi 495776072 230 YNMSFRRLDI 239
Cdd:PRK11153 240 FIQSTLHLDL 249
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-205 |
1.01e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQImllehtlaEWSPVSLAHRRSYLVQQ--------QVPPFAMPVWHY 93
Cdd:PRK13538 24 LNAGELVQIEGPNGAGKTSLLRILAGlARPDAGEV--------LWQGEPIRRQRDEYHQDllylghqpGIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLH-LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQAAL 172
Cdd:PRK13538 96 RFYQrLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAP-------LWILDEPFTAIDKQGVARL 168
|
170 180 190
....*....|....*....|....*....|....
gi 495776072 173 DTLLSA-LSRKGIAVVMSSHDLNHTLRHAHRVWL 205
Cdd:PRK13538 169 EALLAQhAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-245 |
1.22e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 24 NAGEILHLVGPNGAGKS-TLLARMaGMTAGEGQIM------------LLEHTL----AE------WSPV-SLahrRSYL- 78
Cdd:PRK09473 40 RAGETLGIVGESGSGKSqTAFALM-GLLAANGRIGgsatfngreilnLPEKELnklrAEqismifQDPMtSL---NPYMr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 79 VQQQVppfaMPVwhyLMLHLHDKHSTALLTDVAA--ALGLEDKLSR---HVSQLSGGEWQRVRLA-AVIVQihpagnPhg 152
Cdd:PRK09473 116 VGEQL----MEV---LMLHKGMSKAEAFEESVRMldAVKMPEARKRmkmYPHEFSGGMRQRVMIAmALLCR------P-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 153 RMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPnlARAYN 231
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP--SHPYS 258
|
250
....*....|....*...
gi 495776072 232 M----SFRRLDIEGHKML 245
Cdd:PRK09473 259 IgllnAVPRLDAEGESLL 276
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
117-220 |
1.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 117 EDKLSRHVSQLSGGEWQRVRLAAvIVQIHPagnphgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHT 196
Cdd:PRK13649 136 ESLFEKNPFELSGGQMRRVAIAG-ILAMEP------KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDV 208
|
90 100
....*....|....*....|....
gi 495776072 197 LRHAHRVWLLSQGKMIASGTRDQV 220
Cdd:PRK13649 209 ANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-191 |
1.30e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHtlaewsPVSLAHRRSYLVQQQVPP------FAM 88
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGK------TATRGDRSRFMAYLGHLPglkadlSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYLMlHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGewQRVRLAAVIVQIHPAgnphgRMLLLDEPMSGLDVAQ 168
Cdd:PRK13543 101 ENLHFLC-GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAG--QKKRLALARLWLSPA-----PLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|...
gi 495776072 169 QAALDTLLSALSRKGIAVVMSSH 191
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTH 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-226 |
1.70e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVSLAHRRSYLVqqqvppFAMPVWHYL 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSKLQGIRKLVGIV------FQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 -------------MLHLHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPM 161
Cdd:PRK13644 92 grtveedlafgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT-MEP------ECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 162 SGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHtLRHAHRVWLLSQGKMIASGTRDQVLTPPNL 226
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
117-216 |
1.88e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 117 EDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNH 195
Cdd:PRK13645 141 EDYVKRSPFELSGGQKRRVALAGIIAM-------DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQ 213
|
90 100
....*....|....*....|.
gi 495776072 196 TLRHAHRVWLLSQGKMIASGT 216
Cdd:PRK13645 214 VLRIADEVIVMHEGKVISIGS 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-216 |
1.99e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 27 EILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYLMLHLHDKHST-- 104
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSwe 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 105 -------ALLTDVaaalGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNphGRMLLLDEPMSGLD-VAQQAALDTLL 176
Cdd:TIGR01257 1037 eaqlemeAMLEDT----GLHHKRNEEAQDLSGGMQRKLSVAIAFV-----GD--AKVVVLDEPTSGVDpYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495776072 177 SalSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:TIGR01257 1106 K--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-213 |
2.53e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTL---LARMAGMTAGEGQIMllEHTLAEWSPVSLAH-RRSYLvqqqvpPFAMPVW 91
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLmniLGCLDKPTSGTYRVA--GQDVATLDADALAQlRREHF------GFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HyLMLHLHDKHST-------------------ALLTdvaaALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHG 152
Cdd:PRK10535 96 H-LLSHLTAAQNVevpavyaglerkqrllraqELLQ----RLGLEDRVEYQPSQLSGGQQQRVSIARALMN-------GG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 153 RMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDlNHTLRHAHRVWLLSQGKMIA 213
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-201 |
2.80e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.47 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslahRRSYLVQ----QQVppfAMP 89
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIGMPEGEDLLFLP-----QRPYLPLgtlrEQL---IYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 vWHylmlhlhdkhstalltdvaaalgledklsrhvSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDvaqQ 169
Cdd:cd03223 88 -WD--------------------------------DVLSGGEQQRLAFARLLLH-----KP--KFVFLDEATSALD---E 124
|
170 180 190
....*....|....*....|....*....|..
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHdlNHTLRHAH 201
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH--RPSLWKFH 154
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
16-228 |
1.15e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPpFampVWHYL 94
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeQPEAGTIRVGDITIDTARSLSQQKGLIRQLRQHVG-F---VFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHLH------------------DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLL 156
Cdd:PRK11264 95 NLFPHrtvleniiegpvivkgepKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL-----AMRP--EVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 157 LDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLAR 228
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
12-233 |
1.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGEGQIMLlEHTLAEWSPVSLA--HRRSYLVQQ--QVP 84
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALlkpSSGTITIAG-YHITPETGNKNLKklRKKVSLVFQfpEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 PFAMPVWHYLM-----LHLHDKHSTALLTDVAAALGL-EDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLD 158
Cdd:PRK13641 98 LFENTVLKDVEfgpknFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA-YEP------EILCLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 159 EPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLARAYNMS 233
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLD 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
107-193 |
1.23e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 107 LTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALDTLLSALSrKGIAV 186
Cdd:PRK13409 193 LDEVVERLGLENILDRDISELSGGELQRVAIAAALLR-------DADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYV 264
|
....*..
gi 495776072 187 VMSSHDL 193
Cdd:PRK13409 265 LVVEHDL 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-224 |
1.49e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKS-TLLARMAGMTAGEGQI----MLLEH------TLAEWSPVSLAHRR----SYLVQQQV----PPF 86
Cdd:PRK10261 42 GETLAIVGESGSGKSvTALALMRLLEQAGGLVqcdkMLLRRrsrqviELSEQSAAQMRHVRgadmAMIFQEPMtslnPVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AM--PVWHYLMLHLHDKHSTAL-----LTDVAAALGLEDKLSRHVSQLSGGEWQRVrLAAVIVQIHPAgnphgrMLLLDE 159
Cdd:PRK10261 122 TVgeQIAESIRLHQGASREEAMveakrMLDQVRIPEAQTILSRYPHQLSGGMRQRV-MIAMALSCRPA------VLIADE 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-215 |
1.51e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIML-------LEHTLAEWSPVSLAHRRSYL-----VQQQ 82
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITInninynkLDHKLAAQLGIGIIYQELSVideltVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 83 VPPFAMPVWHYLMLHLHD----KHSTALLTDVaaaLGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLD 158
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIDwremRVRAAMMLLR---VGLKVDLDEKVANLSISHKQMLEIAKTLML-------DAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 159 EPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASG 215
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-216 |
1.53e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPFAMPVWHYlmlhlhdkhs 103
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSIVKY---------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 104 talltDVAaaLGLE------DKLSRHVSQ-----------------LSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEP 160
Cdd:PRK13648 104 -----DVA--FGLEnhavpyDEMHRRVSEalkqvdmleradyepnaLSGGQKQRVAIAGVL-----ALNPS--VIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 161 MSGLDVAQQAALDTLLSAL-SRKGIAVVMSSHDLNHTLrHAHRVWLLSQGKMIASGT 216
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGT 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-191 |
1.72e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAG--EGQIMLLEHTLaewsPVSLAHRRSYLVQQQVPPFAMPVWH 92
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGviTGEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHlhdkhstALLTdvaaALGLEDKlsrhvSQLSGGewqrVRLAAvivqihpagNPHgrMLLLDEPMSGLDvaQQAAL 172
Cdd:cd03232 99 ALRFS-------ALLR----GLSVEQR-----KRLTIG----VELAA---------KPS--ILFLDEPTSGLD--SQAAY 145
|
170 180
....*....|....*....|.
gi 495776072 173 DT--LLSALSRKGIAVVMSSH 191
Cdd:cd03232 146 NIvrFLKKLADSGQAILCTIH 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-192 |
1.96e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEhtlaewsPVSLAH---RRSYLVQQQVppfampVWH-------Y 93
Cdd:TIGR03719 347 PGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEIGE-------TVKLAYvdqSRDALDPNKT------VWEeisggldI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLHLHDKHSTALLTDVAAALGLEDKLsrhVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALD 173
Cdd:TIGR03719 414 IKLGKREIPSRAYVGRFNFKGSDQQKK---VGQLSGGERNRVHLAKTLKS-------GGNVLLLDEPTNDLDVETLRALE 483
|
170
....*....|....*....
gi 495776072 174 TLLsaLSRKGIAVVMsSHD 192
Cdd:TIGR03719 484 EAL--LNFAGCAVVI-SHD 499
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
16-165 |
2.36e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLaRM-AGM---TAGEgqimllehtlaewspVSLAHRRsylVQQQVPP---FAM 88
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLL-RMvAGLeriTSGE---------------IWIGGRV---VNELEPAdrdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 pVWHYLMLHLH----------------DKHS-TALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQiHPAgnph 151
Cdd:PRK11650 81 -VFQNYALYPHmsvrenmayglkirgmPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR-EPA---- 154
|
170
....*....|....
gi 495776072 152 grMLLLDEPMSGLD 165
Cdd:PRK11650 155 --VFLFDEPLSNLD 166
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-220 |
2.51e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.51 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSpVSLAH-RRSYLVQQQVPPFAM- 88
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKPTSGKIIIDGVDITDKK-VKLSDiRKKVGLVFQYPEYQLf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 -----------PVwhylMLHLHDKHSTALLTDVAAALGL--EDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRML 155
Cdd:PRK13637 98 eetiekdiafgPI----NLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVV-----AMEP--KIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 156 LLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQV 220
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-224 |
2.92e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLlARMAGM--TAGEGQIMLLEHTLAEWSPVSLAHRRSYLvqQQVppFAMPvwhYLMLHLH 99
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTL-ARLLTMieTPTGGELYYQGQDLLKADPEAQKLLRQKI--QIV--FQNP---YGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 DKHSTALL------TDVAAA------------LGLE-DKLSRHVSQLSGGEWQRVRLA-AVIVqihpagNPhgRMLLLDE 159
Cdd:PRK11308 109 KKVGQILEepllinTSLSAAerrekalammakVGLRpEHYDRYPHMFSGGQRQRIAIArALML------DP--DVVVADE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 160 PMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNhTLRH-AHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLS-VVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-221 |
3.36e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.48 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 11 AEKGRLEPITGAVNAGEILHLVGPNGAGKST---LLARMAGMTagEGQIMLLEHTLAEWSPVSLAHRRSyLVQQQVPPFA 87
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDID--EGEILLDGHDLRDYTLASLRNQVA-LVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVWHYLMLHLHDKHSTALL---TDVAAALGLEDKLSRHVSQ--------LSGGEWQRVRLAAVIVQIHPagnphgrMLL 156
Cdd:PRK11176 431 DTIANNIAYARTEQYSREQIeeaARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSP-------ILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 157 LDEPMSGLDV----AQQAALDTLlsalsRKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGTRDQVL 221
Cdd:PRK11176 504 LDEATSALDTeserAIQAALDEL-----QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
126-224 |
4.63e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 126 QLSGGEWQRVRLA-AVIVQihpagnphGRMLLLDEPMSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRV 203
Cdd:PRK15134 156 QLSGGERQRVMIAmALLTR--------PELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRV 227
|
90 100
....*....|....*....|.
gi 495776072 204 WLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK15134 228 AVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-192 |
5.57e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.72 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM---TAGEgqIMLLEHTLAEWSPvslAHRRSYLVQQQvppFAMpvwhYLMLHLH 99
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLediTSGD--LFIGEKRMNDVPP---AERGVGMVFQS---YAL----YPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 100 DKHSTAL-------------LTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDV 166
Cdd:PRK11000 94 ENMSFGLklagakkeeinqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV-----AEP--SVFLLDEPLSNLDA 166
|
170 180
....*....|....*....|....*..
gi 495776072 167 AQQAALDTLLSALSRK-GIAVVMSSHD 192
Cdd:PRK11000 167 ALRVQMRIEISRLHKRlGRTMIYVTHD 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
26-225 |
5.80e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.80 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEwspVSLAHRRSYLVQQQVPPFA-MPVWHYL-----MLHL 98
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDVTH---RSIQQRDICMVFQSYALFPhMSLGENVgyglkMLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 -----HDKHSTAL-LTDVAaalGLEDklsRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLDVAQQAAL 172
Cdd:PRK11432 109 pkeerKQRVKEALeLVDLA---GFED---RYVDQISGGQQQRVALARALI-LKP------KVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 173 -DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPN 225
Cdd:PRK11432 176 rEKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-220 |
1.22e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEHTLAEWSPvslAHRR----SYlvqqqVP---------PfAM 88
Cdd:COG3845 281 VRAGEILGIAGVAGNGQSELAEALAGLrPPASGSIRLDGEDITGLSP---RERRrlgvAY-----IPedrlgrglvP-DM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 89 PVWHYLMLHLHDKH--STALLTDVAAALGLEDKLSR-----------HVSQLSGGEWQRVRLAAVIvqihpAGNPhgRML 155
Cdd:COG3845 352 SVAENLILGRYRRPpfSRGGFLDRKAIRAFAEELIEefdvrtpgpdtPARSLSGGNQQKVILAREL-----SRDP--KLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 156 LLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQV 220
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
120-203 |
1.65e-07 |
|
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: 50.33 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 120 LSRHVSQLSGGEWQRVRLAAvivQIHpaGNPHGRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNhTLRH 199
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLAT---QIG--SGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED-TIRA 204
|
....
gi 495776072 200 AHRV 203
Cdd:cd03270 205 ADHV 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-191 |
1.77e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGR--LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLlehTLAEWSPVSLAH-RRSY-LVQQQVppFA 87
Cdd:TIGR01271 1229 EAGRavLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQI---DGVSWNSVTLQTwRKAFgVIPQKV--FI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVWHYLMLHLHDKHSTALLTDVAAALGLE-------DKLSRHVSQ----LSGGEWQRVRLAAVIVQihpagnpHGRMLL 156
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQWSDEEIWKVAEEVGLKsvieqfpDKLDFVLVDggyvLSNGHKQLMCLARSILS-------KAKILL 1376
|
170 180 190
....*....|....*....|....*....|....*.
gi 495776072 157 LDEPMSGLD-VAQQAALDTLLSALSrkGIAVVMSSH 191
Cdd:TIGR01271 1377 LDEPSAHLDpVTLQIIRKTLKQSFS--NCTVILSEH 1410
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
109-226 |
1.86e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 109 DVAAALGLEDKLSRHVSQLSGGEWQRVRLAAvIVQIHPagnphgRMLLLDEPMSGLDVA-QQAALDTLLSALSRKGIAVV 187
Cdd:PRK13640 126 DVLADVGMLDYIDSEPANLSGGQKQRVAIAG-ILAVEP------KIIILDESTSMLDPAgKEQILKLIRKLKKKNNLTVI 198
|
90 100 110
....*....|....*....|....*....|....*....
gi 495776072 188 MSSHDLNHTlRHAHRVWLLSQGKMIASGTRDQVLTPPNL 226
Cdd:PRK13640 199 SITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-192 |
2.00e-07 |
|
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: 51.47 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAGM-TAGEGQIMLlehtlaewspvSLAHRRSYLVQQ-QVPPfAMPVWHYLMLHLHD-KHSTALL 107
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVdKDFNGEARP-----------QPGIKVGYLPQEpQLDP-TKTVRENVEEGVAEiKDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 108 TDVAAALG---------------LEDKLSRH------------------------VSQLSGGEWQRVRLAAVIVQihpag 148
Cdd:TIGR03719 104 NEISAKYAepdadfdklaaeqaeLQEIIDAAdawdldsqleiamdalrcppwdadVTKLSGGERRRVALCRLLLS----- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495776072 149 NPHgrMLLLDEPMSGLDVAQQAALDTLLSALsrKGiAVVMSSHD 192
Cdd:TIGR03719 179 KPD--MLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHD 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-216 |
2.17e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.50 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVSLAHRRSYLVQQQVPPF-AMP 89
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFvGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWHYLMLHLHDK---HSTaLLTDVAAAL---GLEDKLSRHVSQLSGGEWQRVRLAAViVQIHPAgnphgrMLLLDEPMSG 163
Cdd:PRK13650 99 VEDDVAFGLENKgipHEE-MKERVNEALelvGMQDFKEREPARLSGGQKQRVAIAGA-VAMRPK------IIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 164 LDV-AQQAALDTLLSALSRKGIAVVMSSHDLNHtLRHAHRVWLLSQGKMIASGT 216
Cdd:PRK13650 171 LDPeGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTST 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-198 |
2.47e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAG-MTAGEGQIMLlehtlaewspvSLAHRRSYLVQQQVP---PFAMPVWHylMLHLHDKHSTAL 106
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGeLAPVSGEIGL-----------AKGIKLGYFAQHQLEflrADESPLQH--LARLAPQELEQK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 107 LTDVAAALGLE-DKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVAQQAALDTLLsaLSRKGiA 185
Cdd:PRK10636 410 LRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQ-----RPN--LLLLDEPTNHLDLDMRQALTEAL--IDFEG-A 479
|
170
....*....|...
gi 495776072 186 VVMSSHDlNHTLR 198
Cdd:PRK10636 480 LVVVSHD-RHLLR 491
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-191 |
2.49e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 9 DVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEwspvslaHRRSYLVQQQVPPFA 87
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSIKK-------DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 MPVWHYLMLH---LHDKH--STAL-LTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPM 161
Cdd:PRK13540 83 SGINPYLTLRencLYDIHfsPGAVgITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMS-------KAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|
gi 495776072 162 SGLDVAQQAALDTLLSALSRKGIAVVMSSH 191
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-214 |
2.91e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGM-TAG--EGQImLLEHTLAEWSPVSLAHRRSYLVQQQ----VP----------- 84
Cdd:NF040905 24 VREGEIHALCGENGAGKSTLMKVLSGVyPHGsyEGEI-LFDGEVCRFKDIRDSEALGIVIIHQelalIPylsiaeniflg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 ----PFAMPVWHYLMlhlhdKHSTALLTDVaaalGLEDKLSRHVSQLSGGEWQrvrlaavIVQIHPAGNPHGRMLLLDEP 160
Cdd:NF040905 103 neraKRGVIDWNETN-----RRARELLAKV----GLDESPDTLVTDIGVGKQQ-------LVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495776072 161 MSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIAS 214
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-224 |
3.02e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTL---LARMAGMTAGE----GQIMlleHTLAEWSPVSLAHRRSYLVQQqvpPFA---------MP 89
Cdd:PRK10261 350 GETLSLVGESGSGKSTTgraLLRLVESQGGEiifnGQRI---DTLSPGKLQALRRDIQFIFQD---PYAsldprqtvgDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 90 VWHYLMLH--LHDKHSTALLTDVAAALGLEDKLS-RHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDV 166
Cdd:PRK10261 424 IMEPLRVHglLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARAL-----ALNP--KVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 167 AQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-167 |
3.68e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.18 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG----EGQIMLLEHTLAEWSpvSLAHRRSYLVQQQvppfa 87
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYNGIPYKEFA--EKYPGEIIYVSEE----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 88 mpvwhylmlHLHDKHSTALLT-DVAAALgledKLSRHVSQLSGGEWQRVRLAAVIVqihpaGNPhgRMLLLDEPMSGLDV 166
Cdd:cd03233 92 ---------DVHFPTLTVRETlDFALRC----KGNEFVRGISGGERKRVSIAEALV-----SRA--SVLCWDNSTRGLDS 151
|
.
gi 495776072 167 A 167
Cdd:cd03233 152 S 152
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
119-193 |
3.68e-07 |
|
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: 48.86 E-value: 3.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495776072 119 KLSRHVSQLSGGEWQRVRLAAvivqiHPAGNPHGRMLLLDEPMSGLDvaqQAALDTLLSALSR---KGIAVVMSSHDL 193
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLAS-----ELFSEPPGTLFILDEPSTGLH---QQDINQLLEVIKGlidLGNTVILIEHNL 149
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-222 |
4.46e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAG---MTAGEGQIML--------------LEHTLAEWSPVSLAHRRSYLVQqqvp 84
Cdd:PRK11147 25 HIEDNERVCLVGRNGAGKSTLMKILNGevlLDDGRIIYEQdlivarlqqdpprnVEGTVYDFVAEGIEEQAEYLKR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 pfampvWHYLMLHLHDKHSTALL----------------------TDVAAALGLE-DKLsrhVSQLSGGeWQR-VRLAAV 140
Cdd:PRK11147 101 ------YHDISHLVETDPSEKNLnelaklqeqldhhnlwqlenriNEVLAQLGLDpDAA---LSSLSGG-WLRkAALGRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 141 IVQihpagNPhgRMLLLDEPMSGLDVAQQAALDTLLsaLSRKGiAVVMSSHDLNHTLRHAHRVWLLSQGKMIA-SGTRDQ 219
Cdd:PRK11147 171 LVS-----NP--DVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLVSyPGNYDQ 240
|
...
gi 495776072 220 VLT 222
Cdd:PRK11147 241 YLL 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-191 |
4.59e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAGmtagegqimllehtLAEWSPVSLAHRrsylvqqqVPPFAMPVWHYLMLHLHDKH 102
Cdd:COG2401 53 IEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVD--------VPDNQFGREASLIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 103 STALLTDVAAALGLEDK--LSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLD--VAQQAALdTLLSA 178
Cdd:COG2401 111 DFKDAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLL-----AERP--KLLVIDEFCSHLDrqTAKRVAR-NLQKL 182
|
170
....*....|...
gi 495776072 179 LSRKGIAVVMSSH 191
Cdd:COG2401 183 ARRAGITLVVATH 195
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
27-203 |
5.24e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.40 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 27 EILHLVGPNGAGKSTLLA---RMAGMTAG---EGQIMLLEHTL--AEWSPVSLaHRRSYLVQQQVPPFAMPVWHYL---- 94
Cdd:PRK14243 37 QITAFIGPSGCGKSTILRcfnRLNDLIPGfrvEGKVTFHGKNLyaPDVDPVEV-RRRIGMVFQKPNPFPKSIYDNIayga 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 --------MLHLHDK--HSTALLTDVaaalglEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGL 164
Cdd:PRK14243 116 ringykgdMDELVERslRQAALWDEV------KDKLKQSGLSLSGGQQQRLCIARAIA-VQP------EVILMDEPCSAL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 495776072 165 DVAQQAALDTLLSALSRKGIAVVMSshdlnHTLRHAHRV 203
Cdd:PRK14243 183 DPISTLRIEELMHELKEQYTIIIVT-----HNMQQAARV 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-228 |
5.40e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.20 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARM--------AGMTAGEGQIMLLEHT-----LAEWSPVSLAHRRSYLVQQQ 82
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpseGSIVVNGQTINLVRDKdgqlkVADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 83 VPPFA-MPVWHYLM------LHLHDKHSTALLTDVAAALGLEDKL-SRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrM 154
Cdd:PRK10619 101 FNLWShMTVLENVMeapiqvLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARAL-----AMEPE--V 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 155 LLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPPNLAR 228
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
15-193 |
6.11e-07 |
|
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: 48.34 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMllehtlaEWSPVSLAHRRSYLvqqqvppfampvwhyl 94
Cdd:cd03222 14 FLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------EWDGITPVYKPQYI---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 mlhlhdkhstalltdvaaalgledklsrhvsQLSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQAALDT 174
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLR-------NATFYLFDEPSAYLDIEQRLNAAR 112
|
170 180
....*....|....*....|
gi 495776072 175 LLSALSRKGI-AVVMSSHDL 193
Cdd:cd03222 113 AIRRLSEEGKkTALVVEHDL 132
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-224 |
6.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.07 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 28 ILHLVGPNGAGKSTLLA---RMAGMTAG---EGQIMLLEHTL--AEWSPVSLaHRRSYLVQQQVPPFA-MPVWHYLMLHL 98
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRtfnRLLELNEEarvEGEVRLFGRNIysPDVDPIEV-RREVGMVFQYPNPFPhLTIYDNVAIGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 99 H-----------DKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPhgRMLLLDEPMSGLDVA 167
Cdd:PRK14267 111 KlnglvkskkelDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL-----AMKP--KILLMDEPTANIDPV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 168 QQAALDTLLSALsRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK14267 184 GTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-219 |
6.92e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 5 MQLTDVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMT-AGEGQIMLLEHTLAEWSPVSlAHRRSYLV---- 79
Cdd:PRK11288 258 LRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATrRTAGQVYLDGKPIDIRSPRD-AIRAGIMLcped 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 80 --QQQVPPFAmPVWHYLMLHLHDKHSTA--LLTDvaaalGLEDKLSRH---------------VSQLSGGEWQRVRLaav 140
Cdd:PRK11288 337 rkAEGIIPVH-SVADNINISARRHHLRAgcLINN-----RWEAENADRfirslniktpsreqlIMNLSGGNQQKAIL--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 141 ivqihpagnphGR-------MLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIA 213
Cdd:PRK11288 408 -----------GRwlsedmkVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
....*.
gi 495776072 214 SGTRDQ 219
Cdd:PRK11288 477 ELAREQ 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-211 |
8.32e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 12 EKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIMLLEHTLAEWSPV-SLAHRRSYLVQQQ-----VP 84
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKrAGGEIRLNGKDISPRSPLdAVKKGMAYITESRrdngfFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 85 PFA----MPV--------WHYLMLHLHDKHSTALLTDVAAALGLE-DKLSRHVSQLSGGEWQRVRLAAVIVqihpagnPH 151
Cdd:PRK09700 355 NFSiaqnMAIsrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLC-------CC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 152 GRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-210 |
8.53e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 48.23 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQimllehtlaewspVSLAHRRSYLVQQqvpPFAMP-------VWHYL 94
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGS-------------VSVPGSIAYVSQE---PWIQNgtireniLFGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MlhlhDK-------HSTALLTDVAAalgLEDKLSRHVSQ----LSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSG 163
Cdd:cd03250 92 F----DEeryekviKACALEPDLEI---LPDGDLTEIGEkginLSGGQKQRISLARAVYSDAD-------IYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495776072 164 LD--VAQQAALDTLLSALsRKGIAVVMSSHDLnHTLRHAHRVWLLSQGK 210
Cdd:cd03250 158 VDahVGRHIFENCILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-211 |
1.29e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 29 LHLVGPNGAGKSTLLARMAGmtagegqimllehtlaEWSPVSLAHRRSylvqqqvPPFAMPVWHYLMLHLHDKHSTALLT 108
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISG----------------ELQPSSGTVFRS-------AKVRMAVFSQHHVDGLDLSSNPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 109 DVAAALG-LEDKLSRHVSQ--------------LSGGEWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDVaqqAALD 173
Cdd:PLN03073 595 MMRCFPGvPEQKLRAHLGSfgvtgnlalqpmytLSGGQKSRVAFAKITFK-----KPH--ILLLDEPSNHLDL---DAVE 664
|
170 180 190
....*....|....*....|....*....|....*...
gi 495776072 174 TLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKM 211
Cdd:PLN03073 665 ALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-220 |
1.46e-06 |
|
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: 48.65 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE---GQIM-----------------------LLEHTLAE---- 65
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIIyhvalcekcgyverpskvgepcpVCGGTLEPeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 66 -WSP-----VSLAHRRSYLVQQQvppFAM----PVWHYLMLHLHD-----KHSTALLTDVAAALGLEDKLSRHVSQLSGG 130
Cdd:TIGR03269 96 fWNLsdklrRRIRKRIAIMLQRT---FALygddTVLDNVLEALEEigyegKEAVGRAVDLIEMVQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 131 EWQRVRLAAVIVQihpagNPHgrMLLLDEPMSGLDvAQQAAL--DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQ 208
Cdd:TIGR03269 173 EKQRVVLARQLAK-----EPF--LFLADEPTGTLD-PQTAKLvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250
....*....|..
gi 495776072 209 GKMIASGTRDQV 220
Cdd:TIGR03269 245 GEIKEEGTPDEV 256
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-216 |
2.09e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.20 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAewsPVSLAHRR--SYL-----------VQQQvppfampvw 91
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGlLPASEGEAWLFGQPVD---AGDIATRRrvGYMsqafslygeltVRQN--------- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 hyLMLH-----LHDKHSTALLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqihpagnpHG-RMLLLDEPMSGLD 165
Cdd:NF033858 360 --LELHarlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI--------HKpELLILDEPTSGVD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 166 vaqQAALD---TLLSALSRK-GIAVVMSSHDLNHTLRhAHRVWLLSQGKMIASGT 216
Cdd:NF033858 430 ---PVARDmfwRLLIELSREdGVTIFISTHFMNEAER-CDRISLMHAGRVLASDT 480
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-230 |
2.73e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 120 LSRHVSQLSGGEWQRVRLAAvivQIhpAGNPHGRMLLLDEPMSGLdvaQQAALDTLLSALSR---KGIAVVMSSHDlNHT 196
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLAT---QI--GSGLTGVLYVLDEPSIGL---HQRDNRRLINTLKRlrdLGNTLIVVEHD-EDT 552
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 495776072 197 LRHAHRVWLLSQ------GKMIASGTRDQVLTPPN-LARAY 230
Cdd:TIGR00630 553 IRAADYVIDIGPgagehgGEVVASGTPEEILANPDsLTGQY 593
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-214 |
3.58e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGM---TAGE----GQIMLLEHTLAewspvSLAHRRSYLVQ--QQVPpf 86
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyqpDAGSilidGQEMRFASTTA-----ALAAGVAIIYQelHLVP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMPVWHYLML-HLHDK----HSTALLTDVA---AALGLEDKLSRHVSQLSGGEWQrvrlaavIVQIHPAGNPHGRMLLLD 158
Cdd:PRK11288 93 EMTVAENLYLgQLPHKggivNRRLLNYEAReqlEHLGVDIDPDTPLKYLSIGQRQ-------MVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495776072 159 EPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIAS 214
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-216 |
3.62e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 119 KLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphGRML-LLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLnHTL 197
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRST-----GKTLyILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVI 235
|
90 100
....*....|....*....|....*..
gi 495776072 198 RHAHrvWLLS--------QGKMIASGT 216
Cdd:cd03271 236 KCAD--WIIDlgpeggdgGGQVVASGT 260
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
125-193 |
3.75e-06 |
|
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: 47.00 E-value: 3.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495776072 125 SQLSGGEWqrvRLAAVIVQIHPAGNPhGRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDL 193
Cdd:pfam13304 235 FELSDGTK---RLLALLAALLSALPK-GGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-224 |
4.17e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAGMTAGEGQIM----------LLEHTLAEWSPVsLAHRRSYLVQQQ---VPPF------ 86
Cdd:PRK15093 33 GEIRGLVGESGSGKSLIAKAICGVTKDNWRVTadrmrfddidLLRLSPRERRKL-VGHNVSMIFQEPqscLDPServgrq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 ---AMPVWHY-----LMLHLHDKHSTALLTDVaaalGLEDK---LSRHVSQLSGGEWQRVRLAavivqIHPAGNPhgRML 155
Cdd:PRK15093 112 lmqNIPGWTYkgrwwQRFGWRKRRAIELLHRV----GIKDHkdaMRSFPYELTEGECQKVMIA-----IALANQP--RLL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 156 LLDEPMSGLDVAQQAALDTLLSALSR-KGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-216 |
4.17e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTA---GEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQvpPFAMP-VW 91
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykiLEGDILFKGESILDLEPEERAHLGIFLAFQY--PIEIPgVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 H--YLMLHLHDKHSTALLTDVAAALGLE---DK----------LSRHVSQ-LSGGEWQRVRLAAVIVQihpagNPhgRML 155
Cdd:CHL00131 101 NadFLRLAYNSKRKFQGLPELDPLEFLEiinEKlklvgmdpsfLSRNVNEgFSGGEKKRNEILQMALL-----DS--ELA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 156 LLDEPMSGLDVaqqAALDTL---LSALSRKGIAVVMSSH----------DLNHTLRHahrvwllsqGKMIASGT 216
Cdd:CHL00131 174 ILDETDSGLDI---DALKIIaegINKLMTSENSIILITHyqrlldyikpDYVHVMQN---------GKIIKTGD 235
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
97-227 |
4.52e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 97 HLHDK-HstALLTdvaaaLGLED-KLSRHVSQLSGGEWQRVRLAAVIVqihpAGNPHGRMLLLDEPMSGLDVAQQAALDT 174
Cdd:PRK00635 785 SIHEKiH--ALCS-----LGLDYlPLGRPLSSLSGGEIQRLKLAYELL----APSKKPTLYVLDEPTTGLHTHDIKALIY 853
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 175 LLSALSRKGIAVVMSSHDLnHTLRHAHRVWLLSQ------GKMIASGTRDQVL---TPPNLA 227
Cdd:PRK00635 854 VLQSLTHQGHTVVIIEHNM-HVVKVADYVLELGPeggnlgGYLLASCSPEELIhlhTPTAKA 914
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
106-220 |
7.74e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 106 LLTDVaaalGLED-KLSRHVSQLSGGEWQRVRLAAVIVQihpagNPHGRML-LLDEPMSGL---DVAQqaaLDTLLSALS 180
Cdd:TIGR00630 812 TLCDV----GLGYiRLGQPATTLSGGEAQRIKLAKELSK-----RSTGRTLyILDEPTTGLhfdDIKK---LLEVLQRLV 879
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 495776072 181 RKGIAVVMSSHDLnHTLRHAHrvWLL--------SQGKMIASGTRDQV 220
Cdd:TIGR00630 880 DKGNTVVVIEHNL-DVIKTAD--YIIdlgpeggdGGGTVVASGTPEEV 924
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-165 |
8.39e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAGM-TAGEGQimllehtlAEWSPvslAHRRSYLvqQQVPPF--AMPVWHYLMLHLHDKhsTALL 107
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVdKEFEGE--------ARPAP---GIKVGYL--PQEPQLdpEKTVRENVEEGVAEV--KAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 108 T---DVAAALG---------------LEDKLSRH------------------------VSQLSGGEWQRVRLAAVIVQih 145
Cdd:PRK11819 103 DrfnEIYAAYAepdadfdalaaeqgeLQEIIDAAdawdldsqleiamdalrcppwdakVTKLSGGERRRVALCRLLLE-- 180
|
170 180
....*....|....*....|
gi 495776072 146 pagNPHgrMLLLDEPMSGLD 165
Cdd:PRK11819 181 ---KPD--MLLLDEPTNHLD 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-216 |
1.18e-05 |
|
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: 46.16 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 22 AVNAGEILHLVGPNGAGKSTLLARMAGMTAgegqIMLLEHTLAEWS---PVSLAHRR-SYLVQQQVPPFAMPVWHYLMLH 97
Cdd:TIGR01257 1961 GVRPGECFGLLGVNGAGKTTTFKMLTGDTT----VTSGDATVAGKSiltNISDVHQNmGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 98 LHDKHSTALLTDVAA-----ALGLEDKLSRHVSQLSGGEWQRVRLAAVIVQIHPagnphgrMLLLDEPMSGLDVAQQAAL 172
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVAnwsiqSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP-------LVLLDEPTTGMDPQARRML 2109
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495776072 173 DTLLSALSRKGIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-232 |
1.46e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.86 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHTLAEWSPVSLahRRSYLVQQQVPP------FA----------MPVWHY 93
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGyYPLTEGEIRLDGRPLSSLSHSVL--RQGVAMVQQDPVvladtfLAnvtlgrdiseEQVWQA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LmlhlhdkhSTALLTDVAAAL--GLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAA 171
Cdd:PRK10790 450 L--------ETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ-----TP--QILILDEATANIDSGTEQA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495776072 172 LDTLLSALsRKGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGTRDQVLTPPnlARAYNM 232
Cdd:PRK10790 515 IQQALAAV-REHTTLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQLLAAQ--GRYWQM 571
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
114-216 |
1.67e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.16 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 114 LGLE-DKLSRHVSQLSGGEWQRVRLAAVIvqihpAGNPHgrMLLLDEPMSGLDVAQQAALDTLLSALS-RKGIAVVMSSH 191
Cdd:PRK13646 132 LGFSrDVMSQSPFQMSGGQMRKIAIVSIL-----AMNPD--IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSH 204
|
90 100
....*....|....*....|....*
gi 495776072 192 DLNHTLRHAHRVWLLSQGKMIASGT 216
Cdd:PRK13646 205 DMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-192 |
2.20e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 25 AGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLLEhtlaewsPVSLAHrrsylVQQQVPpfAMP----VWH------- 92
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQeQPDSGTIKIGE-------TVKLAY-----VDQSRD--ALDpnktVWEeisggld 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 93 YLMLHLHDKHSTALLtdvaAALGLE--DKlSRHVSQLSGGEWQRVRLAAVIVQihpAGNphgrMLLLDEPMSGLDVAQQA 170
Cdd:PRK11819 415 IIKVGNREIPSRAYV----GRFNFKggDQ-QKKVGVLSGGERNRLHLAKTLKQ---GGN----VLLLDEPTNDLDVETLR 482
|
170 180
....*....|....*....|..
gi 495776072 171 ALDTLLsaLSRKGIAVVMsSHD 192
Cdd:PRK11819 483 ALEEAL--LEFPGCAVVI-SHD 501
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-215 |
2.28e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 10 VAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG---MTAGEGQIMLLEHTLAEWSPVSLAHRRSYLVQQQvpPF 86
Cdd:PRK09580 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQY--PV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 87 AMP--------------VWHYLMLHLHDKHSTA-LLTDVAAALGL-EDKLSRHVSQ-LSGGEWQR---VRLAAvivqIHP 146
Cdd:PRK09580 89 EIPgvsnqfflqtalnaVRSYRGQEPLDRFDFQdLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRndiLQMAV----LEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 147 AgnphgrMLLLDEPMSGLDVAQQAALDTLLSAL---SRKGIAVVMSSHDLNHTlrHAHRVWLLSQGKMIASG 215
Cdd:PRK09580 165 E------LCILDESDSGLDIDALKIVADGVNSLrdgKRSFIIVTHYQRILDYI--KPDYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-197 |
3.86e-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: 43.69 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLlehTLAEWSPVSLAH-RRSY-LVQQQVPPFAMPVwhY 93
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQI---DGVSWNSVPLQKwRKAFgVIPQKVFIFSGTF--R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 LMLHLHDKHSTALLTDVAAALGLEDKLSRHVSQ-----------LSGGEWQRVRLAAVIVQihpagnpHGRMLLLDEPMS 162
Cdd:cd03289 95 KNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLS-------KAKILLLDEPSA 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 495776072 163 GLD-VAQQAALDTLLSALSrkGIAVVMSSHDLNHTL 197
Cdd:cd03289 168 HLDpITYQVIRKTLKQAFA--DCTVILSEHRIEAML 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-224 |
4.31e-05 |
|
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: 44.02 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 15 RLEPITGAVNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQIMLLEHtlaewsPVSLAHRRSYlvQQQvppFAmPVW-- 91
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGEILLDGQ------PVTADNREAY--RQL---FS-AVFsd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 92 HYL---MLHLHDKHSTALLTDVAAALGLEDKLS---RHVS--QLSGGewQRVRLAAVIV-----QIhpagnphgrmLLLD 158
Cdd:COG4615 415 FHLfdrLLGLDGEADPARARELLERLELDHKVSvedGRFSttDLSQG--QRKRLALLVAlledrPI----------LVFD 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495776072 159 EpmsgldvaqQAAlD-----------TLLSALSRKGIAVVMSSHDlNHTLRHAHRVWLLSQGKmIASGTRDQVLTPP 224
Cdd:COG4615 483 E---------WAA-DqdpefrrvfytELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGK-LVELTGPAALAAS 547
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-166 |
5.05e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLEHTlaeWspvSLAhrrsyLVQQQVPPFAMPVWHYLM 95
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN---W---QLA-----WVNQETPALPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 96 ------------LHL----HDKHSTALL------------TDVAAAL--GL---EDKLSRHVSQLSGGEWQRVRLAAVIV 142
Cdd:PRK10636 86 dgdreyrqleaqLHDanerNDGHAIATIhgkldaidawtiRSRAASLlhGLgfsNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180
....*....|....*....|....
gi 495776072 143 qihpagnPHGRMLLLDEPMSGLDV 166
Cdd:PRK10636 166 -------CRSDLLLLDEPTNHLDL 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-200 |
7.29e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLLARMAGMTAGEGQIMLLehtlaewspvslahrrsylvqqqvppfampvwhylmlhlhdkHSTA 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 106 LLTDVAAALGLEDKLSRHVSQLSGGEWQRVRLAAVIvqihpagNPHGRMLLLDEPMSGLDVAQQAAL------DTLLSAL 179
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR-------KLKPDVLILDEITSLLDAEQEALLllleelRLLLLLK 112
|
170 180
....*....|....*....|.
gi 495776072 180 SRKGIAVVMSSHDLNHTLRHA 200
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPAL 133
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-222 |
9.44e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 4 LMQLTDVAEKGR------LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAGE-GQIMLLEHTLAEWSPVSLahRRS 76
Cdd:PLN03232 1234 SIKFEDVHLRYRpglppvLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDL--RRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 77 YLVQQQVP------------PFAMPVWHYLMLHLHDKHstalLTDVA--AALGLEDKLSRHVSQLSGGEWQRVRLAAVIV 142
Cdd:PLN03232 1312 LSIIPQSPvlfsgtvrfnidPFSEHNDADLWEALERAH----IKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 143 QihpagnpHGRMLLLDEPMSGLDVaqqaALDTLLSALSR---KGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGTRDQ 219
Cdd:PLN03232 1388 R-------RSKILVLDEATASVDV----RTDSLIQRTIReefKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQE 1455
|
...
gi 495776072 220 VLT 222
Cdd:PLN03232 1456 LLS 1458
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
119-193 |
1.03e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 119 KLSRHVSQLSGGEWQRVRLAAVIVQIHpagnpHGRML-LLDEPMSGL---DVAQqaaldtLLSALSR---KGIAVVMSSH 191
Cdd:COG0178 819 KLGQPATTLSGGEAQRVKLASELSKRS-----TGKTLyILDEPTTGLhfhDIRK------LLEVLHRlvdKGNTVVVIEH 887
|
..
gi 495776072 192 DL 193
Cdd:COG0178 888 NL 889
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-212 |
1.20e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.39 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 2 SLLMQLTDVAEKGRLEPITGAVNAGEILHLVGPNGAGKST-------LLARMAGMTAGEGQIMLLEHTLAEWSPVSLAHR 74
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTtarlidgLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 75 R------SYLVQQQVPpFAMPVWHYLMLHLHDKHSTALLtdvaaALGLEDKLSRHVSQLSGGEWQRVRLAAVIVqIHPag 148
Cdd:PRK13642 89 NpdnqfvGATVEDDVA-FGMENQGIPREEMIKRVDEALL-----AVNMLDFKTREPARLSGGQKQRVAVAGIIA-LRP-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 149 nphgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMS-SHDLNHTLRhAHRVWLLSQGKMI 212
Cdd:PRK13642 160 ----EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAAS-SDRILVMKAGEII 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-222 |
1.32e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 8 TDVAEKGRLEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTAG-----EGQIMLLEHTLAEWSPvslaHRRS------ 76
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhigvEGVITYDGITPEEIKK----HYRGdvvyna 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 77 -------YLVQQQVPPFAM----PVWHYLMLHLHD--KHSTALltdVAAALGLE--------DKLSRHVsqlSGGEWQRV 135
Cdd:TIGR00956 145 etdvhfpHLTVGETLDFAArcktPQNRPDGVSREEyaKHIADV---YMATYGLShtrntkvgNDFVRGV---SGGERKRV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 136 RLAAVIVQihpagnpHGRMLLLDEPMSGLDVAQQ----AALDTLLSAL-SRKGIAVVMSSHDLNHTLrhaHRVWLLSQGK 210
Cdd:TIGR00956 219 SIAEASLG-------GAKIQCWDNATRGLDSATAlefiRALKTSANILdTTPLVAIYQCSQDAYELF---DKVIVLYEGY 288
|
250
....*....|..
gi 495776072 211 MIASGTRDQVLT 222
Cdd:TIGR00956 289 QIYFGPADKAKQ 300
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
31-192 |
2.31e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.10 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 31 LVGPNGAGKSTLLARMA----GMTAGEG-QIML-----LEHTLAEWSPVSLAHRRSYLVQQqvppfampvwhYLMLHLHD 100
Cdd:cd03279 33 ICGPTGAGKSTILDAITyalyGKTPRYGrQENLrsvfaPGEDTAEVSFTFQLGGKKYRVER-----------SRGLDYDQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 101 KHSTALLtdvaaALGLEDK-LSRHVSQLSGGEWQRVRLA---AVIVQIHPAGNPHGRMLLLDEPMSGLDVAQQAALDTLL 176
Cdd:cd03279 102 FTRIVLL-----PQGEFDRfLARPVSTLSGGETFLASLSlalALSEVLQNRGGARLEALFIDEGFGTLDPEALEAVATAL 176
|
170
....*....|....*.
gi 495776072 177 SALSRKGIAVVMSSHD 192
Cdd:cd03279 177 ELIRTENRMVGVISHV 192
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-224 |
2.77e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.31 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIMLLEHTLaEWSPVSLAHRRSYLVQQ------------- 81
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPL-HFGDYSYRSQRIRMIFQdpstslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 82 QVPPFAMPVWHYLMLHLHDKHSTALLTDVAAalgLEDKLSRHVSQLSGGEWQRVRLA-AVIVQihpagnphGRMLLLDEP 160
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLArALILR--------PKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495776072 161 MSGLDVAQQAALDTLLSALSRK-GIAVVMSSHDLNHTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
127-216 |
3.64e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.84 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 127 LSGGEWQRVRLAAVIVqIHPagnphgRMLLLDEPMSGLD-VAQQAALDTLLSALSRKGIAVVMSSHDLNHTLRhAHRVWL 205
Cdd:PRK13633 145 LSGGQKQRVAIAGILA-MRP------ECIIFDEPTAMLDpSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIV 216
|
90
....*....|.
gi 495776072 206 LSQGKMIASGT 216
Cdd:PRK13633 217 MDSGKVVMEGT 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-211 |
4.41e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 18 PITGAVNAGEILHLVGPNGAGKSTLLARMAGM-TAGEGQIMLlehtlaEWSPVSLAHRRSYlvQQQVPPFAMPVW--HYL 94
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILL------DGKPVTAEQPEDY--RKLFSAVFTDFHlfDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 95 MLHLHDKHSTALLTDVAAALGLEDKLS---RHVS--QLSGGewQRVRLAAVIvqihpAGNPHGRMLLLDEPMSGLD-VAQ 168
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLEledGRISnlKLSKG--QKKRLALLL-----ALAEERDILLLDEWAADQDpHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495776072 169 QAALDTLLSALSRKGIAVVMSSHDlNHTLRHAHRVWLLSQGKM 211
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
127-221 |
4.57e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.96 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 127 LSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAALDTLLSALSRKGIAVVMsSHDLNhTLRHAHRVWLL 206
Cdd:COG5265 495 LSGGEKQRVAIARTLLK-----NP--PILIFDEATSALDSRTERAIQAALREVARGRTTLVI-AHRLS-TIVDADEILVL 565
|
90
....*....|....*
gi 495776072 207 SQGKMIASGTRDQVL 221
Cdd:COG5265 566 EAGRIVERGTHAELL 580
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
106-224 |
4.81e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 106 LLTDVAAAL--GLEDKLSRHVSQLSGGEWQRVRLAAVIVQihpagNPhgRMLLLDEPMSGLDVAQQAALDTLLSAL--SR 181
Cdd:PTZ00265 557 LIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIR-----NP--KILILDEATSSLDNKSEYLVQKTINNLkgNE 629
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495776072 182 KGIAVVMsSHDLNhTLRHAHRVWLLSQGKMIASGTRDQVLTPP 224
Cdd:PTZ00265 630 NRITIII-AHRLS-TIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-48 |
1.26e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.26e-03
10 20
....*....|....*....|....*.
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG 48
Cdd:PRK10938 283 VNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
120-225 |
1.29e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 120 LSRHVSQLSGGEWQRVRLAAvivQIhpaG-NPHGRMLLLDEPMSGLdvaQQAALDTLLSALSR---KGIAVVMSSHDLNh 195
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLAT---QI---GsGLTGVLYVLDEPSIGL---HQRDNDRLIETLKHlrdLGNTLIVVEHDED- 552
|
90 100 110
....*....|....*....|....*....|....*...
gi 495776072 196 TLRHAHrvWLLS--------QGKMIASGTRDQVLTPPN 225
Cdd:PRK00349 553 TIRAAD--YIVDigpgagvhGGEVVASGTPEEIMKNPN 588
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-192 |
1.34e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 23 VNAGEILHLVGPNGAGKSTLLARMAG-MTAGEGQImllehtlaEWSPvslAHRRSYLVQQQVPPFA--------MPVWhy 93
Cdd:PRK15064 342 LEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTV--------KWSE---NANIGYYAQDHAYDFEndltlfdwMSQW-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 94 lMLHLHDKHStalltdVAAALGL----EDKLSRHVSQLSGGEWQRVRLAAVIVQIHpagnphgRMLLLDEPMSGLDVaqq 169
Cdd:PRK15064 409 -RQEGDDEQA------VRGTLGRllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKP-------NVLVMDEPTNHMDM--- 471
|
170 180
....*....|....*....|...
gi 495776072 170 AALDTLLSALSRKGIAVVMSSHD 192
Cdd:PRK15064 472 ESIESLNMALEKYEGTLIFVSHD 494
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
115-175 |
1.47e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 115 GLEDKLSRHVSQLSGGEwqRVRLAAVIV--------QIHPAGNPHGRMLLLDEPMSGLD-VAQQAALDTL 175
Cdd:pfam13558 21 GSEVETYRRSGGLSGGE--KQLLAYLPLaaalaaqyGSAEGRPPAPRLVFLDEAFAKLDeENIRTALELL 88
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-215 |
1.67e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 26 GEILHLVGPNGAGKSTLL-ARMAGMTAGEGQImllehtlaeWSPVSLAhrrsYLVQQqvpPFAMPVWHYLMLHLHDKHST 104
Cdd:PTZ00243 686 GKLTVVLGATGSGKSTLLqSLLSQFEISEGRV---------WAERSIA----YVPQQ---AWIMNATVRGNILFFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 105 ALLTDVA---------AAL--GLEDKLSRHVSQLSGGEWQRVRLA-AVIVqihpagnpHGRMLLLDEPMSGLD--VAQQA 170
Cdd:PTZ00243 750 ARLADAVrvsqleadlAQLggGLETEIGEKGVNLSGGQKARVSLArAVYA--------NRDVYLLDDPLSALDahVGERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495776072 171 ALDTLLSALSRKgiAVVMSSHDLnHTLRHAHRVWLLSQGKMIASG 215
Cdd:PTZ00243 822 VEECFLGALAGK--TRVLATHQV-HVVPRADYVVALGDGRVEFSG 863
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-233 |
2.04e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 39.16 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTL-LARMAGMTAGEGQIMLLEHTLAEwspVSLAHRRSYL-------------VQQ 81
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEGEIIIDGLNIAK---IGLHDLRFKItiipqdpvlfsgsLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 82 QVPPFAM----PVWHYLML-HLHDKHSTalltdvaaalgLEDKLSRHVSQ----LSGGEWQRVRLAAVIVQihpagnpHG 152
Cdd:TIGR00957 1379 NLDPFSQysdeEVWWALELaHLKTFVSA-----------LPDKLDHECAEggenLSVGQRQLVCLARALLR-------KT 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 153 RMLLLDEPMSGLDVAQqaalDTLLSALSR---KGIAVVMSSHDLNhTLRHAHRVWLLSQGKMIASGtrdqvlTPPNLARA 229
Cdd:TIGR00957 1441 KILVLDEATAAVDLET----DNLIQSTIRtqfEDCTVLTIAHRLN-TIMDYTRVIVLDKGEVAEFG------APSNLLQQ 1509
|
....*...
gi 495776072 230 ----YNMS 233
Cdd:TIGR00957 1510 rgifYSMA 1517
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
123-211 |
2.29e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776072 123 HVSQLSGGEWQRVrlaaVIvqihpagnphGRMLL-------LDEPMSGLDVAQQAALDTLLSALSRKGIAVVMSSHDLNH 195
Cdd:PRK10982 388 QIGSLSGGNQQKV----II----------GRWLLtqpeilmLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPE 453
|
90
....*....|....*.
gi 495776072 196 TLRHAHRVWLLSQGKM 211
Cdd:PRK10982 454 LLGITDRILVMSNGLV 469
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
127-193 |
3.33e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 3.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495776072 127 LSGGEWQRVRLAAvivQIHPAGNphGRML-LLDEPMSGL---DVAQqaaldtLLSALSR---KGIAVVMSSHDL 193
Cdd:PRK00349 831 LSGGEAQRVKLAK---ELSKRST--GKTLyILDEPTTGLhfeDIRK------LLEVLHRlvdKGNTVVVIEHNL 893
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-76 |
4.41e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.18 E-value: 4.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776072 16 LEPITGAVNAGEILHLVGPNGAGKSTLLARMAGMTA-GEGQIMLLEHTLAewspvSLAHRRS 76
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKiQQGRVEVLGGDMA-----DARHRRA 73
|
|
| |
