|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-258 |
3.07e-130 |
|
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: 368.99 E-value: 3.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA 86
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQI 246
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|..
gi 1560390145 247 IELPETNKPVVL 258
Cdd:COG1120 242 IEDPVTGRPLVL 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-255 |
1.80e-99 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 291.15 E-value: 1.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMsIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEA 244
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV-LHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEA 239
|
250
....*....|.
gi 1560390145 245 QIIELPETNKP 255
Cdd:PRK11231 240 EIHPEPVSGTP 250
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-261 |
2.44e-91 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 270.42 E-value: 2.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYGRYPYQKffsG-LNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSK---GrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQ 245
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIE 238
|
250
....*....|....*.
gi 1560390145 246 IIELPetNKPVVLSYD 261
Cdd:COG4604 239 VEEID--GKRICVYFR 252
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-258 |
2.01e-81 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 245.67 E-value: 2.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 12 ITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEH 91
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 PLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:PRK10253 93 PGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 172 FLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIELPE 251
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPV 252
|
....*..
gi 1560390145 252 TNKPVVL 258
Cdd:PRK10253 253 AGTPLVV 259
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-225 |
1.11e-80 |
|
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: 240.80 E-value: 1.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQ 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 ssehplgmtveevvsygrypyqkffsglneedlhaiqwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILD 167
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-258 |
2.60e-73 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 224.65 E-value: 2.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSehPLG--MTVEEVVSYGRYPYqkffSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEAD 162
Cdd:PRK13548 81 LPQHS--SLSfpFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 163 ------ILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWM 236
Cdd:PRK13548 155 pdgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETL 234
|
250 260
....*....|....*....|..
gi 1560390145 237 REIYEIEAQIIELPETNKPVVL 258
Cdd:PRK13548 235 RRVYGADVLVQPHPETGAPLVL 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
3.70e-73 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 223.81 E-value: 3.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSeistySPKMLAQ 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLAQSSEHPLG--MTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALA 158
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMkAGQIVVQGTPDEVITTSWMRE 238
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSR 233
|
250
....*....|
gi 1560390145 239 IYEIEAQIIE 248
Cdd:COG1121 234 AYGGPVALLA 243
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-258 |
3.72e-72 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 221.91 E-value: 3.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYGRYPYQkffsGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ------- 159
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 160 EADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREI 239
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250
....*....|....*....
gi 1560390145 240 YEIEAQIIELPETNKPVVL 258
Cdd:COG4559 237 YGADLRVLAHPEGGCPQVL 255
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-260 |
1.10e-66 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 208.10 E-value: 1.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGMTVEEVVSYG 104
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 105 RYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHL 184
Cdd:PRK10575 110 RYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 185 LKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIELPETNKPVVLSY 260
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPVSFVY 265
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-232 |
1.55e-64 |
|
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: 201.41 E-value: 1.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPL-GMTVEEVVSYGryPYQkffSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:COG1122 81 FQNPDDQLfAPTVEEDVAFG--PEN---LGLPREEIRErVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-214 |
2.82e-64 |
|
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: 200.07 E-value: 2.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistYSPKMLAQKIALLAQ 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 SSEHPLGM--TVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:cd03235 76 RRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEInHIKQTTILMSIHDINHASRFSDYLI 214
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-240 |
1.34e-56 |
|
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: 181.61 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQ---KIALLAQssEHPL- 93
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQIGMIFQ--QFNLi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 -GMTVEEVVSYGRYPYQKFFSGL-----NEEDLHAIQwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILD 167
Cdd:cd03256 91 eRLSVLENVLSGRLGRRSTWRSLfglfpKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEvITTSWMREIY 240
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-231 |
5.72e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.87 E-value: 5.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLaQKIALLA 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYgrypYQKFFsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:COG1131 80 QEPALYPDLTVRENLRF----FARLY-GLPRKEARErIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-245 |
8.28e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.87 E-value: 8.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQ--- 80
Cdd:COG3638 1 PMLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLAQssEHPL--GMTVEEVVSYGRYPY----QKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIA 154
Cdd:COG3638 81 RIGMIFQ--QFNLvpRLSVLTNVLAGRLGRtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 155 MALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEViTTS 234
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDA 237
|
250
....*....|.
gi 1560390145 235 WMREIYEIEAQ 245
Cdd:COG3638 238 VLREIYGGEAE 248
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-220 |
5.22e-54 |
|
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: 173.81 E-value: 5.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGY--LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPL-GMTVEEVVSYGRYPYqkffsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:cd03225 81 FQNPDDQFfGPTVEEEVAFGLENL-----GLPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQ 220
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-271 |
6.98e-50 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 168.87 E-value: 6.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINHIKQTTIlMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQ 245
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAV-AAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
250 260
....*....|....*....|....*.
gi 1560390145 246 IIELPETNKPVVLSYDLINDRKEDEQ 271
Cdd:PRK09536 242 VGTDPATGAPTVTPLPDPDRTEAAAD 267
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-230 |
2.87e-49 |
|
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: 162.35 E-value: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK-----EGKIIVDGSEIST--YSPKMLA 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 QKIALLAQSSeHPLGMTVEEVVSYGrypyQKFFSGLNEEDLHAI-QWALEATQLTKLKERELS--SLSGGQAQRVWIAMA 156
Cdd:cd03260 81 RRVGMVFQKP-NPFPGSIYDNVAYG----LRLHGIKLKEELDERvEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-252 |
2.98e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 163.78 E-value: 2.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 17 LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA---QKIALLAQSSEHPL 93
Cdd:TIGR04521 16 FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdlrKKVGLVFQFPEHQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 -GMTVEEVVSYGryPyQKFfsGLNEEDLHA-IQWALEATQLT-KLKERELSSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:TIGR04521 96 fEETVYKDIAFG--P-KNL--GLSEEEAEErVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 171 TFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVittswMREIYEIEAQIIELP 250
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV-----FSDVDELEKIGLDVP 245
|
..
gi 1560390145 251 ET 252
Cdd:TIGR04521 246 EI 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
8.96e-49 |
|
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: 168.54 E-value: 8.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK---EGKIIVDGSEISTYSPKM 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 LAQKIALLAQSSEHPL-GMTVEEVVSYGRypyqkFFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAM 155
Cdd:COG1123 81 RGRRIGMVFQDPMTQLnPVTVGDQIAEAL-----ENLGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 156 ALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
18-240 |
1.05e-48 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 161.31 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---MLAQKIALLAQssEHPL- 93
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrKLRRRIGMIFQ--HYNLi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 -GMTVEEVVSYGRYPYQKFFSGL-----NEEDLHAIQwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILD 167
Cdd:TIGR02315 92 eRLTVLENVLHGRLGYKPTWRSLlgrfsEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILAD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEvITTSWMREIY 240
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLRHIY 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-232 |
2.44e-48 |
|
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: 167.39 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNK-----QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP---KML 78
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 79 AQKIALLAQSSEHPL--GMTVEEVVSYGrypyQKFFSGLNEEDLHA-IQWALEATQL-TKLKERELSSLSGGQAQRVWIA 154
Cdd:COG1123 341 RRRVQMVFQDPYSSLnpRMTVGDIIAEP----LRLHGLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 155 MALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-225 |
3.88e-48 |
|
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: 159.21 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTtieaVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA-- 79
Cdd:cd03257 5 KNLS----VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 -QKIALLAQ---SSEHPLgMTVEEVVsygRYPYQKFFSGLNEEdlhaiqwALEATQLTKLKERELSS---------LSGG 146
Cdd:cd03257 81 rKEIQMVFQdpmSSLNPR-MTIGEQI---AEPLRIHGKLSKKE-------ARKEAVLLLLVGVGLPEevlnrypheLSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 147 QAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-252 |
7.13e-48 |
|
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: 159.90 E-value: 7.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN--KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseISTYSPKML---AQK 81
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQSSEHPL-GMTVEEVVSYG----RYPYqkffsglnEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMA 156
Cdd:TIGR04520 79 VGMVFQNPDNQFvGATVEDDVAFGlenlGVPR--------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVIT-TSW 235
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSqVEL 229
|
250 260
....*....|....*....|....*...
gi 1560390145 236 MREI-----------YEIEAQIIELPET 252
Cdd:TIGR04520 230 LKEIgldvpfitelaKALKKRGIPLPPD 257
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-249 |
4.02e-47 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 157.31 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSFTRLLPvKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGMTVEEVVSYGRYPyqkf 111
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQPA---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 112 fSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ-------EADILILDEPTTFLDPAHQLEILHL 184
Cdd:COG4138 97 -GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 185 LKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIEL 249
Cdd:COG4138 176 LRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEV 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-208 |
1.98e-45 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 151.23 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 15 GYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistyspkmlaqKIALLAQSSEHP-- 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVPds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 LGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:NF040873 70 LPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1560390145 173 LDPAHQLEILHLLKEInHIKQTTILMSIHDINHASR 208
Cdd:NF040873 150 LDAESRERIIALLAEE-HARGATVVVVTHDLELVRR 184
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-230 |
3.35e-45 |
|
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: 152.26 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDIT----TGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKI 82
Cdd:COG1124 2 LEVRNLSvsygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQ---SSEHPLgMTVEEVVSYgryPYQKFFSGLNEEDLHAiqwALEATQLTK-LKERELSSLSGGQAQRVWIAMALA 158
Cdd:COG1124 82 QMVFQdpyASLHPR-HTVDRILAE---PLRIHGLPDREERIAE---LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-233 |
2.62e-44 |
|
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: 149.74 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---MLAQKIA 83
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQ-----SSehplgMTVEEVVSYG-RYpyqkfFSGLNEEDLHAI-QWALEATQLTKLKERELSSLSGGQAQRVWIAMA 156
Cdd:COG1127 86 MLFQggalfDS-----LTVFENVAFPlRE-----HTDLSEAEIRELvLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-230 |
6.05e-44 |
|
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: 148.35 E-value: 6.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK-IALL 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGMTVEEVVSYGRYPYQKffsglneedlHAIQWALEA--TQLTKLKERELS---SLSGGQAQRVWIAMALAQE 160
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR----------AKRKARLERvyELFPRLKERRKQlagTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-242 |
6.89e-44 |
|
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: 148.85 E-value: 6.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGsEISTYSPKMLAQKIALLA 86
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEvvsygrypYQKFFSGLN----EEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEAD 162
Cdd:COG4555 81 DERGLYDRLTVRE--------NIRYFAELYglfdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 163 ILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEI 242
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDA 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-221 |
1.38e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.88 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSeHPLGMTVEEVVsygRYPYQKFFSGLNEEDLHAiqwALEATQLTK-LKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:COG4619 81 QEP-ALWGGTVRDNL---PFPFQLRERKFDRERALE---LLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQI 221
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-229 |
4.06e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.44 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPkmlAQ-KIALLAQssEHPL--GMTVEEVVS 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AErPVSMLFQ--ENNLfpHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 103 YGRYPYQKffsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEIL 182
Cdd:COG3840 94 LGLRPGLK----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1560390145 183 HLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:COG3840 170 DLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-221 |
1.47e-42 |
|
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: 144.55 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDIT----TGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA--- 79
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 -QKIALLAQSseHPL--GMTVEEVVSYGrypyqKFFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAM 155
Cdd:cd03255 81 rRHIGFVFQS--FNLlpDLTALENVELP-----LLLAGVPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 156 ALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFsDYLIGMKAGQI 221
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-258 |
1.52e-41 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 143.81 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK--------EGKIIVDGSEISTYSPKMLAQKIALLAQSSEHP 92
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 LGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ---------EADI 163
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIE 243
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGFA 255
|
250
....*....|....*
gi 1560390145 244 AQIIELPETNKPVVL 258
Cdd:PRK13547 256 VRLVDAGDGVPPVIV 270
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-233 |
2.88e-41 |
|
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: 141.87 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---MLAQKIA 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQSSEHPLGMTVEEVVSYGRYPYqkffSGLNEEDLHAIqwALEATQLTKLKEREL---SSLSGGQAQRVWIAMALAQE 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREH----TRLSEEEIREI--VLEKLEAVGLRGAEDlypAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-229 |
2.35e-40 |
|
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: 146.44 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSeHPLGMTVEEVVSYGRypyqkffsglNEEDLHAIQWALEATQL------------TKLKERElSSLSGGQAQRVW 152
Cdd:COG4988 416 VPQNP-YLFAGTIRENLRLGR----------PDASDEELEAALEAAGLdefvaalpdgldTPLGEGG-RGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDInHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-232 |
4.50e-40 |
|
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: 138.72 E-value: 4.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA--------QKIALLAqssehplGMTV 97
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgigrtfQIPRLFP-------ELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVV------SYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:cd03219 93 LENVmvaaqaRTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 172 FLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:cd03219 173 GLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-234 |
6.65e-40 |
|
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: 145.29 E-value: 6.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLN--KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIA 83
Cdd:COG4987 333 SLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQSSeHPLGMTVEEVVSYGRypyqkffSGLNEEDLHAiqwALEATQLTKLKEREL-----------SSLSGGQAQRVW 152
Cdd:COG4987 413 VVPQRP-HLFDTTLRENLRLAR-------PDATDEELWA---ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDINHASRFsDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA 558
|
..
gi 1560390145 233 TS 234
Cdd:COG4987 559 QN 560
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-221 |
7.32e-40 |
|
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: 136.37 E-value: 7.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLaQKIALLA 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYgrypyqkffsglneedlhaiqwaleatqltklkerelsslSGGQAQRVWIAMALAQEADILIL 166
Cdd:cd03230 80 EEPSLYENLTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQI 221
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-220 |
9.90e-40 |
|
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: 135.45 E-value: 9.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQ 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 ssehplgmtveevvsygrypyqkffsglneedlhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADILILD 167
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEInHIKQTTILMSIHDINHASRFSDYLIGMKAGQ 220
Cdd:cd00267 106 EPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-233 |
5.66e-39 |
|
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: 136.28 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSsehpLG----MTVEE----VVSYGRYPYQKffsglneedlhAIQWALEATQLTKLKEREL-----SSLSGGQAQRVW 152
Cdd:cd03295 81 IQQ----IGlfphMTVEEnialVPKLLKWPKEK-----------IRERADELLALVGLDPAEFadrypHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 153 IAMALAQEADILILDEPTTFLDP----AHQLEILHLLKEINHikqtTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPD 228
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQELGK----TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPD 221
|
....*
gi 1560390145 229 EVITT 233
Cdd:cd03295 222 EILRS 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-220 |
5.34e-38 |
|
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: 131.54 E-value: 5.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA--QKIAL 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPLGMTVEEVVSYGrypyqkffsglneedlhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADIL 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQ 220
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-240 |
9.18e-38 |
|
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: 132.80 E-value: 9.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK-IALLAQss 89
Cdd:COG0410 8 NLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPE-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 90 ehplG------MTVEE---VVSYGRypyqkffsglneEDLHAIQWALEA--TQLTKLKERELS---SLSGGQAQRVWIAM 155
Cdd:COG0410 86 ----GrrifpsLTVEEnllLGAYAR------------RDRAEVRADLERvyELFPRLKERRRQragTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 156 ALAQEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSW 235
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
....*
gi 1560390145 236 MREIY 240
Cdd:COG0410 229 VREAY 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-225 |
1.01e-37 |
|
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: 131.93 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGkVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYsPKMLAQKIALLA 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYgrypyQKFFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:cd03264 79 QEFGVYPNFTVREFLDY-----IAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-206 |
1.77e-37 |
|
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: 130.62 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPKMLA---QKIALLAQSSEHPL-GM 95
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLerrQRVGLVFQDPDDQLfAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVSYGryPYQKffsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:TIGR01166 85 DVDQDVAFG--PLNL---GLSEAEVERrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|..
gi 1560390145 175 PAHQLEILHLLKEINHiKQTTILMSIHDINHA 206
Cdd:TIGR01166 160 PAGREQMLAILRRLRA-EGMTVVISTHDVDLA 190
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-232 |
1.88e-37 |
|
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: 134.41 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP---VKEGKIIVDGSEISTYSPKMLAQ----KIALLAQ---SS 89
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQdpmTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 90 EHPLgMTVEEVVsygRYPYQKFFsGLNEEDLH--AIQwALEATQLTKLKEReLSS----LSGGQAQRVWIAMALAQEADI 163
Cdd:COG0444 99 LNPV-MTVGDQI---AEPLRIHG-GLSKAEARerAIE-LLERVGLPDPERR-LDRypheLSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-231 |
2.56e-37 |
|
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: 139.20 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGY--LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSeHPLGMTVEEVVSYGRypyqkffSGLNEEDlhaIQWALEATQL------------TKLKERElSSLSGGQAQRVW 152
Cdd:COG2274 554 VLQDV-FLFSGTIRENITLGD-------PDATDEE---IIEAARLAGLhdfiealpmgydTVVGEGG-SNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSiHD---INHAsrfsDYLIGMKAGQIVVQGTPDE 229
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIA-HRlstIRLA----DRIIVLDKGRIVEDGTHEE 695
|
..
gi 1560390145 230 VI 231
Cdd:COG2274 696 LL 697
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
2.58e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.32 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLttIEAVDIT----TGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK 76
Cdd:COG1136 1 MSPL--LELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 MLA----QKIALLAQSseHPL--GMTVEEVVSYGRYpyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQ 149
Cdd:COG1136 79 ELArlrrRHIGFVFQF--FNLlpELTALENVALPLL-----LAGVSRKERRErARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 150 RVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFsDYLIGMKAGQIV 222
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRIV 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-230 |
3.59e-37 |
|
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: 131.70 E-value: 3.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA--------QKIALLAqsseh 91
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgiartfQNPRLFP----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 plGMTVEEVVSYGRYPYQK--FFSGL--------NEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:COG0411 93 --ELTVLENVLVAAHARLGrgLLAALlrlprarrEEREARErAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMsI-HDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILL-IeHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-222 |
1.12e-36 |
|
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: 129.18 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLAQK 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrnigMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAqsseHplgMTVEEVVSYGRYPyqkffSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:cd03259 81 YALFP----H---LTVAENIAFGLKL-----RGVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-230 |
1.81e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLksftRLL----PVKEGKIIVDGSEISTYSP-----KM 77
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL----RMIagfeTPDSGRILLDGRDVTGLPPekrnvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 LAQKIALLAqsseHplgMTVEEVVSYG-RypyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAM 155
Cdd:COG3842 82 VFQDYALFP----H---LTVAENVAFGlR------MRGVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 156 ALAQEADILILDEPTTFLDPAH----QLEILHLLKEINhikqTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELG----ITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-233 |
2.02e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.77 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTR---LLP-VK-EGKIIVDGSEIstYSPKM---- 77
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPgARvEGEILLDGEDI--YDPDVdvve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 LAQKIALLAQSSeHPLGMTVEEVVSYG-RYpyqkffSGL-NEEDLHAI-QWALEATQL-----TKLKERELsSLSGGQAQ 149
Cdd:COG1117 90 LRRRVGMVFQKP-NPFPKSIYDNVAYGlRL------HGIkSKSELDEIvEESLRKAALwdevkDRLKKSAL-GLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 150 RVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
....
gi 1560390145 230 VITT 233
Cdd:COG1117 240 IFTN 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
3.25e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.81 E-value: 3.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPKMLA---QKI 82
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQSSEHPL-GMTVEEVVSYGryPYQKffsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:PRK13639 81 GIVFQNPDDQLfAPTVEEDVAFG--PLNL---GLSKEEVEKrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-227 |
3.29e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 129.86 E-value: 3.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPL-GMTVEEVVSYGryPYQKFFSGlnEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:PRK13647 85 FQDPDDQVfSSTVWDDVAFG--PVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTP 227
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-254 |
3.35e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.14 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP----KMLAQKIALLAQSSEHPL-GMTVEEV 100
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQFPEHQLfEETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGryPyQKFfsGLNEEDlhAIQWALEATQLTKLKERELS----SLSGGQAQRVWIAMALAQEADILILDEPTTFLDPA 176
Cdd:PRK13634 107 ICFG--P-MNF--GVSEED--AKQKAREMIELVGLPEELLArspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 177 HQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVittswMREIYEIEAQIIELPETNK 254
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI-----FADPDELEAIGLDLPETVK 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-230 |
4.29e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPkmlAQ--KIA 83
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP---PRerRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQsseHPL---GMTVEEVVSYG---RYPyqkffsglNEEDLHAI--QWaLEATQLTKLKERELSSLSGGQAQRVWIAM 155
Cdd:COG1118 79 FVFQ---HYAlfpHMTVAENIAFGlrvRPP--------SKAEIRARveEL-LELVQLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 156 ALAQEADILILDEPttF--LDpAH---QLEIL--HLLKEINHikqTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPD 228
Cdd:COG1118 147 ALAVEPEVLLLDEP--FgaLD-AKvrkELRRWlrRLHDELGG---TTVFVT-HDQEEALELADRVVVMNQGRIEQVGTPD 219
|
..
gi 1560390145 229 EV 230
Cdd:COG1118 220 EV 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-249 |
8.41e-36 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 128.13 E-value: 8.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSFTRLLPvKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGMTVeevvsygrYPYQKF 111
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV--------FQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 112 F--SGLNEEDL-HAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ-------EADILILDEPTTFLDPAHQLEI 181
Cdd:PRK03695 93 HqpDKTRTEAVaSALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 182 LHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIEL 249
Cdd:PRK03695 173 DRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDV 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-232 |
1.17e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.42 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIsTYSPKMLA---QKIA 83
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQSSE---HplgMTVEEVVSYGrypyQKFFSGLNEEDLHAIqwALEatQLTK--LKEREL---SSLSGGQAQRVWIAM 155
Cdd:COG1126 81 MVFQQFNlfpH---LTVLENVTLA----PIKVKKMSKAEAEER--AME--LLERvgLADKADaypAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 156 ALAQEADILILDEPTTFLDPahQL--EILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDP--ELvgEVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
1.29e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN--KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHP-LGMTVEEVVSYG----RYPYQKFFSGLNEedlhaiqwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ 159
Cdd:PRK13632 88 IFQNPDNQfIGATVEDDIAFGlenkKVPPKKMKDIIDD--------LAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 160 EADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-230 |
1.42e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.21 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQ 80
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLAQSSEHP-LGMTVEEVVSYG-------RypyqkffsglnEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVW 152
Cdd:PRK13635 82 QVGMVFQNPDNQfVGATVQDDVAFGlenigvpR-----------EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-245 |
1.73e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 133.37 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQssEHPL-GMT 96
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ--DTFLfSGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 97 VEEVVSYGRypyqkffsglNEEDLHAIQWALEATQL------------TKLKERElSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:COG1132 430 IRENIRYGR----------PDATDEEVEEAAKAAQAhefiealpdgydTVVGERG-VNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEInhIKQTTILMsihdINHasRFS-----DYLIGMKAGQIVVQGTPDEVITTS-WMRE 238
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERL--MKGRTTIV----IAH--RLStirnaDRILVLDDGRIVEQGTHEELLARGgLYAR 570
|
....*..
gi 1560390145 239 IYEIEAQ 245
Cdd:COG1132 571 LYRLQFG 577
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-171 |
2.36e-35 |
|
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: 123.91 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGMTVEEVVSYG 104
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 105 RYPYQKFFSGLNEEdlhaIQWALEATQLTKLKEREL----SSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:pfam00005 84 LLLKGLSKREKDAR----AEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-230 |
7.71e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.70 E-value: 7.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKM--LAQKIALLAQSSEHPL-GM 95
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPEYQLfEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVSYGryPYQKffsGLNEEDLHA-IQWALEATQLT--KLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:PRK13637 100 TIEKDIAFG--PINL---GLSEEEIENrVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-220 |
1.45e-34 |
|
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: 122.49 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSeHPLGMTV 97
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDP-FLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVsygrypyqkffsglneedlhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAH 177
Cdd:cd03228 93 RENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1560390145 178 QLEILHLLKEInhIKQTTILMSIHDINHASRFsDYLIGMKAGQ 220
Cdd:cd03228 132 EALILEALRAL--AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-221 |
1.92e-34 |
|
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: 123.41 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKM--LAQKIAL 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSS---EHplgMTVEEVVSYGrypyQKFFSGLNEEDlhAIQWALEATQLTKLKERELS---SLSGGQAQRVWIAMALA 158
Cdd:cd03262 81 VFQQFnlfPH---LTVLENITLA----PIKVKGMSKAE--AEERALELLEKVGLADKADAypaQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQI 221
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVT-HEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-229 |
2.25e-34 |
|
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: 123.38 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTySPKMLAQKIALLAQSSEHPLGMTVE 98
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 EVVsygrypyqKFFS---GLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:cd03263 94 EHL--------RFYArlkGLPKSEIKEeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 175 PAHQLEILHLLKEInhIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:cd03263 166 PASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-232 |
4.22e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.87 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLL-----PVKEGKIIVDGSEISTYSPKMLAQK 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQSSEHPLGMTVEEVVSYGryPYQKFFSGLNEEDLHAIQWALEATQL-TKLKER---ELSSLSGGQAQRVWIAMAL 157
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 158 AQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-222 |
5.44e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.98 E-value: 5.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGY-LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStysPKMLAQKIALLA 86
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGM-TVEEVVSYGrypyqkffSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:cd03226 78 QDVDYQLFTdSVREELLLG--------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINHIKqTTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQG-KAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-230 |
1.07e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.42 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPK---MLAQKIALLAQSSEHPL-GMTVEEV 100
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDPDNQLfSASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQkffsgLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQL 179
Cdd:PRK13636 104 VSFGAVNLK-----LPEDEVRKrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 180 EILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-232 |
1.52e-33 |
|
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: 127.49 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTtieaVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKS-TLLkSFTRLLP----VKEGKIIVDGSEISTYSPK 76
Cdd:COG4172 10 EDLS----VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPdpaaHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 MLAQ----KIALLAQ---SSEHPLgMTVE----EVVSYGRypyqkffsGLNEEDlhAIQWALEATQLTKLK--ERELSS- 142
Cdd:COG4172 85 ELRRirgnRIAMIFQepmTSLNPL-HTIGkqiaEVLRLHR--------GLSGAA--ARARALELLERVGIPdpERRLDAy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 143 ---LSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAG 219
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250
....*....|...
gi 1560390145 220 QIVVQGTPDEVIT 232
Cdd:COG4172 234 EIVEQGPTAELFA 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-229 |
3.84e-33 |
|
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: 120.55 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTySPKMLAQKIALLA 86
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMT-VEEVVSYGR-YPYQkffsglNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:cd03265 80 QDLSVDDELTgWENLYIHARlYGVP------GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-234 |
4.19e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseISTYSPK---------- 76
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 -MLAQKIALLAQssehplgMTVEEVVSYGryPYQkfFSGLNEEDLHAIQWALeatqLTK--LKERE---LSSLSGGQAQR 150
Cdd:PRK09493 80 gMVFQQFYLFPH-------LTALENVMFG--PLR--VRGASKEEAEKQAREL----LAKvgLAERAhhyPSELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 151 VWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT-HEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
....
gi 1560390145 231 ITTS 234
Cdd:PRK09493 224 IKNP 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
4.80e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.14 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIsTYSPKmlaQKIALL 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDR---RRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 aqssehP------LGMTVEEVVSY-GRypyqkfFSGLNEEDLH--AIQWaLEATQLTKLKERELSSLSGGQAQRVWIAMA 156
Cdd:COG4152 77 ------PeerglyPKMKVGEQLVYlAR------LKGLSKAEAKrrADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-230 |
5.94e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.40 E-value: 5.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHP-LGMTVEEVVSY 103
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQfVGSIVKYDVAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 104 G----RYPYQKFFSGLNEedlhaiqwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQL 179
Cdd:PRK13648 108 GlenhAVPYDEMHRRVSE--------ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 180 EILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-222 |
1.64e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.62 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQ-VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA---QKI 82
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQssEHPL--GMTVEEVVSYgryPYQkfFSGLNEEDLHA-IQWALEATQLTKlKEREL-SSLSGGQAQRVWIAMALA 158
Cdd:COG2884 82 GVVFQ--DFRLlpDRTVYENVAL---PLR--VTGKSRKEIRRrVREVLDLVGLSD-KAKALpHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-225 |
1.84e-32 |
|
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: 118.15 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIsTYSPKmlaQKIALLA 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAAR---NRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSY-GRypyqkfFSGLNEED-LHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:cd03269 77 EERGLYPKMKVIDQLVYlAQ------LKGLKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 165 ILDEPTTFLDPAHQleiLHLLKEINHIKQ--TTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03269 151 ILDEPFSGLDPVNV---ELLKDVIRELARagKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-225 |
2.04e-32 |
|
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: 118.36 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-----KMLAQKIALLAQssehplgMTVEEV 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPadrpvSMLFQENNLFAH-------LTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQKffsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLE 180
Cdd:cd03298 91 VGLGLSPGLK----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1560390145 181 ILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
4.86e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.07 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLttIEAVDITTGYLNKQ---VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKM 77
Cdd:PRK13650 1 MSNI--IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 LAQKIALLAQSSEHP-LGMTVEEVVSYGR----YPYQKFFSGLNEedlhaiqwALEATQLTKLKERELSSLSGGQAQRVW 152
Cdd:PRK13650 79 IRHKIGMVFQNPDNQfVGATVEDDVAFGLenkgIPHEEMKERVNE--------ALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASrFSDYLIGMKAGQIVVQGTPDE 229
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-233 |
6.38e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 118.51 E-value: 6.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----------MLAQKIALLAQssehplg 94
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkisMVFQSFALLPH------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MTVEEVVSYGRYpyqkfFSGLNEEDLH--AIQwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:cd03294 117 RTVLENVAFGLE-----VQGVPRAEREerAAE-ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 173 LDP----AHQLEILHLLKEInhikQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:cd03294 191 LDPlirrEMQDELLRLQAEL----QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-248 |
7.03e-32 |
|
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: 117.88 E-value: 7.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGK-IIVDGSEISTYSPKMLAQKIALL 85
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQS--SEHPLGMTVEEVV------SYGRYPYqkffsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMAL 157
Cdd:COG1119 84 SPAlqLRFPRDETVLDVVlsgffdSIGLYRE------PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 158 AQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHD-------INHAsrfsdylIGMKAGQIVVQGTPDEV 230
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHveeippgITHV-------LLLKDGRVVAAGPKEEV 230
|
250
....*....|....*...
gi 1560390145 231 ITTSWMREIYEIEAQIIE 248
Cdd:COG1119 231 LTSENLSEAFGLPVEVER 248
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-202 |
7.06e-32 |
|
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: 116.42 E-value: 7.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTySPKMLAQKIALLA 86
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEvvsygrypYQKFFSGLNEEDLHAIQW--ALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:COG4133 82 HADGLKPELTVRE--------NLRFWAALYGLRADREAIdeALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEinHIKQ-TTILMSIHD 202
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAA--HLARgGAVLLTTHQ 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-230 |
1.00e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 3 NLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLL---PVKEGKIIVDGSEISTYSPKMLA 79
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 QKIALLAQSSEHP-LGMTVEEVVSYG----RYPYQKFfsglneedLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIA 154
Cdd:PRK13640 84 EKVGIVFQNPDNQfVGATVGDDVAFGlenrAVPRPEM--------IKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 155 MALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-230 |
2.41e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.64 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLA 79
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrniaMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 QKIALLaqssEHplgMTVEEVVSYG-RypyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMAL 157
Cdd:COG3839 82 QSYALY----PH---MTVYENIAFPlK------LRKVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 158 AQEADILILDEPTTFLDPA--HQL--EILHLLKEINhikqTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKlrVEMraEIKRLHRRLG----TTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-234 |
7.92e-31 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 115.75 E-value: 7.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQV-IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStyspKMLAQK-IA 83
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQSSE--HPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEA 161
Cdd:PRK15056 82 YVPQSEEvdWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 162 DILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIgMKAGQIVVQGTPDEVITTS 234
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAE 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-233 |
9.36e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 114.54 E-value: 9.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK-IALLA 86
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSE-HPLgMTVEEVVSYGrypyqkfFSGLNEEDLHAIQWALEA-TQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:TIGR03410 82 QGREiFPR-LTVEENLLTG-------LAALPRRSRKIPDEIYELfPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-230 |
1.08e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.94 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK-----EGKIIVDGSEIstYSPKM---- 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI--YSPDVdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 LAQKIALLAQSSEHPLGMTVEEVVSYGrYPYQKFFSGLNEEDlHAIQWALEATQL-TKLKER---ELSSLSGGQAQRVWI 153
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELD-ERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 154 AMALAQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
3.25e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.13 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYL-NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPL-GMTVEEVVSYGryPYQKffsGLNEEDL-HAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:PRK13652 84 FQNPDDQIfSPTVEQDIAFG--PINL---GLDEETVaHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-234 |
1.20e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHP-LGMTVEEVVSY 103
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 104 GRYPyqkffSGL-NEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEIL 182
Cdd:PRK13642 106 GMEN-----QGIpREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 183 HLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVITTS 234
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-230 |
1.26e-29 |
|
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: 111.66 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLAQ 80
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQernvgFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLaqssEHplgMTVEEVVSYGrYPYQKFFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ 159
Cdd:cd03296 82 HYALF----RH---MTVFDNVAFG-LRVKPRSERPPEAEIRAkVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 160 EADILILDEPTTFLDPAHQLEILHLLKEINH-IKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVT-HDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-230 |
2.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.15 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP----KMLAQKIALLAQSSEHPL-GMTVEE 99
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPESQLfEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRypyQKFfsGLNEEDlhAIQWALEATQLT----KLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDP 175
Cdd:PRK13649 106 DVAFGP---QNF--GVSQEE--AEALAREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 176 AHQLEILHLLKEInHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13649 179 KGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-212 |
2.53e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.41 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTR---LLPV--KEGKIIVDGSEI--STYSPKM 77
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 LAQKIALLAQSSeHPLGMTVEEVVSYGRY--PYQKFFSGLNEEDLHaiQWALEATQLTKLKERELSsLSGGQAQRVWIAM 155
Cdd:PRK14243 89 VRRRIGMVFQKP-NPFPKSIYDNIAYGARinGYKGDMDELVERSLR--QAALWDEVKDKLKQSGLS-LSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 156 ALAQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDY 212
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVSDM 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-222 |
4.85e-29 |
|
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: 109.48 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQ----VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK--MLAQ 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDrgYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLaqssehPLgMTVEEVVSYGRypyqKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:cd03293 81 QDALL------PW-LTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 161 ADILILDEPTTFLDpAHQLEILH-LLKEINHIKQTTILMSIHDINHASRFSDYLIGMKA--GQIV 222
Cdd:cd03293 150 PDVLLLDEPFSALD-ALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-240 |
5.24e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.46 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 17 LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDG----SEISTYSPKMLAQKIALLAQSSEHP 92
Cdd:PRK13641 18 MEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 L-GMTVEEVVSYGryPYQKFFSGlNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:PRK13641 98 LfENTVLKDVEFG--PKNFGFSE-DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 172 FLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTS-WMREIY 240
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVT-HNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKeWLKKHY 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-230 |
5.57e-29 |
|
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: 109.63 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-----KMLAQK 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhkrpvNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQssehplgMTVEEVVSYGRYpyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:cd03300 81 YALFPH-------LTVFENIAFGLR-----LKKLPKAEIKErVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-185 |
7.88e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 114.38 E-value: 7.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQ-VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:TIGR02868 334 TLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSeHPLGMTVEEVVSYGRypyqkffSGLNEEDLhaiQWALEATQL------------TKLKERElSSLSGGQAQRVW 152
Cdd:TIGR02868 414 CAQDA-HLFDTTVRENLRLAR-------PDATDEEL---WAALERVGLadwlralpdgldTVLGEGG-ARLSGGERQRLA 481
|
170 180 190
....*....|....*....|....*....|...
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLL 185
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-231 |
1.04e-28 |
|
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: 109.24 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQ--VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSeHPLGMTVEEVVSYGRypyqkffSGLNEEDLHAIQWALEATQL---------TKLKERElSSLSGGQAQRVWIAM 155
Cdd:cd03251 81 VSQDV-FLFNDTVAENIAYGR-------PGATREEVEEAARAANAHEFimelpegydTVIGERG-VKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 156 ALAQEADILILDEPTTFLDP----AHQLEILHLLKEinhikQTTILMsihdinhASRFS-----DYLIGMKAGQIVVQGT 226
Cdd:cd03251 152 ALLKDPPILILDEATSALDTeserLVQAALERLMKN-----RTTFVI-------AHRLStienaDRIVVLEDGKIVERGT 219
|
....*
gi 1560390145 227 PDEVI 231
Cdd:cd03251 220 HEELL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-231 |
2.03e-28 |
|
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: 108.44 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNK----QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKML---A 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 QKIALLAQ-----SSEhplgmTVEEVVSYgryPYQKffsgLNEEDLHAIQWALEATQLTKLKERE---LSSLSGGQAQRV 151
Cdd:cd03258 82 RRIGMIFQhfnllSSR-----TVFENVAL---PLEI----AGVPKAEIEERVLELLELVGLEDKAdayPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 152 WIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-222 |
3.01e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.64 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK--MLAQKIALLaqssehPLgMT 96
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDrgVVFQEPALL------PW-LT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 97 VEEVVSYGrypyQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPttF--LD 174
Cdd:COG1116 97 VLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP--FgaLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 175 P---AH-QLEILHLLKEinhiKQTTILMSIHDINHASRFSDYLIGMKA--GQIV 222
Cdd:COG1116 171 AltrERlQDELLRLWQE----TGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-231 |
3.47e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSpKMLAQK 81
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQSSEHPLGMTVEE-VVSYGRYpyqkffSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQ 159
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVREnLLVFGRY------FGMSTREIEAvIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 160 EADILILDEPTTFLDPAHQLEILHLLKEInHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-231 |
3.60e-28 |
|
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: 107.70 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGY-LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSehPL-GMTVEEVVSYGRypyqkfFSGLNEE--------DLHAIQWALEATQLTKLKERELsSLSGGQAQRVWIAMA 156
Cdd:cd03253 81 PQDT--VLfNDTIGYNIRYGR------PDATDEEvieaakaaQIHDKIMRFPDGYDTIVGERGL-KLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMS--IHDINHAsrfsDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAhrLSTIVNA----DKIIVLKDGRIVERGTHEELL 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-249 |
3.84e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseISTYSPKML---AQKIALLAQSSEHPLG 94
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLwdiRNKAGMVFQNPDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MT-VEEVVSYGryPYQKffsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:PRK13633 100 ATiVEEDVAFG--PENL---GIPPEEIRErVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVIT-TSWMREIYEIEAQIIEL 249
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKeVEMMKKIGLDVPQVTEL 251
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-231 |
4.18e-28 |
|
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: 107.63 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSsehP--LGMTV 97
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE---PvlFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVSYGRypyqkfFSGLNEEDLHAIQWALEATQLTKLKER---EL----SSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:cd03249 94 AENIRYGK------PDATDEEVEEAAKKANIHDFIMSLPDGydtLVgergSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 171 TFLDPAHQLEILHLLKEInhIKQTTILMSIHDInHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03249 168 SALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
25-229 |
7.03e-28 |
|
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: 108.63 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIsTYSPKMLAQKIALLAQSSEHPLGMTVEE-VVSY 103
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-VREPRKVRRSIGIVPQYASVDEDLTGREnLEMM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 104 GRypyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEIL 182
Cdd:TIGR01188 91 GR------LYGLPKDEAEErAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1560390145 183 HLLKEINHIKqTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:TIGR01188 165 DYIRALKEEG-VTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-240 |
9.87e-28 |
|
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: 106.47 E-value: 9.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK-IALL 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGMTVEE---VVSYGRYPyqkffsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEAD 162
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIRGL-------SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 163 ILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSD--YLIGmkAGQIVVQGTPDEVITTSWMREIY 240
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDraYIIY--EGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-225 |
9.98e-28 |
|
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: 106.30 E-value: 9.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNK----QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTySPKMLAQKI 82
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQSSEHPLGMTVEEVVSY-GRypyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfAG------LYGLKGDELTArLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 161 ADILILDEPTTFLD---PAHQLEILHLLKEinhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03266 155 PPVLLLDEPTTGLDvmaTRALREFIRQLRA----LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-225 |
2.99e-27 |
|
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: 104.61 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKmlAQKIALLA 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYGRYPYqkffsGLNEEDlhaIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLL-----GIRKKR---IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 167 DEPTTFLDPAHQLEILHLLkeINHIKQ-TTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03268 151 DEPTNGLDPDGIKELRELI--LSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-230 |
3.27e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.00 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 3 NLTTIEAVDITTGylNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQ-- 80
Cdd:PRK11831 6 NLVDMRGVSFTRG--NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 -KIALLAQSSEHPLGMTVEEVVSYgryPYQKFfSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALA 158
Cdd:PRK11831 84 kRMSMLFQSGALFTDMNVFDNVAY---PLREH-TQLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-230 |
4.68e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLAQ 80
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARdrkvgFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLaqssEHplgMTVEEVVSYG--RYPYQKffsglnEEDLHAIQWA----LEATQLTKLKERELSSLSGGQAQRVWIA 154
Cdd:PRK10851 82 HYALF----RH---MTVFDNIAFGltVLPRRE------RPNAAAIKAKvtqlLEMVQLAHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 155 MALAQEADILILDEPTTFLDPAHQLEILHLLKEI-NHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-232 |
6.08e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-----KMLAQKIALLAqsseHplgMTVEEV 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPsrrpvSMLFQENNLFS----H---LTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQKffsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLE 180
Cdd:PRK10771 92 IGLGLNPGLK----LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 181 ILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-254 |
1.08e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKI-ALLAQSSEHP-LGMTVEE 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLvGIVFQNPETQfVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGryPYQKFFSGLneEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQL 179
Cdd:PRK13644 98 DLAFG--PENLCLPPI--EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 180 EILHLLKEInHIKQTTILMSIHDINHAsRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIELPETNK 254
Cdd:PRK13644 174 AVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIELAENLK 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-216 |
1.56e-26 |
|
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: 107.76 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQsseHPLGM--TVE 98
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQ---HPFLFagTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 EVVSYGRypyqkffsglNEEDLHAIQWALEATQL------------TKLKERElSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:TIGR02857 414 ENIRLAR----------PDASDAEIREALERAGLdefvaalpqgldTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 167 DEPTTFLDPAHQLEIlhlLKEINHIKQT-TILMSIHDINHASRfSDYLIGM 216
Cdd:TIGR02857 483 DEPTAHLDAETEAEV---LEALRALAQGrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-223 |
1.70e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.01 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSsehPL----- 93
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQD---PMmgtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 GMTVEE--VVSYGRYPYQKFFSGLNEEDLHAIQWALEATQL---TKLKEReLSSLSGGQAQRVWIAMALAQEADILILDE 168
Cdd:COG1101 96 SMTIEEnlALAYRRGKRRGLRRGLTKKRRELFRELLATLGLgleNRLDTK-VGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 169 PTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVV 223
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-211 |
3.59e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTR---LLP--VKEGKIIVDGSEIstYSPKM----LAQK 81
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPevTITGSIVYNGHNI--YSPRTdtvdLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQSSeHPLGMTVEEVVSYGRYpyqkfFSGLNEEDL--HAIQWALEATQL-TKLKERELSS---LSGGQAQRVWIAM 155
Cdd:PRK14239 88 IGMVFQQP-NPFPMSIYENVVYGLR-----LKGIKDKQVldEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 156 ALAQEADILILDEPTTFLDP--AHQLE-ILHLLKeinhiKQTTILMSIHDINHASRFSD 211
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPisAGKIEeTLLGLK-----DDYTMLLVTRSMQQASRISD 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-241 |
4.29e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 104.11 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 37 LIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLAQKIALLAQssehplgMTVEEVVSYGrypyQKF 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHlrhinMVFQSYALFPH-------MTVEENVAFG----LKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 112 FSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHI 191
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1560390145 192 KQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPdevittswmREIYE 241
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP---------EEIYE 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-225 |
6.90e-26 |
|
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: 100.08 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYL--NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSpKMLAQKIAL 84
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSsehplgmtveevvsygryPYqkFFSGlneedlhaiqwaleaTQLTKLKERelssLSGGQAQRVWIAMALAQEADIL 164
Cdd:cd03247 80 LNQR------------------PY--LFDT---------------TLRNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDINHASRFsDYLIGMKAGQIVVQG 225
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-225 |
8.74e-26 |
|
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: 101.19 E-value: 8.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP---VKEGKIIVDGSEIStysPKMLAQKIALLAQSSEHPLGM 95
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVSY-----GRYPYQKFFSGLNEEDLhaiqwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:cd03234 97 TVRETLTYtailrLPRKSSDAIRKKRVEDV-----LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 171 TFLDPAHQLEILHLLKEINHiKQTTILMSIH----DInhaSRFSDYLIGMKAGQIVVQG 225
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLAR-RNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-233 |
1.63e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.27 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVkEGKIIVDGsEISTYSPKMLAQK 81
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEG-RVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IAL----LAQSSEHP----LGMTVEEVVSYGrypyQKFFSGLNEEDLHAI-QWALEATQL-----TKLKERELSsLSGGQ 147
Cdd:PRK14258 81 VNLnrlrRQVSMVHPkpnlFPMSVYDNVAYG----VKIVGWRPKLEIDDIvESALKDADLwdeikHKIHKSALD-LSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 148 AQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKA-----GQIV 222
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLV 235
|
250
....*....|.
gi 1560390145 223 VQGTPDEVITT 233
Cdd:PRK14258 236 EFGLTKKIFNS 246
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-222 |
1.89e-25 |
|
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: 100.02 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLAQK 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdiaMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALlaqsseHPlGMTVEEVVSYGrypyQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEA 161
Cdd:cd03301 81 YAL------YP-HMTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 162 DILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-225 |
2.00e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.06 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 31 EGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDG-----SEISTYSPKMlAQKIALLAQSSEHPLGMTVEEVVSYGr 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdSRKKINLPPQ-QRKIGLVFQQYALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 106 ypyQKFFSglNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLL 185
Cdd:cd03297 100 ---LKRKR--NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1560390145 186 KEI-NHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03297 175 KQIkKNLNIPVIFVT-HDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-262 |
2.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.39 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP----KMLAQKIALLAQSSEHPLG 94
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 M-TVEEVVSYGRypyQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFL 173
Cdd:PRK13646 100 EdTVEREIIFGP---KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 174 DPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVittswMREIYEIEAQIIELPETn 253
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL-----FKDKKKLADWHIGLPEI- 250
|
....*....
gi 1560390145 254 kpVVLSYDL 262
Cdd:PRK13646 251 --VQLQYDF 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-222 |
2.25e-25 |
|
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: 98.27 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-MLAQKIAll 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 aqssehplgmTVeevvsygrypYQkffsglneedlhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADILI 165
Cdd:cd03216 79 ----------MV----------YQ---------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 166 LDEPTTFLDPAhqlEILHLLKEINHIKQ--TTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:cd03216 106 LDEPTAALTPA---EVERLFKVIRRLRAqgVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-232 |
2.49e-25 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 104.95 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQ--VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:TIGR03375 464 IEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPLGmTVEEVVSYGRyPYqkffsgLNEEDlhaIQWALEATQLTKLKERELS-----------SLSGGQAQRVWI 153
Cdd:TIGR03375 544 VPQDPRLFYG-TLRDNIALGA-PY------ADDEE---ILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVAL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 154 AMALAQEADILILDEPTTFLDPAHQLEILHLLKEInhIKQTTILMSIHdinhasRFS-----DYLIGMKAGQIVVQGTPD 228
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW--LAGKTLVLVTH------RTSlldlvDRIIVMDNGRIVADGPKD 684
|
....
gi 1560390145 229 EVIT 232
Cdd:TIGR03375 685 QVLE 688
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-231 |
2.50e-25 |
|
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: 100.10 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMlaQKIALLAQssEHPL--GMTVEEVVSY 103
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQ--NYALfpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 104 G----RYPYQKFfsglnEEDLHAIQwalEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQL 179
Cdd:cd03299 95 GlkkrKVDKKEI-----ERKVLEIA---EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 180 EILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-231 |
4.98e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 103.64 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQ 87
Cdd:TIGR02203 334 RNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 SSeHPLGMTVEEVVSYGRypyqkffsgLNEEDLHAIQWALEATQLTKLKER-----------ELSSLSGGQAQRVWIAMA 156
Cdd:TIGR02203 414 DV-VLFNDTIANNIAYGR---------TEQADRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEInhIKQTTILMSIH---DINHAsrfsDYLIGMKAGQIVVQGTPDEVI 231
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHrlsTIEKA----DRIVVMDDGRIVERGTHNELL 555
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-231 |
5.52e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 99.22 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSeHPLGMTV 97
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT-FLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVSYGRypyqkffSGLNEEDLHAIQWALEATQL---------TKLKERElSSLSGGQAQRVWIAMALAQEADILILDE 168
Cdd:cd03254 94 MENIRLGR-------PNATDEEVIEAAKEAGAHDFimklpngydTVLGENG-GNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 169 PTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINhASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-221 |
7.50e-25 |
|
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: 98.70 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLNK---QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQ 87
Cdd:cd03248 16 NVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 ssEHPL-GMTVEEVVSYG--RYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERElSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:cd03248 96 --EPVLfARSLQDNIAYGlqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRfSDYLIGMKAGQI 221
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-230 |
9.10e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP----KMLAQKIALLAQSSEHPL-GMTVEE 99
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQFPESQLfEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRypyQKFfsGLNEEDLHAIQW-ALEATQLTK-LKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAH 177
Cdd:PRK13643 105 DVAFGP---QNF--GIPKEKAEKIAAeKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 178 QLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVT-HLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-225 |
1.14e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 98.01 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 16 YLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-----KMLAQKIALLAQsse 90
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPyqrpvSMLFQENNLFAH--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 hplgMTVEEVVSYGRYPYQKffsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:TIGR01277 85 ----LTVRQNIGLGLHPGLK----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 171 TFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:TIGR01277 157 SALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-232 |
1.14e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA---QKI-------ALLAQSsehplgm 95
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIgmifqhfNLLSSR------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVSYgryPYQkfFSGLNEEDLHAIqwALEATQLTKLKERE---LSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:COG1135 98 TVAENVAL---PLE--IAGVPKAEIRKR--VAELLELVGLSDKAdayPSQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG1135 171 LDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-202 |
1.17e-24 |
|
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: 97.86 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQV-IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---MLAQKI 82
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQSSEHPLGMTVEEVVSYGRYPYQKFFSGLNEEdlhaIQWALEATQLtKLKERELSS-LSGGQAQRVWIAMALAQEA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKR----VPAALELVGL-SHKHRALPAeLSGGEQQRVAIARAIVNSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1560390145 162 DILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHD 202
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHA 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-232 |
1.75e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQsseHPLGM-- 95
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ---EPVLFsg 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVSYG--RYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERElSSLSGGQAQRVWIAMALAQEADILILDEPTTFL 173
Cdd:TIGR00958 570 SVRENIAYGltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 174 DpahqLEILHLLKEINHIKQTTILMSIHDInHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:TIGR00958 649 D----AECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-251 |
2.06e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA---QKIALLAQ-----SSEhplgmTV 97
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGMIFQhfnllSSR-----TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVSYgryPYQkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPA 176
Cdd:PRK11153 100 FDNVAL---PLE--LAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 177 HQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT---TSWMRE-IYEIEAQiiELPE 251
Cdd:PRK11153 175 TTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFShpkHPLTREfIQSTLHL--DLPE 251
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-202 |
2.68e-24 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 96.92 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 10 VDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK----MLAQKIALL 85
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSsehpLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:TIGR03608 82 FQN----FALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHD 202
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVTHD 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-230 |
3.36e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.16 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 16 YLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA--QKIALLAQSSEHPL 93
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 GMTveEVVSYGRYPYQKFfsGLNEEDL-HAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:PRK13638 91 FYT--DIDSDIAFSLRNL--GVPEAEItRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 173 LDPAHQLEILHLLKEI----NHikqttILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIvaqgNH-----VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-232 |
4.88e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.05 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQ--VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSsehplgmtveevvsygryPYqkFFSG------------LNEEDLHAIqwaLEATQLTKLKERE--LSS-------- 142
Cdd:PRK11160 419 VSQR------------------VH--LFSAtlrdnlllaapnASDEALIEV---LQQVGLEKLLEDDkgLNAwlgeggrq 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 143 LSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDINHASRFsDYLIGMKAGQIV 222
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
250
....*....|
gi 1560390145 223 VQGTPDEVIT 232
Cdd:PRK11160 553 EQGTHQELLA 562
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-243 |
7.50e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKM-----LAQKIALLAQSSEHPLG 94
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 M-TVEEVVSYGryPYQkffsgLNEEDLHAIQWALEATQLTKLKE----RELSSLSGGQAQRVWIAMALAQEADILILDEP 169
Cdd:PRK13645 105 QeTIEKDIAFG--PVN-----LGENKQEAYKKVPELLKLVQLPEdyvkRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 170 TTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIE 243
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-231 |
8.62e-24 |
|
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: 96.40 E-value: 8.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:cd03252 2 TFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHpLGMTVEEVVSYGR--YPYQKFFSGLNEEDLHAIQWALEATQLTKLKERElSSLSGGQAQRVWIAMALAQEADI 163
Cdd:cd03252 82 LQENVL-FNRSIRDNIALADpgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEInhIKQTTILMSIHDINhASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
26-220 |
1.72e-23 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 94.62 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA---QKIALLAQSSEHPLGMTVEEVVS 102
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrRRIGVVFQDFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 103 YgryPYQkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEI 181
Cdd:TIGR02673 102 L---PLE--VRGKKEREIQRrVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1560390145 182 LHLLKEInHIKQTTILMSIHDINHASRFSDYLIGMKAGQ 220
Cdd:TIGR02673 177 LDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-241 |
2.07e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---- 76
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 -MLAQKIALLAqsseHplgMTVEEVVSYG----RYPYQKFFSGLNEedlhaiqwALEATQLTKLKERELSSLSGGQAQRV 151
Cdd:PRK09452 89 nTVFQSYALFP----H---MTVFENVAFGlrmqKTPAAEITPRVME--------ALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 152 WIAMALAQEADILILDEPTTFLD----PAHQLEILHLLKEINhikqTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTP 227
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKLG----ITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
250
....*....|....
gi 1560390145 228 devittswmREIYE 241
Cdd:PRK09452 230 ---------REIYE 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-229 |
2.16e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---- 76
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQqrdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 -MLAQKIALLAQssehplgMTVEEVVSYGrypyQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAM 155
Cdd:PRK11432 81 cMVFQSYALFPH-------MSLGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 156 ALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-231 |
3.41e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.92 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNK-----QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIV---------DGSEIST 72
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 73 YSPKMLAQK---------------IALLAQSSEHPL-GMTVEEVVSYGRYPYqkffsGLNEEDlhAIQWALEATQLTKLK 136
Cdd:PRK13651 83 VLEKLVIQKtrfkkikkikeirrrVGVVFQFAEYQLfEQTIEKDIIFGPVSM-----GVSKEE--AKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 137 ERELS----SLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEInHIKQTTILMSIHDINHASRFSDY 212
Cdd:PRK13651 156 ESYLQrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKR 234
|
250
....*....|....*....
gi 1560390145 213 LIGMKAGQIVVQGTPDEVI 231
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDIL 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-225 |
4.04e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.82 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 4 LTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPkmLAQKIA 83
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS--LSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQSSEHpLGMTVEevvSYGRYPYQKFFSGLNEEDL--------HAIQWALEATQLTKLKERELS---SLSGGQAQRVW 152
Cdd:PRK11264 79 LIRQLRQH-VGFVFQ---NFNLFPHRTVLENIIEGPVivkgepkeEATARARELLAKVGLAGKETSyprRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-230 |
4.78e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-------- 76
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 -----MLAQKIALLAQSSEHPLGMTVEEVVSYGryPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRV 151
Cdd:PRK10619 84 knqlrLLRTRLTMVFQHFNLWSHMTVLENVMEA--PIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 152 WIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT-HEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-226 |
5.24e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP----------------VKEGKIIVDGS 68
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiellgrtvQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 69 EiSTYSPKMLAQKIALLAQssehplgMTVEEVV---SYGRYPYQK----FFSGLNEEdlHAIQwALEATQLTKLKERELS 141
Cdd:PRK09984 83 K-SRANTGYIFQQFNLVNR-------LSVLENVligALGSTPFWRtcfsWFTREQKQ--RALQ-ALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 142 SLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQI 221
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
....*
gi 1560390145 222 VVQGT 226
Cdd:PRK09984 232 FYDGS 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-231 |
5.51e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQ----KIALLAQSSEHPLGMTV 97
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVSYGrypyQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAH 177
Cdd:PRK10070 124 LDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 178 QLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-225 |
5.77e-23 |
|
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: 93.94 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 16 YLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEH---- 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 PLGMTVEEVVSYGRYPYQKFFSGLNEedlhaiqwALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDE--------LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 172 FLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-174 |
5.83e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistyspkmlaqKIALLAQSSE 90
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEVVSYGRYPYQKFFSGLNE---------EDLHAIQ-----------WALEA---TQLTKLK------ERELS 141
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEEleaklaepdEDLERLAelqeefealggWEAEAraeEILSGLGfpeedlDRPVS 151
|
170 180 190
....*....|....*....|....*....|...
gi 1560390145 142 SLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-233 |
6.49e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVD------GSEISTYSPKMLAQKIALLAQSSEH 91
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 PLGMTVEEVVSygrYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSS----LSGGQAQRVWIAMALAQEADILILD 167
Cdd:PRK14246 102 FPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-231 |
7.61e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQV--IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSeHPLGMTVEEVVSYGRypyQKFFSglNEEDLHAIQWALEATQLTKLKE-------RELSSLSGGQAQRVWIAMAL 157
Cdd:PRK11176 422 VSQNV-HLFNDTIANNIAYAR---TEQYS--REQIEEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 158 AQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-230 |
7.74e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 31 EGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA--------QKIALLAQssehplgMTVEE--V 100
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArmgvvrtfQHVRLFRE-------MTVIEnlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQKFFSGL---------NEEDL-HAIQWaLEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:PRK11300 103 VAQHQQLKTGLFSGLlktpafrraESEALdRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 171 TFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-230 |
9.29e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.06 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-----KMLAQK 81
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyqrpiNMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQssehplgMTVEEVVSYG----RYPYQKFFSGLNEedlhaiqwALEATQLTKLKERELSSLSGGQAQRVWIAMAL 157
Cdd:PRK11607 100 YALFPH-------MTVEQNIAFGlkqdKLPKAEIASRVNE--------MLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 158 AQEADILILDEPTTFLDPA----HQLEILHLLKEINhikqTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-226 |
9.73e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 9.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPKMLAQKIALL 85
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD-FSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSsehpLGMTVEEvvsYGRYPYQKFFSGLNEEDL--------HAIQWA---LEATQLTKLKERELSSLSGGQAQRVWIA 154
Cdd:COG4161 81 RQK----VGMVFQQ---YNLWPHLTVMENLIEAPCkvlglskeQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 155 MALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGT 226
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVT-HEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-233 |
1.10e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.97 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTtieaVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP----VKEGKIIVDGSEISTYSP-- 75
Cdd:COG4170 7 RNLT----IEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 76 --KMLAQKIALLAQ---SSEHP---LGMTVEEVVSYGRYPyQKFFSGLNEEDLHAIQWaleatqLTK--LKERE--LSS- 142
Cdd:COG4170 83 rrKIIGREIAMIFQepsSCLDPsakIGDQLIEAIPSWTFK-GKWWQRFKWRKKRAIEL------LHRvgIKDHKdiMNSy 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 143 ---LSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAG 219
Cdd:COG4170 156 pheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG 235
|
250
....*....|....
gi 1560390145 220 QIVVQGTPDEVITT 233
Cdd:COG4170 236 QTVESGPTEQILKS 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-249 |
1.25e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMlAQKIALLA 86
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTV-EEVVSYGRYpyqkffSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:PRK13537 87 QFDNLDPDFTVrENLLVFGRY------FGLSAAAARAlVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEInHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTswmreiyEIEA 244
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES-------EIGC 232
|
....*
gi 1560390145 245 QIIEL 249
Cdd:PRK13537 233 DVIEI 237
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-229 |
1.48e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.45 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVD-ITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVkEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK11174 349 TIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPLGmTVEEVVSYGRypyqkffSGLNEEDLHAiqwALEATQL------------TKLKERElSSLSGGQAQRVW 152
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLLGN-------PDASDEQLQQ---ALENAWVseflpllpqgldTPIGDQA-AGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 153 IAMALAQEADILILDEPTTFLDpAH--QLeILHLLKEINHiKQTTiLMSIHDINHASRFSDYLIgMKAGQIVVQGTPDE 229
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLD-AHseQL-VMQALNAASR-RQTT-LMVTHQLEDLAQWDQIWV-MQDGQIVQQGDYAE 569
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-265 |
1.82e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKI----IVDGSEISTYSP------------KMLAQKIAL 84
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPL-GMTVEEVVSYGRYPYqkffsGLNEEDLHAiqwaLEATQLTKLK------ERELSSLSGGQAQRVWIAMAL 157
Cdd:PRK13631 121 VFQFPEYQLfKDTIEKDIMFGPVAL-----GVKKSEAKK----LAKFYLNKMGlddsylERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 158 AQEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTswmR 237
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD---Q 267
|
250 260
....*....|....*....|....*...
gi 1560390145 238 EIYEIEAqiIELPetnkPVVlsyDLIND 265
Cdd:PRK13631 268 HIINSTS--IQVP----RVI---QVIND 286
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-224 |
2.38e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.95 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP---KMLAQKIALLAQSSEHPLG- 94
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrRAFRRDVQLVFQDSPSAVNp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 -MTVEEVVsygRYPYQKFFSGLNEEDLHAIQWALEATQL-TKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:TIGR02769 104 rMTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQ 224
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-232 |
3.36e-22 |
|
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: 94.01 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistyspKML---AQKIALLAqsseH--PLG--------- 94
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--------EVLqdsARGIFLPP----HrrRIGyvfqearlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 --MTVEEVVSYGRypyqKF-FSGLNEEDLHAIqwaLEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:COG4148 90 phLSVRGNLLYGR----KRaPRAERRISFDEV---VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 172 FLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-230 |
4.58e-22 |
|
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: 95.14 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPvKEGKIIVDGSEISTYSPKmlaqkiALLAQSSE------HPLG----- 94
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRR------ALRPLRRRmqvvfqDPFGslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MTVEEVVSYGRYPYQKffsGLNEEDLHA-IQWALEATQLTK-LKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:COG4172 379 MTVGQIIAEGLRVHGP---GLSAAERRArVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-199 |
4.75e-22 |
|
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: 89.97 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA 86
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEhplgmtveevvsygrypyqkFFSGLNEEDLhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADILIL 166
Cdd:cd03246 83 QDDE--------------------LFSGSIAENI----------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190
....*....|....*....|....*....|...
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMS 199
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIA 153
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-227 |
5.50e-22 |
|
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: 95.47 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTySPKMLAQKIALLAQSSEHPLGMTVE 98
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 EVVSYgrypYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQ 178
Cdd:TIGR01257 1022 EHILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1560390145 179 LEILHLLkeINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTP 227
Cdd:TIGR01257 1098 RSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-233 |
5.69e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.08 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPV-----KEGKIIVDGSEISTYSPKM-LAQ 80
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLeFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLAQSSeHPLGMTVEEVVSYGRYPYQ----KFFSGLNEEDLHAIQ-WALEATQLTKLKERelssLSGGQAQRVWIAM 155
Cdd:PRK14271 102 RVGMLFQRP-NPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGlWDAVKDRLSDSPFR----LSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 156 ALAQEADILILDEPTTFLDPAHQLEILHLLKEInhIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-214 |
6.40e-22 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 91.32 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPkmlaQKIallaqSSEHPlgMTVEEvvsygrypy 108
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKP----QYI-----KADYE--GTVRD--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 109 qkFFSGLNEEDLHAIQWALEAT---QLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLL 185
Cdd:cd03237 81 --LLSSITKDFYTHPYFKTEIAkplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180
....*....|....*....|....*....
gi 1560390145 186 KEINHIKQTTILMSIHDINHASRFSDYLI 214
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-230 |
7.26e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.33 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGylNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPkmlaQ 80
Cdd:PRK09544 1 MTSLVSLENVSVSFG--QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVP----Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIALLAQssehpLGMTVEEvvsygrypYQKFFSGLNEEDlhaIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:PRK09544 75 KLYLDTT-----LPLTVNR--------FLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKaGQIVVQGTPDEV 230
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVV 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-228 |
7.74e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPKMLAQKIALL 85
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSsehpLGMTVEEvvsYGRYPYQKFF----------SGLNEEDlhAIQWA---LEATQLTKLKERELSSLSGGQAQRVW 152
Cdd:PRK11124 81 RRN----VGMVFQQ---YNLWPHLTVQqnlieapcrvLGLSKDQ--ALARAeklLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAHQLEILHLLKEinhIKQTTILMSI--HDINHASRFSDYLIGMKAGQIVVQGTPD 228
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE---LAETGITQVIvtHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-229 |
1.20e-21 |
|
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: 90.15 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistYSPKMLaqkialla 86
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP---WTRKDL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 qsseHPLGMTVEEVVSYGRYPYQ---KFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:TIGR03740 70 ----HKIGSLIESPPLYENLTARenlKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPE-QGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-225 |
1.22e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 89.96 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGmTVEEV 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRyPYQKffsglNEEDLHAIQWAlEATQLTKLK----ERELS----SLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:cd03245 98 ITLGA-PLAD-----DERILRAAELA-GVTDFVNKHpnglDLQIGergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 173 LDPAHQLEILHLLKEInhIKQTTILMSIHdinhasRFS-----DYLIGMKAGQIVVQG 225
Cdd:cd03245 171 MDMNSEERLKERLRQL--LGDKTLIIITH------RPSlldlvDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-227 |
1.27e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 89.86 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQssehplgmtvEEV 100
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ----------DPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VsygrypyqkfFSG--------LNEEDLHAIQWALEATQL------------TKLKERElSSLSGGQAQRVWIAMALAQE 160
Cdd:cd03244 89 L----------FSGtirsnldpFGEYSDEELWQALERVGLkefveslpggldTVVEEGG-ENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTP 227
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-259 |
1.60e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK--------ML 78
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagiaII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 79 AQKIALLAQssehplgMTVEEVVSYGRYPYQKFFsgLNEEDLHAiqwalEATQ-LTKLK-----ERELSSLSGGQAQRVW 152
Cdd:COG1129 85 HQELNLVPN-------LSVAENIFLGREPRRGGL--IDWRAMRR-----RARElLARLGldidpDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAhqlEILHLLKEINHIKQ--TTILMSIHDINHASRFSDYLIGMKAGQIVVQG----- 225
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTER---EVERLFRIIRRLKAqgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvael 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1560390145 226 TPDEVITtsWM--ReiyEIEAQIIELPETNKPVVLS 259
Cdd:COG1129 228 TEDELVR--LMvgR---ELEDLFPKRAAAPGEVVLE 258
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-240 |
2.64e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 4 LTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStyspkmlaqkIA 83
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS----------LL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 84 LLAQSSEHPLGMTVEEVVSYGRYP-YQKFFSGLN-EEDLHAIQWALEATQL------TKLKERELSSLSGGQAQRVWIAM 155
Cdd:PRK10895 71 PLHARARRGIGYLPQEASIFRRLSvYDNLMAVLQiRDDLSAEQREDRANELmeefhiEHLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 156 ALAQEADILILDEPTTFLDPahqLEILHLLKEINHIKQT--TILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDP---ISVIDIKRIIEHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
....*..
gi 1560390145 234 SWMREIY 240
Cdd:PRK10895 228 EHVKRVY 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-240 |
3.63e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.32 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK-IAL 84
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQssEHPL--GMTVEE----VVSYGRYPYQKffsglNEEDLHAIqwaLEATQLTKLKERELSSLSGGQAQRVWIAMALA 158
Cdd:COG1137 83 LPQ--EASIfrKLTVEDnilaVLELRKLSKKE-----REERLEEL---LEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLlkeINHIKQTTI--LMSIHD-------INHAsrfsdYLIgmKAGQIVVQGTPDE 229
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKI---IRHLKERGIgvLITDHNvretlgiCDRA-----YII--SEGKVLAEGTPEE 222
|
250
....*....|.
gi 1560390145 230 VITTSWMREIY 240
Cdd:COG1137 223 ILNNPLVRKVY 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-233 |
8.72e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 8.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK-----EGKIIVDGSEISTYSPKMLAQ----KIALLAQ-- 87
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 -SSEHPLgMTVE----EVVSYGRypyqkffsGLNEEDLHA-IQWALEATQLTKLKEReLS----SLSGGQAQRVWIAMAL 157
Cdd:PRK15134 102 mVSLNPL-HTLEkqlyEVLSLHR--------GMRREAARGeILNCLDRVGIRQAAKR-LTdyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 158 AQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-232 |
1.25e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 90.87 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:TIGR01842 318 SVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGMTVEEVVSYGRYP-YQKFFSGLNEEDLHAIQWALEATQLTKLKERElSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:TIGR01842 398 PQDVELFPGTVAENIARFGENAdPEKIIEAAKLAGVHELILRLPDGYDTVIGPGG-ATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINhASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGITVVVIT-HRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-231 |
1.33e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.95 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGY-LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALL 85
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGMTVEEVVSYGRypyqkffSGLNEEDLHA------IQWALEATQL---TKLKErELSSLSGGQAQRVWIAMA 156
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAK-------ENVSQDEIWAaceiaeIKDDIENMPLgyqTELSE-EGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHikqTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-225 |
3.87e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 85.30 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTTieAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFT--RLLPVKEGKIIVDGSEIStysPKMLA 79
Cdd:cd03213 7 RNLTV--TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 QKIALLAQSSEHPLGMTVEEVVSYgrypyqkffsglneedlHAiqwaleatqltklkerELSSLSGGQAQRVWIAMALAQ 159
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMF-----------------AA----------------KLRGLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 160 EADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINhASRFS--DYLIGMKAGQIVVQG 225
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPS-SEIFElfDKLLLLSQGRVIYFG 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-261 |
6.85e-20 |
|
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: 87.47 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 24 KMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKML----AQKIALLAQSSEHPLGMTVEE 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRypyqKFFSGlneeDLHAIQWA--LEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAH 177
Cdd:TIGR02142 95 NLRYGM----KRARP----SERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 178 QLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIelpetNKPVV 257
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSL-----IEGVV 241
|
....
gi 1560390145 258 LSYD 261
Cdd:TIGR02142 242 AEHD 245
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-229 |
8.79e-20 |
|
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: 88.34 E-value: 8.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSsehplgmTV------EE 99
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD-------TVlfndtiAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRyPyqkffsGLNEEDLHAiqwALEATQL------------TKLKERELsSLSGGQAQRVWIAMALAQEADILILD 167
Cdd:COG5265 451 NIAYGR-P------DASEEEVEA---AARAAQIhdfieslpdgydTRVGERGL-KLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEI--NHikqTTILmsihdINHasRFS-----DYLIGMKAGQIVVQGTPDE 229
Cdd:COG5265 520 EATSALDSRTERAIQAALREVarGR---TTLV-----IAH--RLStivdaDEILVLEAGRIVERGTHAE 578
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-222 |
9.74e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYS---PKMLAQKIALLAQSSehpLGM 95
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDS---ISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 -----TVEEVVsygRYPYQKFFSgLNEED-LHAIQWALEATQLT-KLKERELSSLSGGQAQRVWIAMALAQEADILILDE 168
Cdd:PRK10419 102 vnprkTVREII---REPLRHLLS-LDKAErLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 169 PTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-240 |
1.30e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 12 ITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTY-SPKMLAQKIALLAQSSE 90
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEVVSYGrypyqKFFSGlNEEDLHAIQWALEAtqLTKLKERELS---SLSGGQAQRVWIAMALAQEADILILD 167
Cdd:PRK11614 91 VFSRMTVEENLAMG-----GFFAE-RDQFQERIKWVYEL--FPRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIY 240
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-233 |
1.63e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPvKEGKIIVDGSEISTYSPK-MLA--QKIALLAQ---SSEH 91
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRqLLPvrHRIQVVFQdpnSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 PLgMTVEEVVSYGRYPYQKFFSGLNEEDlHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:PRK15134 377 PR-LNVLQIIEEGLRVHQPTLSAAQREQ-QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 172 FLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVITT 233
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-231 |
1.94e-19 |
|
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: 87.50 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEhpL--Gm 95
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVE--LfdG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVSygRYPyqkffsglnEEDLHAIqwaLEATQL---------------TKLKEReLSSLSGGQAQRVWIAMALAQE 160
Cdd:COG4618 421 TIAENIA--RFG---------DADPEKV---VAAAKLagvhemilrlpdgydTRIGEG-GARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 161 ADILILDEPTTFLDPA-HQleilHLLKEINHIKQ---TTILMSiHD---INHAsrfsDYLIGMKAGQIVVQGTPDEVI 231
Cdd:COG4618 486 PRLVVLDEPNSNLDDEgEA----ALAAAIRALKArgaTVVVIT-HRpslLAAV----DKLLVLRDGRVQAFGPRDEVL 554
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-227 |
2.38e-19 |
|
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: 87.15 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 28 KIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDgSEIStYSPKMLAQKIallaqssehplGMTVEEVVSygRYP 107
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS-YKPQYISPDY-----------DGTVEEFLR--SAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 108 YQKFFSGLNEEDLhaiqwaLEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKE 187
Cdd:COG1245 427 TDDFGSSYYKTEI------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1560390145 188 INHIKQTTILMSIHDInhasrfsdYLIGMKAGQIVV-QGTP 227
Cdd:COG1245 501 FAENRGKTAMVVDHDI--------YLIDYISDRLMVfEGEP 533
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-231 |
2.68e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNK-QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK13657 334 AVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSehplGM---TVEEVVSYGRypyqkffSGLNEEDLHAiqwALEATQLTKLKEREL-----------SSLSGGQAQR 150
Cdd:PRK13657 414 VFQDA----GLfnrSIEDNIRVGR-------PDATDEEMRA---AAERAQAHDFIERKPdgydtvvgergRQLSGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 151 VWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILmsihdinhASRFS-----DYLIGMKAGQIVVQG 225
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII--------AHRLStvrnaDRILVFDNGRVVESG 551
|
....*.
gi 1560390145 226 TPDEVI 231
Cdd:PRK13657 552 SFDELV 557
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-222 |
3.60e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.14 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK--MLAQKIALLaqssehPLgMT 96
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgVVFQKDALL------PW-LN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 97 VEEVVSYG-RypyqkfFSGLNEEDLHAIqwALEATQLTKLK---ERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:COG4525 93 VLDNVAFGlR------LRGVPKAERRAR--AEELLALVGLAdfaRRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKA--GQIV 222
Cdd:COG4525 165 LDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-230 |
4.56e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKM-LAQKIALLAQsseHPL---GMTVEEVV 101
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQ---HFMlvpNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 102 SYGRYPYQKFFSGLNEedlhAIQWALEATQLTKLK---ERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAhq 178
Cdd:COG3845 102 VLGLEPTKGGRLDRKA----ARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ-- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 179 lEILHLLKEINHIKQ--TTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:COG3845 176 -EADELFEILRRLAAegKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-230 |
6.71e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.31 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTY----------SP 75
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKpdrdgelvpaDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 76 KMLAQ---KIALLAQSS---EHplgMTVEEVVSYGryPYQKFfsGLNEEDlhAIQWA---LEATQLTKLKERELSSLSGG 146
Cdd:COG4598 88 RQLQRirtRLGMVFQSFnlwSH---MTVLENVIEA--PVHVL--GRPKAE--AIERAealLAKVGLADKRDAYPAHLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 147 QAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGT 226
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVT-HEMGFARDVSSHVVFLHQGRIEEQGP 237
|
....
gi 1560390145 227 PDEV 230
Cdd:COG4598 238 PAEV 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-201 |
1.35e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKmlaqkiallaqSSEHPLG--- 94
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA-----------EACHYLGhrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 -----MTVEEVVSygrypyqkFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEP 169
Cdd:PRK13539 83 amkpaLTVAENLE--------FWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 1560390145 170 TTFLDPAHQLEILHLLKEinHIKQ-TTILMSIH 201
Cdd:PRK13539 155 TAALDAAAVALFAELIRA--HLAQgGIVIAATH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-187 |
1.36e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVdGSEIstyspkmlaqKIALLA 86
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEH-PLGMTVEEVVSYGRypyqkffSGLNEEDLHAIqwaLEA------TQLTKLKerelsSLSGGQAQRVWIAMALAQ 159
Cdd:COG0488 385 QHQEElDPDKTVLDELRDGA-------PGGTEQEVRGY---LGRflfsgdDAFKPVG-----VLSGGEKARLALAKLLLS 449
|
170 180
....*....|....*....|....*...
gi 1560390145 160 EADILILDEPTTFLDpahqLEILHLLKE 187
Cdd:COG0488 450 PPNVLLLDEPTNHLD----IETLEALEE 473
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-220 |
1.38e-18 |
|
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: 81.36 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSeistyspkmlaqkIALLAQSSEHpLGMTVEEVVSYGr 105
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWI-QNGTIRENILFG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 106 YPYqkffsglNEEDLHAiqwALEATQLTK----LKERELS-------SLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:cd03250 90 KPF-------DEERYEK---VIKACALEPdleiLPDGDLTeigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 175 P---AHQLE--ILHLLKeinhiKQTTILMSIHDINHASRFsDYLIGMKAGQ 220
Cdd:cd03250 160 AhvgRHIFEncILGLLL-----NNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-225 |
1.63e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP----VKEGKIIVDGSEISTYSPKmlAQKIALLAQ---SSEHPL- 93
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALR--GRKIATIMQnprSAFNPLh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 GMT---VEEVVSYGRYPyqkffsglneeDLHAIQWALEATQLTKlKERELSS----LSGGQAQRVWIAMALAQEADILIL 166
Cdd:PRK10418 97 TMHthaRETCLALGKPA-----------DDATLTAALEAVGLEN-AARVLKLypfeMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-226 |
2.19e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSsehP--LGMTVEEVVSYGRypyqkffsGLNEEDLhaiqW-ALEATQLTKLKeRELS------------SLSGGQAQ 149
Cdd:PRK10790 420 VQQD---PvvLADTFLANVTLGR--------DISEEQV----WqALETVQLAELA-RSLPdglytplgeqgnNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 150 RVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHdinhasRFS-----DYLIGMKAGQIVVQ 224
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVVIAH------RLStiveaDTILVLHRGQAVEQ 555
|
..
gi 1560390145 225 GT 226
Cdd:PRK10790 556 GT 557
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-219 |
4.59e-18 |
|
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: 80.59 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-KMLA-QKIALLA-QSSEHPLGMTVE 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPdRMVVfQNYSLLPwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 EVVSYGRYPYQKffsglneedlHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQ 178
Cdd:TIGR01184 81 RVLPDLSKSERR----------AIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1560390145 179 LEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAG 219
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
26-230 |
6.14e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.70 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP---KMLAQKIALLAQ---SSEHPlGMTVEE 99
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQdpyASLNP-RMTVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVS-------------------------------YGRYPYQkffsglneedlhaiqwaleatqltklkerelssLSGGQA 148
Cdd:COG4608 117 IIAeplrihglaskaerrervaellelvglrpehADRYPHE---------------------------------FSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 149 QRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPD 228
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
..
gi 1560390145 229 EV 230
Cdd:COG4608 244 EL 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-227 |
1.24e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDgSEIStYSPkmlaQKIallaqSSEHPlgMTVEEVVSYgrypy 108
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS-YKP----QYI-----KPDYD--GTVEDLLRS----- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 109 qkffsglNEEDLHAIQWALEAT---QLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLL 185
Cdd:PRK13409 424 -------ITDDLGSSYYKSEIIkplQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1560390145 186 KEINHIKQTTILMSIHDInhasrfsdYLIGMKAGQIVV-QGTP 227
Cdd:PRK13409 497 RRIAEEREATALVVDHDI--------YMIDYISDRLMVfEGEP 531
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-225 |
1.78e-17 |
|
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: 78.73 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistyspkmlaqKIALL--AQSSEHPlGMT 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSLlgLGGGFNP-ELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 97 VEE-VVSYGRypyqkfFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:cd03220 101 GREnIYLNGR------LLGLSRKEIDEkIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 175 PAHQLEILHLLKEInhIKQ-TTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:cd03220 175 AAFQEKCQRRLREL--LKQgKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-257 |
1.93e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.68 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQS----SEhpl 93
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTpflfSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 gmTVEEVVSYGRyPyqkffSGLNEEDLHAIQWA--------LEATQLTKLKERELSsLSGGQAQRVWIAMALAQEADILI 165
Cdd:PRK10789 404 --TVANNIALGR-P-----DATQQEIEHVARLAsvhddilrLPQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKEINhiKQTTILMSIHDINHASRFSDYLIgMKAGQIVVQGTPDEVITTS-WMREIY---E 241
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWG--EGRTVIISAHRLSALTEASEILV-MQHGHIAQRGNHDQLAQQSgWYRDMYryqQ 551
|
250
....*....|....*.
gi 1560390145 242 IEAQIIELPETNKPVV 257
Cdd:PRK10789 552 LEAALDDAPEIREEAV 567
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-233 |
2.50e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 80.23 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTtieaVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRL----LPVKEGKIIVDGSEISTYSP- 75
Cdd:PRK15093 6 IRNLT----IEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 76 ---KMLAQKIALLAQSSEHPL------GMTVEEVV---SY-GRYpYQKFfsglneedlhaiQW----ALEATQLTKLKER 138
Cdd:PRK15093 82 errKLVGHNVSMIFQEPQSCLdpservGRQLMQNIpgwTYkGRW-WQRF------------GWrkrrAIELLHRVGIKDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 139 E--LSS----LSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDY 212
Cdd:PRK15093 149 KdaMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
250 260
....*....|....*....|.
gi 1560390145 213 LIGMKAGQIVVQGTPDEVITT 233
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVTT 249
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-201 |
2.92e-17 |
|
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: 77.78 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKmLAQKIALLAQSSEHPLGMTVEEV 100
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYgrypYQKFFSGlneEDLhAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLE 180
Cdd:TIGR01189 94 LHF----WAAIHGG---AQR-TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|..
gi 1560390145 181 ILHLLKEinHI-KQTTILMSIH 201
Cdd:TIGR01189 166 LAGLLRA--HLaRGGIVLLTTH 185
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-229 |
3.02e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.91 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGylNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK---EGKIIVDGSEISTYSPkmLAQKI 82
Cdd:COG4136 3 SLENLTITLG--GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQSS---EHplgMTVEEVVSYGRYPyqkffsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALA 158
Cdd:COG4136 79 GILFQDDllfPH---LSVGENLAFALPP------TIGRAQRRArVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEinHIKQTTI--LMSIHDINHASrfsdyligmKAGQIVVQGTPDE 229
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFE--QIRQRGIpaLLVTHDEEDAP---------AAGRVLDLGNWQH 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-213 |
4.12e-17 |
|
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: 78.56 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 31 EGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKI--------IVD---GSEISTYSPKMLAQKIallaqssehplgmtveE 99
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDV----------------K 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRYPYQ--KFFSGLNEE------DLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:cd03236 89 VIVKPQYVDLipKAVKGKVGEllkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1560390145 172 FLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYL 213
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLVVE-HDLAVLDYLSDYI 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-222 |
5.70e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 12 ITTGYLN-KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK---MLAQKIALLAQ 87
Cdd:PRK10908 7 VSKAYLGgRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 ssEHPLGMtveEVVSYGRYPYQKFFSGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:PRK10908 87 --DHHLLM---DRTVYDNVAIPLIIAGASGDDIRRrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKqTTILMSIHDINHASRFSDYLIGMKAGQIV 222
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVG-VTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-230 |
7.56e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKsftrLLP----VKEGKIIVDGSEIStySPK---MLAQKIALLAQSsehpLG---- 94
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLS----LIAgarkIQQGRVEVLGGDMA--DARhrrAVCPRIAYMPQG----LGknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 --MTVEEVVSygrypyqkFFS---GLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDE 168
Cdd:NF033858 91 ptLSVFENLD--------FFGrlfGQDAAERRRrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 169 PTTFLDPAH-----QLeilhllkeINHIKQT----TILMSIHDINHASRFsDYLIGMKAGQIVVQGTPDEV 230
Cdd:NF033858 163 PTTGVDPLSrrqfwEL--------IDRIRAErpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-230 |
7.80e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNK-QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLA 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdiaMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 QKIALLAqsseHplgMTVEEVVSYG---RypyqkffsGLNEEDLHA-IQWALEATQLTKLKERELSSLSGGQAQRVwiAM 155
Cdd:PRK11650 83 QNYALYP----H---MSVRENMAYGlkiR--------GMPKAEIEErVAEAARILELEPLLDRKPRELSGGQRQRV--AM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 156 --ALAQEADILILDEPTTFLDP----AHQLEILHLLKEINhikqTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:PRK11650 146 grAIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRLK----TTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
.
gi 1560390145 230 V 230
Cdd:PRK11650 222 V 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-226 |
2.19e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 15 GYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLA----QKIALLAQSSE 90
Cdd:PRK11629 18 GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEVVSY-----GRYPYQkffsglneedlhAIQWALE---ATQLTKLKERELSSLSGGQAQRVWIAMALAQEAD 162
Cdd:PRK11629 98 LLPDFTALENVAMplligKKKPAE------------INSRALEmlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 163 ILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLiGMKAGQIVVQGT 226
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAELS 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-231 |
2.62e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSeIStyspkmlaqkiALLA-QSSEHP----- 92
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VS-----------ALLElGAGFHPeltgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 ---------LGMTVEEVvsygrypYQKF-----FSGLnEEDLHaiqwaleatqlTKLKerelsSLSGGQAQRVWIAMALA 158
Cdd:COG1134 107 eniylngrlLGLSRKEI-------DEKFdeiveFAEL-GDFID-----------QPVK-----TYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEInhIKQ-TTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIREL--RESgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-214 |
2.63e-16 |
|
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: 73.64 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistyspkmlaqKIALLA 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QssehplgmtveevvsygrypyqkffsglneedlhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADILIL 166
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1560390145 167 DEPTTFLDPAHqleILHLLKEINHIKQTTILMSiHDINHASRFSDYLI 214
Cdd:cd03221 95 DEPTNHLDLES---IEALEEALKEYPGTVILVS-HDRYFLDQVATKII 138
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-232 |
5.76e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.46 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFT----RLLPVKEGKIIVDGseistYSP-KMLAQKIALLAQSSE--- 90
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG-----ITPeEIKKHYRGDVVYNAEtdv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEVVSYG---RYPyQKFFSGLNEE-------DLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:TIGR00956 149 HFPHLTVGETLDFAarcKTP-QNRPDGVSREeyakhiaDVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINH-ASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-176 |
9.11e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 73.68 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKmLAQKIALLA 86
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVsygrypyqKFFSGLNEEDlhAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:cd03231 80 HAPGIKTTLSVLENL--------RFWHADHSDE--QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170
....*....|
gi 1560390145 167 DEPTTFLDPA 176
Cdd:cd03231 150 DEPTTALDKA 159
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-229 |
9.26e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEK-MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-----MLAQKIALLAQssehplg 94
Cdd:PRK11000 17 VISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergvgMVFQSYALYPH------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MTVEEVVSYGrypyQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:PRK11000 90 LSVAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 175 PA----HQLEILHLLKEInhikQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:PRK11000 166 AAlrvqMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-227 |
9.82e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.60 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGMTVEE 99
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRYPYQKFFSGLneedlhaiqwaleatqltKLKERELsSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQL 179
Cdd:cd03369 102 LDPFDEYSDEEIYGAL------------------RVSEGGL-NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1560390145 180 EILHLLKEinHIKQTTILMSIHDINHASRFsDYLIGMKAGQIVVQGTP 227
Cdd:cd03369 163 LIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-206 |
1.41e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 2 KNLTTIEAVDITTGylNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK 81
Cdd:PRK10247 5 SPLLQLQNVGYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQSsehP--LGMTVEEVVSygrYPYQ---------KFFSGLneedlhaIQWALEATQLTKlkerELSSLSGGQAQR 150
Cdd:PRK10247 83 VSYCAQT---PtlFGDTVYDNLI---FPWQirnqqpdpaIFLDDL-------ERFALPDTILTK----NIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 151 VWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHD---INHA 206
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDkdeINHA 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-219 |
1.44e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 10 VDITTGYL----NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGS-EISTYSPKMLAQKIAL 84
Cdd:cd03290 1 VQVTNGYFswgsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHP--LGMTVEEVVSYGR-YPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSsLSGGQAQRVWIAMALAQEA 161
Cdd:cd03290 81 VAYAAQKPwlLNATVEENITFGSpFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 162 DILILDEPTTFLD---PAHQLE--ILHLLKEinhiKQTTILMSIHDINHASRfSDYLIGMKAG 219
Cdd:cd03290 160 NIVFLDDPFSALDihlSDHLMQegILKFLQD----DKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
26-222 |
1.46e-15 |
|
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: 73.62 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAqkiALLAQS------SEHPLG-MTVE 98
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA---RLRARHvgfvfqSFQLLPtLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 EVVsygrypyqkffsGLNEE---DLHAIQWALEATQLTKLKEREL---SSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:COG4181 109 ENV------------MLPLElagRRDARARARALLERVGLGHRLDhypAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIV 222
Cdd:COG4181 177 LDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-230 |
1.89e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP----VKEGKIIVDGSEISTYSPK----MLAQKIALLAQ---SSE 90
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKerrnLVGAEVAMIFQdpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HP---LGMTVEEVVsygrypyqKFFSGLNEEDLHaiQWALEATQLTKLKERELS------SLSGGQAQRVWIAMALAQEA 161
Cdd:PRK11022 103 NPcytVGFQIMEAI--------KVHQGGNKKTRR--QRAIDLLNQVGIPDPASRldvyphQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 162 DILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-239 |
2.12e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQ-KIALL 85
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGMTVEEVVSYGRYPYQKFFsGLNEEDLHAI-QWALEATQLTKLK---ERELSSLSGGQAQRVWIAMALAQEA 161
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVC-GVNIIDWREMrVRAAMMLLRVGLKvdlDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 162 DILILDEPTTFLDpahQLEILHLLKEINHIKQ--TTILMSIHDINHASRFSDYLIGMKAGQIVVQG-----TPDEVITTS 234
Cdd:PRK09700 165 KVIIMDEPTSSLT---NKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGmvsdvSNDDIVRLM 241
|
....*
gi 1560390145 235 WMREI 239
Cdd:PRK09700 242 VGREL 246
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-229 |
2.36e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP---VKEGKIIVDGSEIStySPKMlaQKIALLAQSSEHPLGM 95
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPID--AKEM--RAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 -TVEEVVSY------GRYPYQKffsglneEDLHAIQWALEATQLTKLK------ERELSSLSGGQAQRVWIAMALAQEAD 162
Cdd:TIGR00955 114 lTVREHLMFqahlrmPRRVTKK-------EKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 163 ILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHD-INHASRFSDYLIGMKAGQIVVQGTPDE 229
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-230 |
2.44e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.38 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 28 KIPEGKVTS---------------LIGPNGSGKSTLLKSFTRLLpVKEGKI----IVDGSEISTYSPKML----AQKIAL 84
Cdd:PRK09473 23 STPDGDVTAvndlnfslragetlgIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPEKELnklrAEQISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQ---SSEHP---LGMTVEEVVS-YGRYPYQKFFsglnEED---LHAIQWAlEATQLTKLKERELSslsGGQAQRVWIA 154
Cdd:PRK09473 102 IFQdpmTSLNPymrVGEQLMEVLMlHKGMSKAEAF----EESvrmLDAVKMP-EARKRMKMYPHEFS---GGMRQRVMIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 155 MALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-197 |
2.61e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGylNKQV-IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVdgseistysPKmlAQKIAL 84
Cdd:COG4178 364 ALEDLTLRTP--DGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PA--GARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPLGmTVEEVVSYgryPYQKffSGLNEEDLHAiqwALEATQLTKLKEReLSS-------LSGGQAQRVWIAMAL 157
Cdd:COG4178 431 LPQRPYLPLG-TLREALLY---PATA--EAFSDAELRE---ALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1560390145 158 AQEADILILDEPTTFLDPAHQLEILHLLKEinHIKQTTIL 197
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVI 538
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-254 |
6.15e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.07 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSF--TRLLPVKEGKII-------------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 65 -------------VDGSEISTYSPKMLAQKIALLAQSSehpLGMTVEEVVsygrypYQKFFSGLNE---EDLHAIQWALE 128
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRT---FALYGDDTV------LDNVLEALEEigyEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 129 ATQLTKLKEREL---SSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPaHQLEILH-LLKEINHIKQTTILMSIHDIN 204
Cdd:TIGR03269 152 LIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP-QTAKLVHnALEEAVKASGISMVLTSHWPE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 205 HASRFSDYLIGMKAGQIVVQGTPDEVITTsWMR--------EIYEIEAQIIELPETNK 254
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVAV-FMEgvsevekeCEVEVGEPIIKVRNVSK 287
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-230 |
8.50e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK---IALLAQSsehPLG-----MTV 97
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQD---PLAslnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVSYgryPYQKFFSGLNEEDLHAIQWA--LEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDP 175
Cdd:PRK15079 118 GEIIAE---PLRTYHPKLSRQEVKDRVKAmmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 176 AHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-206 |
1.78e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 16 YLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK--MLAQKIALLAQSSehpl 93
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgVVFQNEGLLPWRN---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 gmtVEEVVSYGRYpyqkfFSGL-NEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:PRK11248 87 ---VQDNVAFGLQ-----LAGVeKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|....
gi 1560390145 173 LDPAHQLEILHLLKEINHIKQTTILMSIHDINHA 206
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-174 |
2.50e-14 |
|
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: 72.28 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVdGSEIstyspkmlaqKIALLA 86
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEH--PlGMTVEEVVSYG-------------RYPYQKF-FSGlneedlhaiqwaleATQLTKLKErelssLSGGQAQR 150
Cdd:TIGR03719 392 QSRDAldP-NKTVWEEISGGldiiklgkreipsRAYVGRFnFKG--------------SDQQKKVGQ-----LSGGERNR 451
|
170 180
....*....|....*....|....
gi 1560390145 151 VWIAMALAQEADILILDEPTTFLD 174
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-174 |
6.39e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 31 EGKVTSLIGPNGSGKSTLLKSFT-RLLP-----VKEGKI--IVD---GSEISTYSPKM------LAQKIALLAQSSEHPL 93
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSgELIPnlgdyEEEPSWdeVLKrfrGTELQNYFKKLyngeikVVHKPQYVDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 GmTVEEVVSygRYPYQKFFSGLNEEdlhaiqwaLEatqLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFL 173
Cdd:PRK13409 178 G-KVRELLK--KVDERGKLDEVVER--------LG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
.
gi 1560390145 174 D 174
Cdd:PRK13409 244 D 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-174 |
6.69e-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: 70.97 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 31 EGKVTSLIGPNGSGKSTLLKSFTRLL---------PVKEGKII--VDGSEISTYSPKMLAQKIallaqssehplgmtveE 99
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSWDEVLkrFRGTELQDYFKKLANGEI----------------K 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRYPYQ--KFFSGlNEEDLhaiqwaLEATQ-------------LTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:COG1245 162 VAHKPQYVDLipKVFKG-TVREL------LEKVDergkldelaeklgLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170
....*....|
gi 1560390145 165 ILDEPTTFLD 174
Cdd:COG1245 235 FFDEPSSYLD 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-242 |
8.48e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 12 ITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-MLAQKIALLAQSSE 90
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEVVSYGRYPYQkfFSGLNEEDLhaIQWALEatQLTKLKER-----ELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:PRK11288 90 LVPEMTVAENLYLGQLPHK--GGIVNRRLL--NYEARE--QLEHLGVDidpdtPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 166 LDEPTTFLDpahQLEILHLLKEINHIKQ--TTILMSIHDINHASRFSDYLIGMKAGQIV-----VQGTP-DEVITTSWMR 237
Cdd:PRK11288 164 FDEPTSSLS---AREIEQLFRVIRELRAegRVILYVSHRMEEIFALCDAITVFKDGRYVatfddMAQVDrDQLVQAMVGR 240
|
....*
gi 1560390145 238 EIYEI 242
Cdd:PRK11288 241 EIGDI 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-239 |
9.69e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLT----TIEAVDittgylnkqvieKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK--EGKIIVDGSEISTYS 74
Cdd:PRK13549 8 MKNITktfgGVKALD------------NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 75 PKMLAQK-IALLAQSSEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWaLEATQLTKLKERELSSLSGGQAQRVWI 153
Cdd:PRK13549 76 IRDTERAgIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKL-LAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 154 AMALAQEADILILDEPTTFLDPAhqlEILHLLKEINHIKQ---TTILMSiHDINHASRFSDYLIGMKAGQIV-----VQG 225
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTES---ETAVLLDIIRDLKAhgiACIYIS-HKLNEVKAISDTICVIRDGRHIgtrpaAGM 230
|
250
....*....|....
gi 1560390145 226 TPDEVITTSWMREI 239
Cdd:PRK13549 231 TEDDIITMMVGREL 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-225 |
1.45e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 14 TGYLNK-----QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP---KMLAQKIALL 85
Cdd:PRK10261 327 SGLLNRvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSS------EHPLGMTVEEvvsygryPYQKFFSGLNEEDLHAIQWALEATQLtkLKE---RELSSLSGGQAQRVWIAMA 156
Cdd:PRK10261 407 FQDPyasldpRQTVGDSIME-------PLRVHGLLPGKAAAARVAWLLERVGL--LPEhawRYPHEFSGGQRQRICIARA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQG 225
Cdd:PRK10261 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-231 |
2.17e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKII-------VDGSEISTYSPKMLAQKIALLAQSsehplg 94
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 mtveevvsYGRYPYQKFFSGLNEE------DLHAIQWA---LEATQLTKLKEREL-----SSLSGGQAQRVWIAMALAQE 160
Cdd:TIGR03269 374 --------YDLYPHRTVLDNLTEAiglelpDELARMKAvitLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILH-LLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVS-HDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-225 |
2.38e-13 |
|
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: 66.90 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK---EGKIIVDGSEISTYSPKMLAQkIALLAQSSEHPLG 94
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGE-IIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MTVEEVVSygrypyqkfFSglneedlhaiqwaleatqlTKLKERE-LSSLSGGQAQRVWIAMALAQEADILILDEPTTFL 173
Cdd:cd03233 98 LTVRETLD---------FA-------------------LRCKGNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 174 DPAHQLEILHLLKEINHIKQTTILMSIH----DINHAsrFsDYLIGMKAGQIVVQG 225
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLYqasdEIYDL--F-DKVLVLYEGRQIYYG 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-193 |
2.42e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-MLAQKIALLAQSSEHPLGMTVEEV 100
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQKFFSGLNE--EDLHAIQWALEATQLTKLKereLSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDpahQ 178
Cdd:PRK10982 94 MWLGRYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAK---VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT---E 167
|
170
....*....|....*
gi 1560390145 179 LEILHLLKEINHIKQ 193
Cdd:PRK10982 168 KEVNHLFTIIRKLKE 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-230 |
3.45e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGS----------EISTYSPKML----AQKIALL 85
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMrhvrGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQ---SSEHPLgMTVEEVVSYGRYPYQkffsGLN-EEDLHAIQWALEATQLTKLKE---RELSSLSGGQAQRVWIAMALA 158
Cdd:PRK10261 110 FQepmTSLNPV-FTVGEQIAESIRLHQ----GASrEEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 159 QEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-221 |
5.28e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLksftRLLPvkegkiivdGSEISTySPKMLAQKiALLAQSSE 90
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLA---------GLETPS-AGELLAGT-APLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEVVsygrYPYQKFFS----GLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:PRK11247 82 DTRLMFQDARL----LPWKKVIDnvglGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQI 221
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-234 |
6.48e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.65 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSeistyspkmlaqkIALLAQSSeHPLGMTVE 98
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQA-WIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 EVVSygrypyqkFFSGLNEEDLH-AIQWA-LEA--TQLTKLKERELS----SLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:PTZ00243 739 GNIL--------FFDEEDAARLAdAVRVSqLEAdlAQLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 171 TFLDpAHQLEilHLLKE--INHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVITTS 234
Cdd:PTZ00243 811 SALD-AHVGE--RVVEEcfLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-231 |
8.99e-13 |
|
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: 68.12 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 138 RELSSLSGGQAQRVWIAMALAQEAD---ILILDEPTT---FLDPAHQLEILHLLKEINHikqtTILMSIHDInHASRFSD 211
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTglhFDDIKKLLEVLQRLVDKGN----TVVVIEHNL-DVIKTAD 899
|
90 100
....*....|....*....|....*.
gi 1560390145 212 YLI------GMKAGQIVVQGTPDEVI 231
Cdd:TIGR00630 900 YIIdlgpegGDGGGTVVASGTPEEVA 925
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-174 |
9.54e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVdGSEIstyspkmlaqKIALLA 86
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEH--PlGMTVEEVVSYG-------------RYPYQKF-FSGlneedlhaiqwaleATQLTKLKErelssLSGGQAQR 150
Cdd:PRK11819 394 QSRDAldP-NKTVWEEISGGldiikvgnreipsRAYVGRFnFKG--------------GDQQKKVGV-----LSGGERNR 453
|
170 180
....*....|....*....|....
gi 1560390145 151 VWIAMALAQEADILILDEPTTFLD 174
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-227 |
1.05e-12 |
|
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: 66.10 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLL-----KSFTRLLPVKEGK----------------IIVDGSEI--------STYS-- 74
Cdd:cd03271 15 DVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQpgnhdrieglehidkvIVIDQSPIgrtprsnpATYTgv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 75 ------------------PKMLAqkIALLAQSSEHPLGMTVEEVVsygrypyqKFFsgLNEEDLHAIQWALEATQLTKLK 136
Cdd:cd03271 95 fdeirelfcevckgkrynRETLE--VRYKGKSIADVLDMTVEEAL--------EFF--ENIPKIARKLQTLCDVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 137 -ERELSSLSGGQAQRVWIAMALAQEAD---ILILDEPTT---FLDPAHQLEILHLLKEINHikqtTILMSIHDInHASRF 209
Cdd:cd03271 163 lGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTglhFHDVKKLLEVLQRLVDKGN----TVVVIEHNL-DVIKC 237
|
250 260
....*....|....*....|....
gi 1560390145 210 SDYLI------GMKAGQIVVQGTP 227
Cdd:cd03271 238 ADWIIdlgpegGDGGGQVVASGTP 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-239 |
1.42e-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: 67.16 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 12 ITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP--VKEGKIIVDGSEISTYSPKMLAQK-IALLAQS 88
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 89 SEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKE-RELSSLSGGQAQRVWIAMALAQEADILILD 167
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQG-----TPDEVITTSWMREI 239
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQHVATKdmstmSEDDIITMMVGREI 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-187 |
1.43e-12 |
|
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: 64.38 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-KMLAQKIALLAQS-SEHPL--GMTVEEVV 101
Cdd:cd03215 20 SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDrKREGLvlDLSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 102 SYGRYpyqkffsglneedlhaiqwaleatqltklkerelssLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEI 181
Cdd:cd03215 100 ALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
....*.
gi 1560390145 182 LHLLKE 187
Cdd:cd03215 144 YRLIRE 149
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-241 |
1.53e-12 |
|
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: 64.86 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLK------SFTrllpVKEGKIIVDGSEISTYSPKMLAQK-IALLAQSSE 90
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtimghpKYE----VTEGEILFKGEDITDLPPEERARLgIFLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGMTVEEvvsygrypyqkFFSGLNEedlhaiqwaleatqltklkerelsSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:cd03217 88 EIPGVKNAD-----------FLRYVNE------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 171 TFLDpahqLEILHLL-KEINHIKQ--TTILMsihdINHASRFSDYLIG-----MKAGQIVVQGTPDEVittswmREIYE 241
Cdd:cd03217 133 SGLD----IDALRLVaEVINKLREegKSVLI----ITHYQRLLDYIKPdrvhvLYDGRIVKSGDKELA------LEIEK 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-235 |
2.54e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.67 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQkiallaQSSEHpLGMTvee 99
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ------LRREH-FGFI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 vvsYGRYPYQKFFSGLNEEDLHAIQWALEATQ--------LTKL--KER---ELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:PRK10535 92 ---FQRYHLLSHLTAAQNVEVPAVYAGLERKQrllraqelLQRLglEDRveyQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRfSDYLIGMKAGQIV----------VQGTPDEVITT--S 234
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVT-HDPQVAAQ-AERVIEIRDGEIVrnppaqekvnVAGGTEPVVNTasG 246
|
.
gi 1560390145 235 W 235
Cdd:PRK10535 247 W 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-204 |
2.91e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 5 TTIEAVDittgylnkqvieKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistYSP----KMLAQ 80
Cdd:COG4586 33 REVEAVD------------DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPfkrrKEFAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 81 KIAL-LAQSSE----HPLGMTVE---EVvsYgRYPYQKFFSGLNE--EDLhaiqwaleatQLTKLKERELSSLSGGQAQR 150
Cdd:COG4586 96 RIGVvFGQRSQlwwdLPAIDSFRllkAI--Y-RIPDAEYKKRLDElvELL----------DLGELLDTPVRQLSLGQRMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 151 VWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDIN 204
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-221 |
3.25e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistyspkmlaqkiallaqssehplgmtvEEVVSYGR 105
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG------------------------------KPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 106 YPYQKFFS----------------GLNEEDLHAIQWaLEATQL---TKLKERELS--SLSGGQAQRVWIAMALAQEADIL 164
Cdd:PRK10522 393 EDYRKLFSavftdfhlfdqllgpeGKPANPALVEKW-LERLKMahkLELEDGRISnlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 165 ILDEPTTFLDPAHQ----LEILHLLKEINHikqtTILMSIHDiNHASRFSDYLIGMKAGQI 221
Cdd:PRK10522 472 LLDEWAADQDPHFRrefyQVLLPLLQEMGK----TIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
93-231 |
3.42e-12 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 66.20 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 LGMTVEEVVsygrypyqKFFsglneEDLHAIQWALEATQ---LTKLKereL----SSLSGGQAQRVWIAMALAQEAD--- 162
Cdd:COG0178 786 LDMTVEEAL--------EFF-----ENIPKIARKLQTLQdvgLGYIK---LgqpaTTLSGGEAQRVKLASELSKRSTgkt 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 163 ILILDEPTT---FLDPAHQLEILHLLKE-------INH----IKQttilmsihdinhasrfSDYLI------GMKAGQIV 222
Cdd:COG0178 850 LYILDEPTTglhFHDIRKLLEVLHRLVDkgntvvvIEHnldvIKT----------------ADWIIdlgpegGDGGGEIV 913
|
....*....
gi 1560390145 223 VQGTPDEVI 231
Cdd:COG0178 914 AEGTPEEVA 922
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-231 |
5.03e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKI-----IVDGSEISTyspkmlAQKIALLAQSsehplgmtveev 100
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT------RRRVGYMSQA------------ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 vsygrypyqkfFSgLNEE-------DLHA-------------IQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQE 160
Cdd:NF033858 348 -----------FS-LYGEltvrqnlELHArlfhlpaaeiaarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALV 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-192 |
7.62e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK--------MLAQKIALLAQssehplgMTVEEVVSY 103
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqeagigIIHQELNLIPQ-------LTIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 104 GRYPYQKFfsglneedlHAIQWA---LEATQ-LTKLK-----ERELSSLSGGQAQRVWIAMALAQEADILILDEPTtflD 174
Cdd:PRK10762 103 GREFVNRF---------GRIDWKkmyAEADKlLARLNlrfssDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT---D 170
|
170
....*....|....*...
gi 1560390145 175 PAHQLEILHLLKEINHIK 192
Cdd:PRK10762 171 ALTDTETESLFRVIRELK 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-228 |
1.02e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.16 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSftrLL-----PVKEGKIIVDGSEISTYSPKMLAQK-IALLAQsseH 91
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV---LMghpkyEVTSGSILLDGEDILELSPDERARAgIFLAFQ---Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 PL---GMTVEEVVsygRYPYQKffsgLNEEDLHAIQW---ALEATQLTKLKE----REL-SSLSGGQAQRVWIAMALAQE 160
Cdd:COG0396 86 PVeipGVSVSNFL---RTALNA----RRGEELSAREFlklLKEKMKELGLDEdfldRYVnEGFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 161 ADILILDEPTTFLDpahqLEILHLLKE-INHI--KQTTILMsihdINHASRFSDYL-----IGMKAGQIVVQGTPD 228
Cdd:COG0396 159 PKLAILDETDSGLD----IDALRIVAEgVNKLrsPDRGILI----ITHYQRILDYIkpdfvHVLVDGRIVKSGGKE 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-231 |
1.07e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSeiSTYSPKMlaqkiALLAQSSehplgmtVEEVVSYG 104
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ-----AWIQNDS-------LRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 105 RYPYQKFFSGLNEE-----DLHAiqwaLEATQLTKLKERELSsLSGGQAQRVWIAMALAQEADILILDEPTTFLDP---A 176
Cdd:TIGR00957 723 KALNEKYYQQVLEAcallpDLEI----LPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 177 HQLEilHLLKEINHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:TIGR00957 798 HIFE--HVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-187 |
1.35e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.40 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGyLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistyspkmlaqKIALL 85
Cdd:cd03223 2 ELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 86 AQSSEHPLGmTVEEVVSygrYPYQKffsglneedlhaiqwaleatqltklkerelsSLSGGQAQRVWIAMALAQEADILI 165
Cdd:cd03223 70 PQRPYLPLG-TLREQLI---YPWDD-------------------------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180
....*....|....*....|..
gi 1560390145 166 LDEPTTFLDPAHQLEILHLLKE 187
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE 136
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-201 |
1.64e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLK--SFTRLLPVKEGKIIVDGSEIstysPKMLAQKIALLAQSSEHPLGMTVEEVVSygrypyq 109
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDvlAGRKTAGVITGEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTVREALR------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 110 kfFSGLneedlhaiqwaleatqltklkereLSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEIN 189
Cdd:cd03232 102 --FSAL------------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170
....*....|..
gi 1560390145 190 HIKQtTILMSIH 201
Cdd:cd03232 156 DSGQ-AILCTIH 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-232 |
2.08e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSehplgMTVEEV 100
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP-----VLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPyqkfFSGLNEEDLhaiqW-ALEATQLTKLKER-------ELS----SLSGGQAQRVWIAMALAQEADILILDE 168
Cdd:PLN03232 1326 VRFNIDP----FSEHNDADL----WeALERAHIKDVIDRnpfgldaEVSeggeNFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 169 PTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
32-230 |
2.21e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIV---DGSEISTYSpkMLAQKIALLAQSS-----EHP---LGMTVEev 100
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYA--LSEAERRRLLRTEwgfvhQHPrdgLRMQVS-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 vsygrypyqkffSGLN-EEDLHAIQW----ALEATQLTKLKEREL---------SSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:PRK11701 108 ------------AGGNiGERLMAVGArhygDIRATAGDWLERVEIdaariddlpTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQV 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-221 |
2.99e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-MLAQKIALLAQSSEHP---LGMTV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRKRDglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVSYGRYPYQKFFSG-LNEEDLHaiQWALEATQLTKLK----ERELSSLSGGQAQRVWIAMALAQEADILILDEPTTF 172
Cdd:PRK10762 348 KENMSLTALRYFSRAGGsLKHADEQ--QAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 173 LDPAHQLEILHLlkeINHIKQ---TTILMSiHDINHASRFSDYLIGMKAGQI 221
Cdd:PRK10762 426 VDVGAKKEIYQL---INQFKAeglSIILVS-SEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-189 |
3.25e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 63.23 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSeistyspkmlaQKIALLAQSSEHPLGmTVEEV 100
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLG-TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQKFFSGLNEEDLHAIqwaLEATQLTKLKERELS---------SLSGGQAQRVWIAMALAQEADILILDEPTT 171
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQI---LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170
....*....|....*...
gi 1560390145 172 FLDPAHQLEILHLLKEIN 189
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREFG 629
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-208 |
3.70e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYS----PKMLAQKIALLAQSSehplgMTVEEVVSYGRYP 107
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSF-----MLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 108 YQKFFSGlnEEDLHAIQWALEATQLTKLKEREL---SSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHL 184
Cdd:PRK10584 111 LPALLRG--ESSRQSRNGAKALLEQLGLGKRLDhlpAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|....
gi 1560390145 185 LKEINHIKQTTILMSIHDINHASR 208
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAAR 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
42-170 |
4.07e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.73 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 42 GSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPK-MLAQKIALLaqssehP---------LGMTVEEVVSYGRYPYQKF 111
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYV------PedrkgeglvLDLSIRENITLASLDRLSR 361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 112 FSGLNEEDLHAIqwALEATQLTKLK----ERELSSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:COG1129 362 GGLLDRRRERAL--AEEYIKRLRIKtpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-230 |
4.81e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP---KMLAQKIALLAQSsehPlgmtveevvs 102
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQN---P---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 103 YGRY-PYQKFFSGLnEEDLhAIQWALEATQLtklKERELSSL-----------------SGGQAQRVWIAMALAQEADIL 164
Cdd:PRK11308 102 YGSLnPRKKVGQIL-EEPL-LINTSLSAAER---REKALAMMakvglrpehydryphmfSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEV 230
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-220 |
5.32e-11 |
|
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: 60.91 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 20 QVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSE----ISTYSPKmlaQKIALLaqssEHPLG- 94
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPR---EILALR----RRTIGy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 ----------MTVEEVVsygrypyqkffsglnEEDLHAIQWALEATQ------LTKL--KEReLSSL-----SGGQAQRV 151
Cdd:COG4778 98 vsqflrviprVSALDVV---------------AEPLLERGVDREEARararelLARLnlPER-LWDLppatfSGGEQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 152 WIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEinhIKQ--TTILMSIHDINHASRFSDYLIGMKAGQ 220
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE---AKArgTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-231 |
5.66e-11 |
|
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: 62.66 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGMTVEEV 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKERElSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDpahqLE 180
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGG-ENLSVGQRQLVCLARALLRKTKILVLDEATAAVD----LE 1455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 181 ILHLLKEI--NHIKQTTILMSIHDINHASRFSDYLIgMKAGQIVVQGTPDEVI 231
Cdd:TIGR00957 1456 TDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTRVIV-LDKGEVAEFGAPSNLL 1507
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-225 |
9.11e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 60.35 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTL----------------LKSFTRLLPVKEGKIIVDgsEISTYSPKM-LAQKiaLLAQS 88
Cdd:cd03270 15 DVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARQFLGQMDKPDVD--SIEGLSPAIaIDQK--TTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 89 SEHPLGmTVEEVVSYGRYPYQKffSGLNEEDLHAIQWALEATQLtklkERELSSLSGGQAQRVWIAMALAQEAD--ILIL 166
Cdd:cd03270 91 PRSTVG-TVTEIYDYLRLLFAR--VGIRERLGFLVDVGLGYLTL----SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHD---INHAsrfsDYLI------GMKAGQIVVQG 225
Cdd:cd03270 164 DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE-HDedtIRAA----DHVIdigpgaGVHGGEIVAQG 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-226 |
9.33e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLK------SFTrllpVKEGKIIVDGSEISTYS 74
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKviaghpAYK----ILEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 75 PKMLAQKIALLAqsSEHPL---GMTVEEVVSYGRYPYQKfFSGLNEED-LHAIQWALEATQLTKLKERELS-----SLSG 145
Cdd:CHL00131 78 PEERAHLGIFLA--FQYPIeipGVSNADFLRLAYNSKRK-FQGLPELDpLEFLEIINEKLKLVGMDPSFLSrnvneGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 146 GQAQRVWI-AMALAqEADILILDEPTTFLDpAHQLEILHllKEINHIKQTTilMSIHDINHASRFSDYLIG-----MKAG 219
Cdd:CHL00131 155 GEKKRNEIlQMALL-DSELAILDETDSGLD-IDALKIIA--EGINKLMTSE--NSIILITHYQRLLDYIKPdyvhvMQNG 228
|
....*..
gi 1560390145 220 QIVVQGT 226
Cdd:CHL00131 229 KIIKTGD 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-192 |
1.13e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 1 MKNLTTIEAVDITTGYLNKQVIE---KMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIV-DGSEISTYSPK 76
Cdd:PTZ00265 377 LKDIKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 77 MLAQKIALLAQSsehPL--GMTVEEVVSYGRYPYQKF--------------FSGLNEE---------DLHAIQWALEATQ 131
Cdd:PTZ00265 457 WWRSKIGVVSQD---PLlfSNSIKNNIKYSLYSLKDLealsnyynedgndsQENKNKRnscrakcagDLNDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 132 LTKLKER-----------------------------------ELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDpa 176
Cdd:PTZ00265 534 LIEMRKNyqtikdsevvdvskkvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-- 611
|
250
....*....|....*.
gi 1560390145 177 HQLEILhLLKEINHIK 192
Cdd:PTZ00265 612 NKSEYL-VQKTINNLK 626
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-221 |
1.32e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKM-LAQKIALLA---QSS----EHPLGMT 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSglylDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 97 VEEVVsYGRYPyqkFFsglneedlhaIQWALEATQLTKL----------KERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:PRK15439 362 VCALT-HNRRG---FW----------IKPARENAVLERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHASRFSDYLIGMKAGQI 221
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
143-230 |
2.39e-10 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 60.86 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 143 LSGGQAQRVWIAMALAQEAD---ILILDEPTT---FLDPAHQLEILHLLKE-------INH----IKQttilmsihdinh 205
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTglhFEDIRKLLEVLHRLVDkgntvvvIEHnldvIKT------------ 898
|
90 100 110
....*....|....*....|....*....|.
gi 1560390145 206 asrfSDYLI------GMKAGQIVVQGTPDEV 230
Cdd:PRK00349 899 ----ADWIIdlgpegGDGGGEIVATGTPEEV 925
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-174 |
2.79e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEI--------------STYSpkMLAQKIALLAQSSE--HP 92
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqqdpprnvegTVYD--FVAEGIEEQAEYLKryHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 LGMTVEEvvsygrYPYQKFFSGLNE--EDL-HAIQWALEA---TQLTKLK---ERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:PRK11147 104 ISHLVET------DPSEKNLNELAKlqEQLdHHNLWQLENrinEVLAQLGldpDAALSSLSGGWLRKAALGRALVSNPDV 177
|
170
....*....|.
gi 1560390145 164 LILDEPTTFLD 174
Cdd:PRK11147 178 LLLDEPTNHLD 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-179 |
3.50e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGY------LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFT-RLLPVKEGKIIVDGSeiSTYSPKMla 79
Cdd:PLN03232 612 APAISIKNGYfswdskTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLgELSHAETSSVVIRGS--VAYVPQV-- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 80 qkiallaqssEHPLGMTVEEVVSYG-RYPYQKFFSGLneeDLHAIQWALE---ATQLTKLKERELSsLSGGQAQRVWIAM 155
Cdd:PLN03232 688 ----------SWIFNATVRENILFGsDFESERYWRAI---DVTALQHDLDllpGRDLTEIGERGVN-ISGGQKQRVSMAR 753
|
170 180
....*....|....*....|....*.
gi 1560390145 156 ALAQEADILILDEPTTFLDP--AHQL 179
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAhvAHQV 779
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-232 |
4.47e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYL---NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK------------------------ 59
Cdd:PTZ00265 1166 IEIMDVNFRYIsrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 60 ------------------------------EGKIIVDGSEISTYSPKMLAQKIALLAQsseHPL--GMTVEEVVSYGRyp 107
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQ---EPMlfNMSIYENIKFGK-- 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 108 yqkffSGLNEEDL-HAIQWALEATQLTKLKERELS-------SLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQL 179
Cdd:PTZ00265 1321 -----EDATREDVkRACKFAAIDEFIESLPNKYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 180 EILHLLKEINHIKQTTILMSIHDINHASRfSDYLIGM----KAGQIV-VQGTPDEVIT 232
Cdd:PTZ00265 1396 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVqAHGTHEELLS 1452
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-227 |
5.11e-10 |
|
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: 57.20 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStYSPkmlaQKIallaqssehplgmtveevvsygrypy 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKP----QYI-------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 109 qkffsglneedlhaiqwaleatqltklkerelsSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEI 188
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 1560390145 189 NHIKQTTILMSIHDINHASRFSDYLigmkagqIVVQGTP 227
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRI-------HVFEGEP 149
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-225 |
7.41e-10 |
|
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: 56.56 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLksFTRLLPVKEGKIIvdgSEISTYSPkmlaQKIALLAQSSehplgmtveevv 101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLI---SFLPKFSR----NKLIFIDQLQ------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 102 sygrypyqkffsglneedlhaiqwALEATQLTKLK-ERELSSLSGGQAQRVWIAMALAQEAD--ILILDEPTTFLdpaHQ 178
Cdd:cd03238 70 ------------------------FLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL---HQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 179 LEILHLLKEINHIKQ--TTILMSIHDINhASRFSDYLI------GMKAGQIVVQG 225
Cdd:cd03238 123 QDINQLLEVIKGLIDlgNTVILIEHNLD-VLSSADWIIdfgpgsGKSGGKVVFSG 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-203 |
7.76e-10 |
|
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: 59.15 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLN--KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVkEGKIIVDGSEISTYSPKMLAQKIALLAQS 88
Cdd:TIGR01271 1222 GLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 89 SEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIqwaLE--ATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILIL 166
Cdd:TIGR01271 1301 VFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSV---IEqfPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1560390145 167 DEPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDI 203
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRV 1412
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-226 |
8.97e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTyspkmlaqKIALLAQSSEH-PLGMTVEEV 100
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--------NISDVHQNMGYcPQFDAIDDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSyGR---YPYQKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAH 177
Cdd:TIGR01257 2027 LT-GRehlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1560390145 178 QLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGT 226
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTS-HSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-222 |
1.34e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 58.27 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIStyspkmlaqkiallAQSSEHplgmtveevvsygr 105
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--------------ADNREA-------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 106 ypYQKFFS-------------GLNEEDLHAI--QWaLEATQL---TKLKERELSS--LSGGQAQRVWIAMALAQEADILI 165
Cdd:COG4615 404 --YRQLFSavfsdfhlfdrllGLDGEADPARarEL-LERLELdhkVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILV 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 166 LDEPTtfldpAHQ---------LEILHLLKEINHikqtTILMSIHD---INHASRfsdyLIGMKAGQIV 222
Cdd:COG4615 481 FDEWA-----ADQdpefrrvfyTELLPELKARGK----TVIAISHDdryFDLADR----VLKMDYGKLV 536
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
132-237 |
1.80e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 132 LTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEIL----HLLKEINhikqTTILMSIHDINHAS 207
Cdd:PRK11144 118 IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLpyleRLAREIN----IPILYVSHSLDEIL 193
|
90 100 110
....*....|....*....|....*....|
gi 1560390145 208 RFSDYLIGMKAGQIVVQGTPDEVITTSWMR 237
Cdd:PRK11144 194 RLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
19-228 |
1.97e-09 |
|
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: 56.50 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFT--RLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA-QSSEHPLGM 95
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDERARAGLFLAfQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVsygRYPYQKFFSGLNEEDLHAIQWALEATQLTKLKE--RELSS------LSGGQAQRVWIAMALAQEADILILD 167
Cdd:TIGR01978 93 SNLEFL---RSALNARRSARGEEPLDLLDFEKLLKEKLALLDmdEEFLNrsvnegFSGGEKKRNEILQMALLEPKLAILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 168 EPTTFLDpAHQLEIlhLLKEINHIKQTTilMSIHDINHASRFSDYLIG-----MKAGQIVVQGTPD 228
Cdd:TIGR01978 170 EIDSGLD-IDALKI--VAEGINRLREPD--RSFLIITHYQRLLNYIKPdyvhvLLDGRIVKSGDVE 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-175 |
2.42e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA 86
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEhplgmtVEEVVSYgrypyqkffSGLNEedlhAIQWaleatqLTKLKErelssLSGGQAQRVWIAMALAQEADILIL 166
Cdd:COG2401 111 DFKD------AVELLNA---------VGLSD----AVLW------LRRFKE-----LSTGQKFRFRLALLLAERPKLLVI 160
|
....*....
gi 1560390145 167 DEPTTFLDP 175
Cdd:COG2401 161 DEFCSHLDR 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-176 |
2.54e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPLGmTVEEV 100
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSygrypyqKFFSGLNEEdlhaiQWAleATQLTKLKERELSSLSG--------------GQAQRVWIAMALAQEADILIL 166
Cdd:PTZ00243 1404 VD-------PFLEASSAE-----VWA--ALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSGFIL 1469
|
170
....*....|.
gi 1560390145 167 -DEPTTFLDPA 176
Cdd:PTZ00243 1470 mDEATANIDPA 1480
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-203 |
2.59e-09 |
|
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: 56.40 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLN--KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVkEGKIIVDGSEISTYSPKMLAQKIAL 84
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEHPLGMTVEEVVSYGRYPYQKFFSGLNEEDLHAIQWALEAtQLTKLKERELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPG-QLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDI 203
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRI 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-232 |
2.79e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKI-PEGKVtSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSehplgMTVEE 99
Cdd:PLN03130 1254 VLHGLSFEIsPSEKV-GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAP-----VLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 100 VVSYGRYPyqkfFSGLNEEDLhaiqW-ALEATQLTKLKER-------ELS----SLSGGQAQRVWIAMALAQEADILILD 167
Cdd:PLN03130 1328 TVRFNLDP----FNEHNDADL----WeSLERAHLKDVIRRnslgldaEVSeageNFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 168 EPTTFLDPAHQLEILHLLKEinHIKQTTILMSIHDINHASRfSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-232 |
3.05e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPkMLAQK--IAL 84
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQlgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQsseHPL---GMTVEEVVSYG----RYPYQKFFSGLNEE----DLHAIQWALE-ATQltklkerelsslsggqaQRVW 152
Cdd:PRK15439 91 VPQ---EPLlfpNLSVKENILFGlpkrQASMQKMKQLLAALgcqlDLDSSAGSLEvADR-----------------QIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 153 IAMALAQEADILILDEPTTFLDPAhqlEILHLLKEINHIKQTT--ILMSIHDINHASRFSDYLIGMKAGQIVVQG----- 225
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPA---ETERLFSRIRELLAQGvgIVFISHKLPEIRQLADRISVMRDGTIALSGktadl 227
|
....*..
gi 1560390145 226 TPDEVIT 232
Cdd:PRK15439 228 STDDIIQ 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
39-207 |
3.05e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 39 GPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKmLAQKIALLAqsseHPLG----MTVEEVVSYgrypYQKFFSG 114
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-YHQDLLYLG----HQPGikteLTALENLRF----YQRLHGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 115 LNEEDLHAiqwALEATQLTKLKERELSSLSGGQAQRVwiamALA----QEADILILDEPTTFLDPAHQLEILHLLKEinH 190
Cdd:PRK13538 105 GDDEALWE---ALAQVGLAGFEDVPVRQLSAGQQRRV----ALArlwlTRAPLWILDEPFTAIDKQGVARLEALLAQ--H 175
|
170
....*....|....*....
gi 1560390145 191 IKQ--TTILMSIHDINHAS 207
Cdd:PRK13538 176 AEQggMVILTTHQDLPVAS 194
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-181 |
3.69e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.02 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistyspkmlaqKIALLAQSSEHPLGMTVEEV 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 ---VSYGRYPYQKFFSGLN-EEDLHAiqwaLEATQLTKLKERELSsLSGGQAQRVWIAMALAQEADILILDEPTTFLDPA 176
Cdd:cd03291 119 ifgVSYDEYRYKSVVKACQlEEDITK----FPEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
....*
gi 1560390145 177 HQLEI 181
Cdd:cd03291 194 TEKEI 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-201 |
3.94e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 11 DITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK--EGKIIVDGSEIStyspKMLAQKIALLAQS 88
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 89 SEHPLGMTVEEV---VSYGRYPYqkffSGLNEEDLHAIQWALEATQLTKLKERELSS-----LSGGQAQRVWIAMALAQE 160
Cdd:PLN03211 149 DILYPHLTVRETlvfCSLLRLPK----SLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1560390145 161 ADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIH 201
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH 264
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-231 |
4.36e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 14 TGYLNKQVIE---KMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSE 90
Cdd:PRK15112 18 TGWFRRQTVEavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 91 HPLGmtveevvsygryPYQKFFSGLN-----EEDLHAIqwALEATQLTKLKEREL---------SSLSGGQAQRVWIAMA 156
Cdd:PRK15112 98 TSLN------------PRQRISQILDfplrlNTDLEPE--QREKQIIETLRQVGLlpdhasyypHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 157 LAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-205 |
6.09e-09 |
|
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: 53.53 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEIstyspkmlaqkiallaqssehplgmtveevvsygrypyqkf 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGED----------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 112 fsglneedlhaIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEIL-----HLLK 186
Cdd:smart00382 41 -----------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLL 109
|
170
....*....|....*....
gi 1560390145 187 EINHIKQTTILMSIHDINH 205
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKD 128
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-254 |
9.21e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 21 VIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGseistyspkmlaqKIALLAQSSEHPLGMTVEEV 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 ---VSYGRYPYQKFFSGLN-EEDLhaiqwaleatqlTKLKERELS-------SLSGGQAQRVWIAMALAQEADILILDEP 169
Cdd:TIGR01271 508 ifgLSYDEYRYTSVIKACQlEEDI------------ALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 170 TTFLDPAHQLEILH--------------LLKEINHIKQTTILMSIHD------------INHASRFSDYLIGMKAGQIVV 223
Cdd:TIGR01271 576 FTHLDVVTEKEIFEsclcklmsnktrilVTSKLEHLKKADKILLLHEgvcyfygtfselQAKRPDFSSLLLGLEAFDNFS 655
|
250 260 270
....*....|....*....|....*....|.
gi 1560390145 224 QGTPDEVITTSWMREIYEIEAQIIELPETNK 254
Cdd:TIGR01271 656 AERRNSILTETLRRVSIDGDSTVFSGPETIK 686
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-201 |
1.32e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEI----STYSpkmlaQKI 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlCTYQ-----KQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 83 ALLAQSSEHPLGMTVEEVVSYgrypyqkffsglneeDLHAIQWALEATQLTKLKERE------LSSLSGGQAQRVWIAMA 156
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLY---------------DIHFSPGAVGITELCRLFSLEhlidypCGLLSSGQKRQVALLRL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1560390145 157 LAQEADILILDEPTTFLDpahQLEILHLLKEIN-HIKQ-TTILMSIH 201
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALD---ELSLLTIITKIQeHRAKgGAVLLTSH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-199 |
1.44e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 6 TIEAVDITTGYLNKQViEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQK-IAL 84
Cdd:PRK09700 264 TVFEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 85 LAQSSEH---------PLGMTVEEVVSYGRYpyqKFFSGLNEEDLHAiQWALEATQLTKLK----ERELSSLSGGQAQRV 151
Cdd:PRK09700 343 ITESRRDngffpnfsiAQNMAISRSLKDGGY---KGAMGLFHEVDEQ-RTAENQRELLALKchsvNQNITELSGGNQQKV 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1560390145 152 WIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMS 199
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-174 |
1.98e-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: 54.56 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKsftrllpvkegkiIVDGSEiSTYSPKMLAQ---KIALLAQSSEHPLG 94
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVD-KDFNGEARPQpgiKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MTVEEVVSYGRYPYQKFFSGLNE---------EDLHA-------IQWALEATQLTKLkEREL----------------SS 142
Cdd:TIGR03719 83 KTVRENVEEGVAEIKDALDRFNEisakyaepdADFDKlaaeqaeLQEIIDAADAWDL-DSQLeiamdalrcppwdadvTK 161
|
170 180 190
....*....|....*....|....*....|..
gi 1560390145 143 LSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-232 |
2.89e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKSFT----RLLPVKeGKIIVDGSEISTYSPKMLAqkiALLAQSSEHPLGMTVEEVVSYG 104
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAgkldPSLKVS-GEITYNGYRLNEFVPRKTS---AYISQNDVHVGVMTVKETLDFS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 105 --------RYpyqKFFSGL------------NEEDLHAIQWALEATQL------------------TKLKERELSSLSGG 146
Cdd:PLN03140 264 arcqgvgtRY---DLLSELarrekdagifpeAEVDLFMKATAMEGVKSslitdytlkilgldickdTIVGDEMIRGISGG 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 147 QAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSIhdINHASR----FSDyLIGMKAGQIV 222
Cdd:PLN03140 341 QKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSL--LQPAPEtfdlFDD-IILLSEGQIV 417
|
250
....*....|
gi 1560390145 223 VQGTPDEVIT 232
Cdd:PLN03140 418 YQGPRDHILE 427
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-202 |
3.69e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.22 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 34 VTSLIGPNGSGKSTLLK----SFTRLLPvkegkiivDGSEISTYSPKMlAQKIALLAQSSEHplgmtveevvsygrypyq 109
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELP--------PNSKGGAHDPKL-IREGEVRAQVKLA------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 110 kfFSGLNEEDLHAIQW--ALEAT------QLTKLKERELSSLSGGQ------AQRVWIAMALAQEADILILDEPTTFLDP 175
Cdd:cd03240 77 --FENANGKKYTITRSlaILENVifchqgESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180
....*....|....*....|....*...
gi 1560390145 176 AHQLEILH-LLKEINHIKQTTILMSIHD 202
Cdd:cd03240 155 ENIEESLAeIIEERKSQKNFQLIVITHD 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-211 |
5.22e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSSEHPL--------GMTV 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMlspgeddtGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 98 EEVVsygrypyqkffsglnEEDLHAIQWALE-ATQL--TKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:PRK10938 103 AEII---------------QDEVKDPARCEQlAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1560390145 175 PAHQLEILHLLKEINHIKQTTILMSihdinhaSRFSD 211
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVL-------NRFDE 197
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-211 |
8.47e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP--VKEGKIIVDGSEISTYSPK--------MLAQKIALLaqssehPLgM 95
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCRFKDIRdsealgivIIHQELALI------PY-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 96 TVEEVVsygrypyqkfFSGlNEedlHA----IQWA---LEATQLTK---LKER---ELSSLSGGQAQRVWIAMALAQEAD 162
Cdd:NF040905 94 SIAENI----------FLG-NE---RAkrgvIDWNetnRRARELLAkvgLDESpdtLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1560390145 163 ILILDEPTTFL---DPAHQLEILHLLKEinhikQ--TTILMSiHDINHASRFSD 211
Cdd:NF040905 160 LLILDEPTAALneeDSAALLDLLLELKA-----QgiTSIIIS-HKLNEIRRVAD 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
94-231 |
1.02e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 94 GMTVEEVVSYGRYPYQKFFsgLNEEDLHAIQWALEATQLTKLK-ERELSSLSGGQAQRVWIAMAL---AQEADILILDEP 169
Cdd:PRK00635 762 GKNIADILEMTAYEAEKFF--LDEPSIHEKIHALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEP 839
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 170 TTFLDPAHQLEILHLLKEINHIKQTTILMSiHDInHASRFSDYLI------GMKAGQIVVQGTPDEVI 231
Cdd:PRK00635 840 TTGLHTHDIKALIYVLQSLTHQGHTVVIIE-HNM-HVVKVADYVLelgpegGNLGGYLLASCSPEELI 905
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-231 |
1.74e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.06 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLAQSsehPLgmtve 98
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD---PI----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 99 evvsygrypyqkFFSG-----LNEEDLHAIQWALEATQLTKLKEReLSSLSG---------------GQAQRVWIAMALA 158
Cdd:cd03288 106 ------------LFSGsirfnLDPECKCTDDRLWEALEIAQLKNM-VKSLPGgldavvteggenfsvGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390145 159 QEADILILDEPTTFLDPAHQlEILHLLKEINHIKQTTILMS--IHDINHAsrfsDYLIGMKAGQIVVQGTPDEVI 231
Cdd:cd03288 173 RKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAhrVSTILDA----DLVLVLSRGILVECDTPENLL 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-257 |
2.13e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 9 AVDITTGYL------NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKS-FTRLLPVKEGKIIVDGSeistyspkmlaqk 81
Cdd:PLN03130 614 AISIKNGYFswdskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRGT------------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 82 IALLAQSSeHPLGMTVEEVVSYGRyPYQ--KFFSGLNEEDLHAIQWALEATQLTKLKERELSsLSGGQAQRVWIAMALAQ 159
Cdd:PLN03130 681 VAYVPQVS-WIFNATVRDNILFGS-PFDpeRYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 160 EADILILDEPTTFLDpAH---QLEILHLLKEINHIKQTTILMSIHDINHAsrfsDYLIGMKAGQIVVQGTPDEVITTSW- 235
Cdd:PLN03130 758 NSDVYIFDDPLSALD-AHvgrQVFDKCIKDELRGKTRVLVTNQLHFLSQV----DRIILVHEGMIKEEGTYEELSNNGPl 832
|
250 260 270
....*....|....*....|....*....|..
gi 1560390145 236 ----------MREIYEIEAQIIELPETNKPVV 257
Cdd:PLN03130 833 fqklmenagkMEEYVEENGEEEDDQTSSKPVA 864
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-229 |
3.60e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKiiVDGSEIStyspkmlaqKIALLA 86
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--VKWSENA---------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEH--PLGMTVEEVVSYGRYPyqkffsGLNEEDLHAIQWALEATQLTKLKerELSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:PRK15064 389 QDHAYdfENDLTLFDWMSQWRQE------GDDEQAVRGTLGRLLFSQDDIKK--SVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390145 165 ILDEPTTFLDpAHQLEILHLLKEinHIKQTTILMSiHDINHASRFSDYLIGMKAGQIV-VQGTPDE 229
Cdd:PRK15064 461 VMDEPTNHMD-MESIESLNMALE--KYEGTLIFVS-HDREFVSSLATRIIEITPDGVVdFSGTYEE 522
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-202 |
6.70e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 8 EAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVdGSEIstyspkmlaqKIALLAQ 87
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL----------EVAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 SSEH--PlGMTVEEVVSYGRypyQKFFsgLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILI 165
Cdd:PRK11147 390 HRAEldP-EKTVMDNLAEGK---QEVM--VNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190
....*....|....*....|....*....|....*..
gi 1560390145 166 LDEPTTFLDpahqLEILHLLKEINHIKQTTILMSIHD 202
Cdd:PRK11147 464 LDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-217 |
1.31e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSftrllpvkegkIIVdgseistyspkmlaqkIALLAQSSEHPLGMTVEEVVSygr 105
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDA-----------IGL----------------ALGGAQSATRRRSGVKAGCIV--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 106 yPYQKffsglneedLHAIQwaleatqltklkerELSSLSGGQAQRVWIAMALA----QEADILILDEPTTFLDPAHQLEI 181
Cdd:cd03227 65 -AAVS---------AELIF--------------TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 1560390145 182 LHLLKEinHIKQTTILMSIHDINHASRFSDYLIGMK 217
Cdd:cd03227 121 AEAILE--HLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
127-249 |
1.36e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 127 LEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIHDINHA 206
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEA 207
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1560390145 207 SRFSDYLIGMKAGQIVVQGTPDEVITTSWMREIYEIEAQIIEL 249
Cdd:NF000106 208 EQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAEL 250
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
42-170 |
1.37e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 42 GSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSP-KMLAQKIALLaqsSEHPLG------MTVEE---VVSYGRYPYQKF 111
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrERRRLGVAYI---PEDRLGrglvpdMSVAEnliLGRYRRPPFSRG 370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560390145 112 FSglneedlhaIQWALEATQLTKLKER----------ELSSLSGGQAQRVWIAMALAQEADILILDEPT 170
Cdd:COG3845 371 GF---------LDRKAIRAFAEELIEEfdvrtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
137-231 |
1.62e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.87 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 137 ERELSSLSGGQAQRVWIAMAL-AQEADIL-ILDEPTTFLdpaHQ------LEILHLLKEI-NhikqtTILMSIHD---IN 204
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQIgSGLVGVLyVLDEPSIGL---HQrdndrlIETLKRLRDLgN-----TVIVVEHDedtIR 551
|
90 100 110
....*....|....*....|....*....|...
gi 1560390145 205 HAsrfsDYLI------GMKAGQIVVQGTPDEVI 231
Cdd:COG0178 552 AA----DYIIdigpgaGEHGGEVVAQGTPEEIL 580
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-202 |
2.16e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 36 SLIGPNGSGKSTLLKSFTRLLPVKEGKIIvdgseistYSPKMlaqKIALLAQSSEHPLGMTVEEVVSYGRypyqkFFSGL 115
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKV---RMAVFSQHHVDGLDLSSNPLLYMMR-----CFPGV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 116 NEEDLHAIQWALEATqlTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDpahqLEILHLLKEINHIKQTT 195
Cdd:PLN03073 603 PEQKLRAHLGSFGVT--GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQGLVLFQGG 676
|
....*..
gi 1560390145 196 ILMSIHD 202
Cdd:PLN03073 677 VLMVSHD 683
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-230 |
2.58e-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: 48.47 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 137 ERELSSLSGGQAQRVWIAMALAQE--ADILILDEPTTFLdpaHQLEILHLLKEINHIKQ--TTILMSIHD---INHASRF 209
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGL---HQRDNRRLINTLKRLRDlgNTLIVVEHDedtIRAADYV 559
|
90 100
....*....|....*....|....*
gi 1560390145 210 SDylIGMKA----GQIVVQGTPDEV 230
Cdd:TIGR00630 560 ID--IGPGAgehgGEVVASGTPEEI 582
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-185 |
2.86e-06 |
|
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: 47.90 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVK-EGKIIVDGSEISTYSPkmlaqkiallAQSSEHPLGMTVEEV 100
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNP----------AQAIRAGIAMVPEDR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 101 VSYGRYPYQ-----------KFFSGLNEEDLHAIQWAL-EATQLTKLKERE----LSSLSGGQAQRVWIAMALAQEADIL 164
Cdd:TIGR02633 346 KRHGIVPILgvgknitlsvlKSFCFKMRIDAAAELQIIgSAIQRLKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180
....*....|....*....|.
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLL 185
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLI 446
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-185 |
4.30e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 18 NKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLP-VKEGKIIVDGSEISTYSP-KMLAQKIALLAQSSEH---- 91
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPqQAIAQGIAMVPEDRKRdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 92 PLgMTVEE---VVSYGRYpyqKFFSGLNEE-DLHAIQwalEATQLTKLK----ERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:PRK13549 354 PV-MGVGKnitLAALDRF---TGGSRIDDAaELKTIL---ESIQRLKVKtaspELAIARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180
....*....|....*....|..
gi 1560390145 164 LILDEPTTFLDPAHQLEILHLL 185
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLI 448
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-199 |
5.66e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 17 LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKmlaqkiallaQSSEHPLGMT 96
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN----------EAINHGFALV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 97 VEEVVSYGRYP---------------YQKFFSGLNEEDLHA-IQWALEATQL-TKLKERELSSLSGGQAQRVWIAMALAQ 159
Cdd:PRK10982 329 TEERRSTGIYAyldigfnslisnirnYKNKVGLLDNSRMKSdTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLT 408
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1560390145 160 EADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMS 199
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-201 |
6.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSftrLLPVKEGKIIVDGSEISTYSP--KMLAQKIALLAQSSEHPLGMTVEEVVSYGRYPYQ 109
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPldSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 110 KFFSGLNEEDLHaIQWALEATQLTKLKEREL----SSLSGGQAQRVWIAMALAQEADILI-LDEPTTFLDPAHQLEILHL 184
Cdd:TIGR00956 866 PKSVSKSEKMEY-VEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
170
....*....|....*..
gi 1560390145 185 LKEINHIKQtTILMSIH 201
Cdd:TIGR00956 945 MRKLADHGQ-AILCTIH 960
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-202 |
6.78e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 29 IPEGKVTSLIGPNGSGKSTLLKsftrLLpvkEGKIIVDGSEIStyspkmLAQKIALLAQSSEHP-LGMTVEEVVSYGRYP 107
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLA----LL---KNEISADGGSYT------FPGNWQLAWVNQETPaLPQPALEYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 108 YQKFFSGLN----EEDLHAIQ-----------WALEATQLTKLK---------ERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:PRK10636 91 YRQLEAQLHdaneRNDGHAIAtihgkldaidaWTIRSRAASLLHglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1560390145 164 LILDEPTTFLDpahqLE-ILHLLKEINHIKQTTILMSiHD 202
Cdd:PRK10636 171 LLLDEPTNHLD----LDaVIWLEKWLKSYQGTLILIS-HD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-174 |
6.88e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 37 LIGPNGSGKSTLLKSFTRLLPVKEGKIIVdgseistySPKMlaqKIALLAQssEHPL--GMTVEEVVSYG---------R 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGI---KVGYLPQ--EPQLdpEKTVRENVEEGvaevkaaldR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 106 YP--YQKF------FSGLNEE--DLHAIQWALEATQL-TKL-----------KERELSSLSGGQAQRVWIAMALAQEADI 163
Cdd:PRK11819 105 FNeiYAAYaepdadFDALAAEqgELQEIIDAADAWDLdSQLeiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKPDM 184
|
170
....*....|.
gi 1560390145 164 LILDEPTTFLD 174
Cdd:PRK11819 185 LLLDEPTNHLD 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-174 |
7.75e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 19 KQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFT--RLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA---------Q 87
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAfqypveipgV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 88 SSEHPLGMTVEEVVSY-GRYPYQKF-FSGLNEEDLHAIQwaLEATQLTklkeRELS-SLSGGQAQRVWIAMALAQEADIL 164
Cdd:PRK09580 94 SNQFFLQTALNAVRSYrGQEPLDRFdFQDLMEEKIALLK--MPEDLLT----RSVNvGFSGGEKKRNDILQMAVLEPELC 167
|
170
....*....|
gi 1560390145 165 ILDEPTTFLD 174
Cdd:PRK09580 168 ILDESDSGLD 177
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
111-251 |
1.05e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 111 FFSGLNEEDLhAIQWALEA--TQLTKL---------KERELSSLSGGQAQRVWIAMALAQE--ADILILDEPTTFLDPAH 177
Cdd:PRK00635 435 FLSQLPSKSL-SIEEVLQGlkSRLSILidlglpyltPERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQD 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 178 QLEILHLLKEINHiKQTTILMSIHD---INHASRFSDylIGMKA----GQIVVQGTPDEVITTS-WMREIYEIEAQIIEL 249
Cdd:PRK00635 514 THKLINVIKKLRD-QGNTVLLVEHDeqmISLADRIID--IGPGAgifgGEVLFNGSPREFLAKSdSLTAKYLRQELTIPI 590
|
..
gi 1560390145 250 PE 251
Cdd:PRK00635 591 PE 592
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-246 |
1.19e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 32 GKVTSLIGPNGSGKSTLLKSftrLLPVKEGKIIVDGSEISTYSPKM--LAQKIALLAQSSEHPLGMTVEEVVSYG---RY 106
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPKKQetFARISGYCEQNDIHSPQVTVRESLIYSaflRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 107 PyqKFFSglNEEDLHAIQWALEATQLTKLKER-----ELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDpAHQLEI 181
Cdd:PLN03140 983 P--KEVS--KEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAAAI 1057
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 182 lhLLKEINHIKQT--TILMSIH----DINHAsrFSDYLIGMKAGQIVVQGT---------------------PDEVITTS 234
Cdd:PLN03140 1058 --VMRTVRNTVDTgrTVVCTIHqpsiDIFEA--FDELLLMKRGGQVIYSGPlgrnshkiieyfeaipgvpkiKEKYNPAT 1133
|
250
....*....|..
gi 1560390145 235 WMREIYEIEAQI 246
Cdd:PLN03140 1134 WMLEVSSLAAEV 1145
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
15-56 |
1.90e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.43 E-value: 1.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1560390145 15 GYLNKQVIEkmsikIPEGKVTSLIGPNGSGKSTLLKSFTRLL 56
Cdd:pfam13555 10 GTFDGHTIP-----IDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
22-230 |
2.86e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.57 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIpeGKVTSLIGPNGSGKSTLLKSFT-------------RLLPVKEGKIIVDGSEISTYSPKMLAQkiaLLAQS 88
Cdd:COG4938 12 FKEAELEL--KPLTLLIGPNGSGKSTLIQALLlllqsnfiylpaeRSGPARLYPSLVRELSDLGSRGEYTAD---FLAEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 89 SEHPLGMTVEEVVSYGRYPY-QKFFSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMAL---AQEADIL 164
Cdd:COG4938 87 ENLEILDDKSKELLEQVEEWlEKIFPGKVEVDASSDLVRLVFRPSGNGKRIPLSNVGSGVSELLPILLALlsaAKPGSLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 165 ILDEPTTFLDPAHQLEILHLLKEI-NHIKQttILMSIHdinhasrfSDYLI-----GMKAGQIVvqgTPDEV 230
Cdd:COG4938 167 IIEEPEAHLHPKAQSALAELLAELaNSGVQ--VIIETH--------SDYILnglrnLIKEGKLL---DPDDV 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-232 |
4.34e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 25 MSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistyspkmlaqkiALLAQSSEHPLGMTVEEVVSyg 104
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------ALIAISSGLNGQLTGIENIE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 105 rypYQKFFSGLNEEDLHAI-QWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDpahQLEILH 183
Cdd:PRK13545 108 ---LKGLMMGLTKEKIKEIiPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 184 LLKEINHIKQT--TILMSIHDINHASRFSDYLIGMKAGQIVVQGTPDEVIT 232
Cdd:PRK13545 182 CLDKMNEFKEQgkTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-174 |
5.52e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGylNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFT-----------RLLPVKEGkiiVDGSEISTYS- 74
Cdd:PLN03073 180 MENFSISVG--GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncQILHVEQE---VVGDDTTALQc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 75 --------PKMLAQKIALLAQ--------------------SSEHPLGMTVEEVvsYGRYPYQKFFSGlnEEDLHAIQWA 126
Cdd:PLN03073 255 vlntdierTQLLEEEAQLVAQqrelefetetgkgkgankdgVDKDAVSQRLEEI--YKRLELIDAYTA--EARAASILAG 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1560390145 127 LEATqlTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:PLN03073 331 LSFT--PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
34-227 |
9.01e-05 |
|
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: 43.15 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 34 VTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYSPKMLAQKIALLA--QSSEHPLGMTVEEVVSYgrypyqKF 111
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDpkEPIEFEISEFLEDGVRY------RY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 112 FSGLNEEDLHAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHI 191
Cdd:pfam13304 75 GLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1560390145 192 KQTTILMSIHDINHASRFSDYLIGMKAGQIVVQGTP 227
Cdd:pfam13304 155 LLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVR 190
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
14-189 |
1.17e-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: 42.26 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 14 TGYLNKQVIEKMSIkipEGKVTSLI-GPNGSGKSTLLKSFTRLLpvkEGKIIVDGSEISTYSpkmlaqkialLAQSSEHP 92
Cdd:cd03279 12 GPFREEQVIDFTGL---DNNGLFLIcGPTGAGKSTILDAITYAL---YGKTPRYGRQENLRS----------VFAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 93 LGMTVEEVVSYGRYPYQKFFsGLNEEDLhaIQWA-LEATQLTKLKERELSSLSGGQAQRVWIAMALA-----QEA----- 161
Cdd:cd03279 76 AEVSFTFQLGGKKYRVERSR-GLDYDQF--TRIVlLPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlQNRggarl 152
|
170 180
....*....|....*....|....*...
gi 1560390145 162 DILILDEPTTFLDPAHQLEILHLLKEIN 189
Cdd:cd03279 153 EALFIDEGFGTLDPEALEAVATALELIR 180
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-191 |
1.35e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 34 VTSLIGPNGSGKSTLLKSFTRLLpvkEGKIIVDGSEIStyspkmlaqkiALLAQSSEHplgMTVEEVVSYGRYPY----- 108
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYAL---YGKARSRSKLRS-----------DLINVGSEE---ASVELEFEHGGKRYrierr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 109 ---------------QKFFSGL--------NEEDLHAIQWALE-----ATQLTKLKERELS---------SLSGGQAqrv 151
Cdd:COG0419 88 qgefaefleakpserKEALKRLlgleiyeeLKERLKELEEALEsaleeLAELQKLKQEILAqlsgldpieTLSGGER--- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1560390145 152 wIAMALAQEADiLILDepTTFLDPAHQLEILHLLKEINHI 191
Cdd:COG0419 165 -LRLALADLLS-LILD--FGSLDEERLERLLDALEELAII 200
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-174 |
1.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1560390145 136 KERELSSLSGGQ------AQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:PRK03918 782 KERPLTFLSGGErialglAFRLALSLYLAGNIPLLILDEPTPFLD 826
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-201 |
1.67e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGkVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIV--DGSEISTYSP---------KMLAQKI--ALLAQS 88
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDeeDFYLGDDPDLpeieieltfGSLLSRLlrLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 89 SEHPLGMTVEEVvsygRYPYQKFFSGLNEE---------DLHAIQWALEATQLTKL-----------KERELSSLSGGQA 148
Cdd:COG3593 93 DKEELEEALEEL----NEELKEALKALNELlseylkellDGLDLELELSLDELEDLlkslslriedgKELPLDRLGSGFQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390145 149 QrvWIAMALAQ---------EADILILDEPTTFLDPAHQLEILHLLKEINHiKQTTILMSIH 201
Cdd:COG3593 169 R--LILLALLSalaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSE-KPNQVIITTH 227
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-174 |
1.98e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 17 LNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEISTYsPKMLAQKIAllaqsseHPLGMT 96
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-AKPYCTYIG-------HNLGLK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560390145 97 VEEVVSYGRYPYQKFFSGLNeedlhAIQWALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLD 174
Cdd:PRK13541 83 LEMTVFENLKFWSEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-231 |
2.17e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 137 ERELSSLSGGQAQRVWIAmalAQeadI---L-----ILDEPTTFLdpaHQ------LEILHLLKEI-NhikqtTILMSIH 201
Cdd:PRK00349 484 SRSAGTLSGGEAQRIRLA---TQ---IgsgLtgvlyVLDEPSIGL---HQrdndrlIETLKHLRDLgN-----TLIVVEH 549
|
90 100 110
....*....|....*....|....*....|....*....
gi 1560390145 202 D---INHAsrfsDYL--IGMKAG----QIVVQGTPDEVI 231
Cdd:PRK00349 550 DedtIRAA----DYIvdIGPGAGvhggEVVASGTPEEIM 584
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
143-232 |
2.27e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 143 LSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLEILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIV 222
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVS-SDLPEVLGVADRIVVMREGRIA 475
|
90
....*....|....*
gi 1560390145 223 -----VQGTPDEVIT 232
Cdd:PRK11288 476 gelarEQATERQALS 490
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-56 |
3.34e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 3.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1560390145 4 LTTIEAvditTGYLNkqvIEKMSIKIpeGKVTSLIGPNGSGKSTLLKSFtRLL 56
Cdd:COG4637 2 ITRIRI----KNFKS---LRDLELPL--GPLTVLIGANGSGKSNLLDAL-RFL 44
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-175 |
4.34e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKsftrllpvkegkiIVDGSEISTYSPKM--------- 77
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS-------------LITGDHPQGYSNDLtlfgrrrgs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 78 ------LAQKIALLAQS--SEHPLGMTVEEVVSYGrypyqkFFS--GL-----NEEDLHAIQWaLEATQLTK-LKERELS 141
Cdd:PRK10938 328 getiwdIKKHIGYVSSSlhLDYRVSTSVRNVILSG------FFDsiGIyqavsDRQQKLAQQW-LDILGIDKrTADAPFH 400
|
170 180 190
....*....|....*....|....*....|....
gi 1560390145 142 SLSGGQAQRVWIAMALAQEADILILDEPTTFLDP 175
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-201 |
5.02e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEG-KVTSLIGPNGSGKSTLLKSFTRLLPVKEGKII-VDGSEISTYSPKMLAQKIALLAQSS-----EHPLG 94
Cdd:COG3950 14 FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIALALSGLLSRLDdVKFRKLLIRNGEFGDSAKLILYYGTsrlllDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 95 MTVEEVVSYG------------RYPYQKFFSGLNE--EDLHAIQWALEATQLTKLK------------------------ 136
Cdd:COG3950 94 KLERLKEEYFsrldgydslldeDSNLREFLEWLREylEDLENKLSDELDEKLEAVRealnkllpdfkdiridrdpgrlvi 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 137 ------ERELSSLSGGQAQRV----WIAMALAQEAD----------ILILDEPTTFLDPAHQLEILHLLKEInhIKQTTI 196
Cdd:COG3950 174 ldkngeELPLNQLSDGERSLLalvgDLARRLAELNPalenplegegIVLIDEIDLHLHPKWQRRILPDLRKI--FPNIQF 251
|
....*
gi 1560390145 197 LMSIH 201
Cdd:COG3950 252 IVTTH 256
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-202 |
1.49e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 7 IEAVDITTGYLNKQVIEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGSEistyspkmlaqKIALLA 86
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 87 QSSEHPLGMTVEEVVSYGrypYQKFFSGLNEEDlhAIQWALEATQLTKLKEREL-------------------------- 140
Cdd:PRK15064 71 QDQFAFEEFTVLDTVIMG---HTELWEVKQERD--RIYALPEMSEEDGMKVADLevkfaemdgytaearagelllgvgip 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 141 --------SSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAhqlEILHLLKEINHIKQTTILMSiHD 202
Cdd:PRK15064 146 eeqhyglmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN---TIRWLEDVLNERNSTMIIIS-HD 211
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
23-46 |
4.00e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.44 E-value: 4.00e-03
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
20-64 |
4.70e-03 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 36.69 E-value: 4.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1560390145 20 QVIEKMsIKIPEGKVtsLI-GPNGSGKSTLLKSFTRLLPVKEGKII 64
Cdd:cd01129 1 ARLRRL-IKRPHGLI--LVtGPTGSGKTTTLYAMLRELNGPERNII 43
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-231 |
5.59e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.49 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 22 IEKMSIKIPEGKVTSLIGPNGSGKSTLLKSFTRLLPVKEGKIIVDGsEISTyspkmlaqkIALLAQSSEHPLGMTVEEvv 101
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSV---------IAISAGLSGQLTGIENIE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390145 102 sygrypYQKFFSGLNEEDLHAIQ-WALEATQLTKLKERELSSLSGGQAQRVWIAMALAQEADILILDEPTTFLDPAHQLE 180
Cdd:PRK13546 108 ------FKMLCMGFKRKEIKAMTpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560390145 181 ILHLLKEINHIKQTTILMSiHDINHASRFSDYLIGMKAGQIVVQGTPDEVI 231
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVS-HNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
26-52 |
7.56e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 36.84 E-value: 7.56e-03
10 20
....*....|....*....|....*..
gi 1560390145 26 SIKIPEGKVTSLIGPNGSGKSTLLKSF 52
Cdd:cd03243 23 DINLGSGRLLLITGPNMGGKSTYLRSI 49
|
|
|