|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-258 |
3.50e-143 |
|
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: 401.34 E-value: 3.50e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLP 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIVPEGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQV 245
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|...
gi 1752086653 246 INDPVSNTPLIVP 258
Cdd:COG1120 242 IEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-257 |
9.56e-116 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 332.36 E-value: 9.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:PRK11231 84 HHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQVI 246
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIH 242
|
250
....*....|.
gi 1752086653 247 NDPVSNTPLIV 257
Cdd:PRK11231 243 PEPVSGTPMCV 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-261 |
2.69e-106 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 308.84 E-value: 2.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEG 93
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLD 173
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 174 ITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQVINDPVSNT 253
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAGT 255
|
....*...
gi 1752086653 254 PLIVPIGR 261
Cdd:PRK10253 256 PLVVPLGR 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-247 |
6.49e-98 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 286.98 E-value: 6.49e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVGRGRFPHQsvmKGW-SKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:COG4604 83 ENHINSRLTVRELVAFGRFPYS---KGRlTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQV 245
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV 239
|
..
gi 1752086653 246 IN 247
Cdd:COG4604 240 EE 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-224 |
1.41e-90 |
|
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: 265.45 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 spivpegitvadlvgrgrfphqsvmkgwskkdyeavaeALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-246 |
5.83e-87 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 258.87 E-value: 5.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKqlakv 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LGLLPQSPIVPEG--ITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ 158
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVkNGQLIAEGAPIEIITADLIKET 238
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRA 234
|
....*...
gi 1752086653 239 FQLDCQVI 246
Cdd:COG1121 235 YGGPVALL 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-258 |
1.98e-84 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 252.73 E-value: 1.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVGRGRFPHQSVmkgwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ-------Q 159
Cdd:COG4559 83 HSSLAFPFTVEEVVALGRAPHGSS----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdgG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETF 239
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....*....
gi 1752086653 240 QLDCQVINDPVSNTPLIVP 258
Cdd:COG4559 238 GADLRVLAHPEGGCPQVLP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-258 |
9.08e-79 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 238.52 E-value: 9.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITV 96
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGRGRFPHQSVmkgwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ------QTDILFLDEPTT 170
Cdd:PRK13548 94 EEVVAMGRAPHGLS----RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 171 YLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQVINDPV 250
Cdd:PRK13548 170 ALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADVLVQPHPE 249
|
....*...
gi 1752086653 251 SNTPLIVP 258
Cdd:PRK13548 250 TGAPLVLP 257
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-224 |
2.84e-72 |
|
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: 220.10 E-value: 2.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMApkqlaKVLGLLPQ 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEG--ITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNkRYGTTIVMVLHDINLSARYADYLFTVkNGQLIAEG 224
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-255 |
4.04e-71 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 219.27 E-value: 4.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQ 244
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMG 250
|
250
....*....|.
gi 1752086653 245 VINDPVSNTPL 255
Cdd:PRK10575 251 ILPHPAGAAPV 261
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-231 |
7.40e-67 |
|
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: 207.18 E-value: 7.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSP---IVpeGITVADLVGRGrfPHQSvmkGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQT 160
Cdd:COG1122 81 FQNPddqLF--APTVEEDVAFG--PENL---GLPREEIRErVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 161 DILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-259 |
4.02e-64 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 205.85 E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQ 244
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
250
....*....|....*
gi 1752086653 245 VINDPVSNTPLIVPI 259
Cdd:PRK09536 242 VGTDPATGAPTVTPL 256
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-237 |
1.92e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 193.73 E-value: 1.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLLPQSPIVPE 92
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrIGMIFQQFNLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 GITVAD--LVGR-GRFP-HQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:COG3638 94 RLSVLTnvLAGRlGRTStWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEiITADLIKE 237
Cdd:COG3638 174 VASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAVLRE 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-219 |
4.25e-60 |
|
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: 189.22 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT--ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSP---IVpeGITVADLVGRGRfphqsVMKGWSKKD-YEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQT 160
Cdd:cd03225 81 FQNPddqFF--GPTVEEEVAFGL-----ENLGLPEEEiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 161 DILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-234 |
2.12e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 188.35 E-value: 2.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVlGLLPQ 86
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI-GYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVgrgRFphQSVMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:COG1131 81 EPALYPDLTVRENL---RF--FARLYGLPRKEARErIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADL 234
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-223 |
1.15e-57 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 183.32 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LGL 83
Cdd:COG1136 11 TKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLrrrhIGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSP-IVPEgITVADLVgrgRFPHqsVMKGWSKK-DYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTD 161
Cdd:COG1136 91 VFQFFnLLPE-LTALENV---ALPL--LLAGVSRKeRRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 162 ILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLsARYADYLFTVKNGQLIAE 223
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVSD 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-220 |
3.43e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 3.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLP 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIVPEGiTVADLVgrgRFPHQSVMKGWskkDYEAVAEALEMMNITE-FADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:COG4619 81 QEPALWGG-TVRDNL---PFPFQLRERKF---DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-224 |
5.34e-57 |
|
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: 181.94 E-value: 5.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 3 THTFETKNIQsgydnKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA---K 79
Cdd:cd03257 8 SVSFPTGGGS-----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLLPQSPI--VPEGITVADLVGRGRFPHQSVMKGWSKKdyEAVAEALEMMNITE-FADRNIDELSGGQRQRVWIAMAL 156
Cdd:cd03257 83 EIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARK--EAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-233 |
1.39e-56 |
|
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: 181.33 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLLP 85
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSpivpeG-----ITVADLVGrgrFP---HqsvmKGWSKKD-YEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:COG1127 89 QG-----GalfdsLTVFENVA---FPlreH----TDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 157 AQQTDILFLDEPTTYLD-ITYQVeILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:COG1127 157 ALDPEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-234 |
1.92e-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: 180.84 E-value: 1.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDN-KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---L 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 82 GLLPQSPIVPEGITVADLVGRGRFPH----QSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADL 234
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-233 |
2.30e-56 |
|
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: 180.39 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGL 83
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGITVADLVG-----RGRFPHQSVMkgwskkdyEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ 158
Cdd:cd03261 82 LFQSGALFDSLTVFENVAfplreHTRLSEEEIR--------EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 159 QTDILFLDEPTTYLD-ITYQVeILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:cd03261 154 DPELLLYDEPTAGLDpIASGV-IDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-240 |
1.36e-55 |
|
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: 178.84 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQS 87
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PivpEGI-----TVADLVG-----RGRFPHQsvmkgwskkdyEAVAEALEMMNIT-EFADRNIDELSGGQRQRVWIAMAL 156
Cdd:COG1124 88 P---YASlhprhTVDRILAeplriHGLPDRE-----------ERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLiaegapIEIITADLIK 236
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI------VEELTVADLL 227
|
....
gi 1752086653 237 ETFQ 240
Cdd:COG1124 228 AGPK 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-242 |
1.02e-54 |
|
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: 183.95 E-value: 1.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKM---APKQLAKVLGLLPQSP---IVP 91
Cdd:COG1123 278 VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPyssLNP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 EgITVADLVGRGrfphQSVMKGWSKKDYEA-VAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:COG1123 358 R-MTVGDIIAEP----LRLHGLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPT 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG-------APIEIITADLIKETFQLD 242
Cdd:COG1123 433 SALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGpteevfaNPQHPYTRALLAAVPSLD 512
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-220 |
5.65e-54 |
|
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: 173.83 E-value: 5.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LGL 83
Cdd:cd03255 7 SKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSP-IVPEgITVADLVgrgRFPhqSVMKGWSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTD 161
Cdd:cd03255 87 VFQSFnLLPD-LTALENV---ELP--LLLAGVPKKERRERAeELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 162 ILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLsARYADYLFTVKNGQL 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-207 |
8.54e-53 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 169.72 E-value: 8.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGksihkmapkqlAKVLGLLPQSPIVPEG 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 --ITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752086653 172 LDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSAR 207
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-224 |
3.25e-52 |
|
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: 169.24 E-value: 3.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQ 86
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:cd03259 80 DYAL--------------FPHLTVaeniafglkLRGVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-234 |
6.12e-52 |
|
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: 169.40 E-value: 6.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LG 82
Cdd:TIGR02315 3 EVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrrIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVPEGITVADLVGRGRFPHQSVMKG----WSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ 158
Cdd:TIGR02315 83 MIFQHYNLIERLTVLENVLHGRLGYKPTWRSllgrFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADL 234
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-232 |
1.04e-51 |
|
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: 175.86 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTG---GDVLLDGKSIHKMAPKQLAKVLGLLPQSP---I 89
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRIGMVFQDPmtqL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 VPegITVADLVGRGrfphqSVMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:COG1123 97 NP--VTVGDQIAEA-----LENLGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-229 |
4.05e-50 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 164.65 E-value: 4.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGLLPQ 86
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVgrgRFpHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:COG4555 82 ERGLYDRLTVRENI---RY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-220 |
1.24e-49 |
|
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: 161.03 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGLLPQ 86
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVgrgrfphqsvmkgwskkdyeavaealemmnitefadrnidELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:cd03230 81 EPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-248 |
1.30e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.81 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKV 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LGLLPQSPivpegitvaDLvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRV 150
Cdd:COG3842 79 VGMVFQDY---------AL-----FPHLTVaenvafglrMRGVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDIN--LSarYADYLFTVKNGQLIAEGAPIE 228
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGTPEE 222
|
250 260
....*....|....*....|....*..
gi 1752086653 229 I-------ITADLIKETFQLDCQVIND 248
Cdd:COG3842 223 IyerpatrFVADFIGEANLLPGTVLGD 249
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-229 |
4.91e-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: 163.01 E-value: 4.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH---KMAPKQLAKVLGLLPQspivpegi 94
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDLRKKVGLVFQ-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 tvadlvgrgrFP-HQ----SVMK---------GWSKKD-YEAVAEALEMMNITE-FADRNIDELSGGQRQRVWIAMALAQ 158
Cdd:TIGR04521 90 ----------FPeHQlfeeTVYKdiafgpknlGLSEEEaEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-231 |
1.88e-48 |
|
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: 160.54 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLP 85
Cdd:cd03295 2 EFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPivpegitvadlvgrGRFPHQSV---------MKGWSKKDYEA-VAEALEMMNI--TEFADRNIDELSGGQRQRVWIA 153
Cdd:cd03295 82 QQI--------------GLFPHMTVeenialvpkLLKWPKEKIRErADELLALVGLdpAEFADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 154 MALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-231 |
2.30e-48 |
|
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: 159.91 E-value: 2.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvLGLLP- 85
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 -QSPIVPEGITVAD------LVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ 158
Cdd:cd03219 81 fQIPRLFPELTVLEnvmvaaQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-230 |
2.61e-48 |
|
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: 159.65 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIK-----PTGGDVLLDGKSIHK--MAPKQLA 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KVLGLLPQSPIVPEGiTVADLVGRGRFPHQSvmkgWSKKDYEA-VAEALEMMNIT-EFADR-NIDELSGGQRQRVWIAMA 155
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGI----KLKEELDErVEEALRKAALWdEVKDRlHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgtTIVMVLHDINLSARYADYLFTVKNGQLIaEGAPIEII 230
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLV-EFGPTEQI 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-258 |
6.42e-48 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 159.99 E-value: 6.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA----RLIKPTG----GDVLLDGKSIHKMAPKQLAKVLGLLPQS 87
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PIVPEGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ--------- 158
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKET 238
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARC 251
|
250 260
....*....|....*....|
gi 1752086653 239 FQLDCQVINDPVSNTPLIVP 258
Cdd:PRK13547 252 YGFAVRLVDAGDGVPPVIVP 271
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-225 |
3.54e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 156.37 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LG-------LLP 85
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrIGvvfqdfrLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QspivpegITVADLVgrgRFPhqsvMK--GWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDI 162
Cdd:COG2884 93 D-------RTVYENV---ALP----LRvtGKSRKEIRRrVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGA 225
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-229 |
8.56e-47 |
|
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: 156.35 E-value: 8.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 19 TILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvLGLLP--QSPIVPEGITV 96
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR-LGIARtfQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 AD--LVGR----GRFPHQSVMKGWSKKDYEA-----VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:COG0411 97 LEnvLVAAharlGRGLLAALLRLPRARREERearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-231 |
8.58e-47 |
|
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: 157.03 E-value: 8.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LGLLPQSpivpegitv 96
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQS--------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 adlvgRGRFPHQSVM---------KGWSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:cd03294 111 -----FALLPHRTVLenvafglevQGVPRAEREERAaEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-242 |
9.68e-47 |
|
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: 156.82 E-value: 9.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDN--KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGksIHKMAPKQLAKV---L 81
Cdd:TIGR04520 2 EVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIrkkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 82 GLLPQSP---IVpeGITVADLVGRG----RFPHQSvMKgwskkdyEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAM 154
Cdd:TIGR04520 80 GMVFQNPdnqFV--GATVEDDVAFGlenlGVPREE-MR-------KRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEIIT-AD 233
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDME-EAVLADRVIVMNKGKIVAEGTPREIFSqVE 228
|
....*....
gi 1752086653 234 LIKEtFQLD 242
Cdd:TIGR04520 229 LLKE-IGLD 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-223 |
1.98e-46 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 154.55 E-value: 1.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 3 THTFETKNIQsgydnKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKqlakvLG 82
Cdd:cd03293 7 SKTYGGGGGA-----VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVpegitvadlvgrgrFPHQSV---------MKGWSKKD-YEAVAEALEMMNITEFADRNIDELSGGQRQRVWI 152
Cdd:cd03293 77 YVFQQDAL--------------LPWLTVldnvalgleLQGVPKAEaRERAEELLELVGLSGFENAYPHQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 153 AMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYAD--YLFTVKNGQLIAE 223
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADrvVVLSARPGRIVAE 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-228 |
2.62e-46 |
|
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: 157.14 E-value: 2.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP---TGGDVLLDGKSIHKMAPKQLAKVLG----LLPQSPI---- 89
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGreiqMIFQDPMtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 -VpegITVADLVGRGRFPHQsvmkGWSKKD-YEAVAEALEMMNITEfADRNID----ELSGGQRQRVWIAMALAQQTDIL 163
Cdd:COG0444 101 pV---MTVGDQIAEPLRIHG----GLSKAEaRERAIELLERVGLPD-PERRLDryphELSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYAD-----YLftvknGQlIAEGAPIE 228
Cdd:COG0444 173 IADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADrvavmYA-----GR-IVEEGPVE 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-219 |
5.74e-46 |
|
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: 151.96 E-value: 5.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMA--PKQLAKVLGL 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVpegitvadlvgrgrFPHQSVMKgwskkdyeavaealemmNITEfadrnidELSGGQRQRVWIAMALAQQTDIL 163
Cdd:cd03229 81 VFQDFAL--------------FPHLTVLE-----------------NIAL-------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-229 |
8.84e-46 |
|
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: 152.97 E-value: 8.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-LGLLP 85
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QspivpegitvadlvGRGRFPHQSVMK----GWSKKDYEAVAEALEMM-----NITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:cd03224 82 E--------------GRRIFPELTVEEnlllGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-202 |
1.16e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.71 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 3 THTFETKNiqsgyDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKqlakvLG 82
Cdd:COG1116 14 SKRFPTGG-----GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWI 152
Cdd:COG1116 84 VVFQEPAL--------------LPWLTVldnvalgleLRGVPKAERRErARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 153 AMALAQQTDILFLDEPTTYLD-ITYQvEILDLLTDLNKRYGTTIVMVLHDI 202
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDaLTRE-RLQDELLRLWQETGKTVLFVTHDV 199
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
16-232 |
1.34e-45 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 154.86 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPivpegit 95
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYVIQQI------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 vadlvgrGRFPHQSV---------MKGWSKKDYEA-VAEALEMMNI--TEFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:COG1125 86 -------GLFPHMTVaeniatvprLLGWDKERIRArVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 164 FLDEPTTYLD-IT---YQVEILDLLTDLNKrygtTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG1125 159 LMDEPFGALDpITreqLQDELLRLQRELGK----TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILAN 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-239 |
5.95e-45 |
|
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: 151.29 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvLGLLpq 86
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR-LGIG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 spIVPEgitvadlvGRGRFPHQSV-----MKGWSKKDYEAVAEALEMM-----NITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:COG0410 82 --YVPE--------GRRIFPSLTVeenllLGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIK 236
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
...
gi 1752086653 237 ETF 239
Cdd:COG0410 231 EAY 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-229 |
2.17e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.92 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ--LAKVlgllPQ 86
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrnIAMV----FQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:COG3839 83 SYAL--------------YPHMTVyeniafplkLRKVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHD----INLsaryADYLFTVKNGQLIAEGAPIEI 229
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-219 |
2.27e-44 |
|
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: 147.01 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 spivpegitvadlvgrgrfphqsvmkgwskkdyeavaealemmnitefadrnideLSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-232 |
4.21e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.99 E-value: 4.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHkMAPKQLAKV---LGL 83
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrkVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSpivpegitvADLvgrgrFPHQSVM----------KGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWI 152
Cdd:COG1126 82 VFQQ---------FNL-----FPHLTVLenvtlapikvKKMSKAEAEERAMElLERVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 153 AMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-226 |
6.56e-44 |
|
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: 156.07 E-value: 6.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiT 95
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAG-T 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVGRGRfPHQSVmkgwskkdyEAVAEALEMMNITEFADR-------NIDE----LSGGQRQRVWIAMALAQQTDILF 164
Cdd:COG4988 427 IRENLRLGR-PDASD---------EELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLsARYADYLFTVKNGQLIAEGAP 226
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDGRIVEQGTH 555
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-232 |
8.24e-44 |
|
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: 148.11 E-value: 8.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLL 84
Cdd:cd03258 8 SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKArrrIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLVGrgrFPHQsvMKGWSKKD-YEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:cd03258 88 FQHFNLLSSRTVFENVA---LPLE--IAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-229 |
2.23e-43 |
|
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: 147.00 E-value: 2.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQ 86
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:cd03300 80 NYAL--------------FPHLTVfeniafglrLKKLPKAEIKErVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-221 |
5.05e-43 |
|
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: 145.09 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQ-SGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHkmaPKQLAKVLGLLP 85
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSP---IVPEgiTVADLVGRGrfphqsvMKGWSkKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDI 162
Cdd:cd03226 78 QDVdyqLFTD--SVREELLLG-------LKELD-AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLI 221
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-201 |
2.23e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.77 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 4 HTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGL 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGITVADLVgrgRFpHQSvMKGwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:COG4133 80 LGHADGLKPELTVRENL---RF-WAA-LYG-LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHD 201
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-170 |
1.04e-41 |
|
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: 140.09 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITVADLV 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 101 GRGRfphqsVMKGWSKKDYEA-VAEALEMMNITEFADRNID----ELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:pfam00005 81 RLGL-----LLKGLSKREKDArAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-224 |
2.04e-41 |
|
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: 141.18 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPsNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMaPKQLAKVLGLLPQSP 88
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVPEGITVADLVGrgrfpHQSVMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:cd03264 82 GVYPNFTVREFLD-----YIAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 168 PTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
36-239 |
3.52e-41 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 141.14 E-value: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihkmaPKQLAKVLGLLPQS-------PIvpegiTVADLVGRGRFPHQ 108
Cdd:TIGR03771 11 LLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRhefawdfPI-----SVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 109 SVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLN 188
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 189 KRyGTTIVMVLHDINLSARYADYLFTVkNGQLIAEGAPIEIITADLIKETF 239
Cdd:TIGR03771 161 GA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTF 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-242 |
4.61e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.06 E-value: 4.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 3 THTFETKNiqsgyDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-- 80
Cdd:COG1135 8 SKTFPTKG-----GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 -LG-------LLPQSpivpegiTVADLVGrgrFPhqsvMK--GWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQR 149
Cdd:COG1135 83 kIGmifqhfnLLSSR-------TVAENVA---LP----LEiaGVPKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLD--ITYQveILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPI 227
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDpeTTRS--ILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250 260
....*....|....*....|..
gi 1752086653 228 EI-------ITADLIKETFQLD 242
Cdd:COG1135 227 DVfanpqseLTRRFLPTVLNDE 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-229 |
8.70e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 143.36 E-value: 8.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGK--SIHkMAPKQLaKVlGLLPQ 86
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTN-LPPRER-RV-GFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPivpegitvaDLvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:COG1118 83 HY---------AL-----FPHMTVaeniafglrVRPPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-233 |
1.41e-40 |
|
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: 148.44 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiT 95
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VAD--LVGRGRFphqsvmkgwskkDYEAVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVWIAMALAQQTDI 162
Cdd:COG2274 565 IREniTLGDPDA------------TDEEIIEAARLAGLHDFIealpmgyDTVVGEggsnLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDinLS-ARYADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR--LStIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-229 |
1.75e-40 |
|
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: 139.18 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGLLPQSPIVPEG 93
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVADLVgrgRFphQSVMKGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYL 172
Cdd:cd03263 90 LTVREHL---RF--YARLKGLPKSEIKEEVELlLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 173 DITYQVEILDLLTDLnkRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:cd03263 165 DPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-219 |
2.74e-40 |
|
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: 137.13 E-value: 2.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKT--ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:cd03228 4 KNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGiTVADlvgrgrfphqsvmkgwskkdyeavaealemmNItefadrnideLSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:cd03228 84 DPFLFSG-TIRE-------------------------------NI----------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINlSARYADYLFTVKNGQ 219
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-229 |
3.33e-40 |
|
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: 138.66 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGLLPQ 86
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVAD-LVGRGRFphQSVmkGWSKKDyEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:cd03265 81 DLSVDDELTGWEnLYIHARL--YGV--PGAERR-ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-229 |
4.09e-40 |
|
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: 140.60 E-value: 4.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGLLPQSPIVPEGI 94
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 T-VADLVGRGRFphqsvmKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYL 172
Cdd:TIGR01188 82 TgRENLEMMGRL------YGLPKDEAEErAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 173 DITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-235 |
6.78e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.96 E-value: 6.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 25 NLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLakvlgllPQSPIVPEG-----ITVADL 99
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER-------PVSMLFQENnlfphLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VGRGRFPHqsvMKgWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVE 179
Cdd:COG3840 92 IGLGLRPG---LK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 180 ILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGApieiiTADLI 235
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP-----TAALL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-242 |
8.20e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.71 E-value: 8.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLL 84
Cdd:PRK11153 8 SKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLVGrgrFPHQsvMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:PRK11153 88 FQHFNLLSSRTVFDNVA---LPLE--LAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI-------ITADLIK 236
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVfshpkhpLTREFIQ 242
|
....*.
gi 1752086653 237 ETFQLD 242
Cdd:PRK11153 243 STLHLD 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-246 |
2.91e-39 |
|
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: 136.75 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPT-GGDVLLDGKSIHKMAPKQLAKVLGLLpqSPI---- 89
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVWELRKRIGLV--SPAlqlr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 VPEGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:COG1119 91 FPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQVI 246
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPVEVE 247
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-259 |
3.38e-39 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 136.51 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIkPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITV---ADLvgrgrfpHQSVmK 112
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVfqyLAL-------HQPA-G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 113 GWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ-------QTDILFLDEPTTYLDITYQVEILDLLT 185
Cdd:COG4138 98 ASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 186 DLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQVINdpVSNTPLIVPI 259
Cdd:COG4138 178 EL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE--VEGHRWLIPT 248
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-210 |
4.12e-39 |
|
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: 135.35 E-value: 4.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSI--HKMAPKQLAKVLGL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSpivpegitvADLvgrgrFPHQSVM----------KGWSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWI 152
Cdd:cd03262 81 VFQQ---------FNL-----FPHLTVLenitlapikvKGMSKAEAEERAlELLEKVGLADKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 153 AMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYAD 210
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVAD 203
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-220 |
1.56e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 134.02 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LG- 82
Cdd:TIGR02211 8 GKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLrnkkLGf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 ------LLPQSPIVpEGITVADLVGrgrfpHQSVmkgwsKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:TIGR02211 88 iyqfhhLLPDFTAL-ENVAMPLLIG-----KKSV-----KEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQL 220
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-246 |
1.15e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.77 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 4 HTFETKNIQSGYD-NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLG 82
Cdd:PRK13652 2 HLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQ-------SPIVPEGITVADL-VGRgrfphqsvmkgwskkDYEAVA----EALEMMNITEFADRNIDELSGGQRQRV 150
Cdd:PRK13652 82 LVFQnpddqifSPTVEQDIAFGPInLGL---------------DEETVAhrvsSALHMLGLEELRDRVPHHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
250
....*....|....*.
gi 1752086653 231 TADLIKETFQLDCQVI 246
Cdd:PRK13652 227 LQPDLLARVHLDLPSL 242
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-242 |
2.32e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.42 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDN--KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGL 83
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSP----IvpeGITVADLVGRG----RFPhQSVMKgwskkdyEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMA 155
Cdd:PRK13632 88 IFQNPdnqfI---GATVEDDIAFGlenkKVP-PKKMK-------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEIITADLI 235
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
....*..
gi 1752086653 236 KETFQLD 242
Cdd:PRK13632 236 LEKAKID 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-229 |
9.07e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 9.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDN--KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KVLGLLPQSP---IVpeGITVADLVGRG----RFPHQSVMkgwskkdyEAVAEALEMMNITEFADRNIDELSGGQRQRVW 151
Cdd:PRK13635 81 RQVGMVFQNPdnqFV--GATVQDDVAFGleniGVPREEMV--------ERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-239 |
1.30e-36 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 130.77 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 19 TILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLakvLGLLPQSPIVPEG--ITV 96
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITY 176
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 177 QVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKnGQLIAEGAPIEIITADLIKETF 239
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-231 |
2.26e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 130.20 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT-ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhKMAPKQLAKV---LG 82
Cdd:PRK13639 3 ETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSP----IVPegiTVADLVGRG----RFPHQSVMKgwskkdyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAM 154
Cdd:PRK13639 82 IVFQNPddqlFAP---TVEEDVAFGplnlGLSKEEVEK--------RVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-230 |
2.74e-36 |
|
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: 128.61 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQspivpegitvadlv 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQ-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 GRGRFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:cd03299 79 NYALFPHMTVykniayglkKRKVDKKEIERkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 171 YLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-226 |
3.04e-36 |
|
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: 128.71 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 19 TILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LGLLPQS-PIVP-- 91
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLrarhVGFVFQSfQLLPtl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 ---EGITV-ADLVGRgrfphqsvmkgwskKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:COG4181 106 talENVMLpLELAGR--------------RDARARARAlLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAP 226
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAA 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-229 |
3.99e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.88 E-value: 3.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKV 80
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LGLLPQSPIVpegitvadlvgrgrFPHQSVMKGWS---KKDYEA-------VAEALEMMNITEFADRNIDELSGGQRQRV 150
Cdd:PRK11607 93 INMMFQSYAL--------------FPHMTVEQNIAfglKQDKLPkaeiasrVNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLDIT----YQVEILDLLtdlnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAP 226
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
...
gi 1752086653 227 IEI 229
Cdd:PRK11607 235 EEI 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-233 |
1.30e-35 |
|
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: 133.35 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 2 TTHTFETKNIQSGYDN--KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAK 79
Cdd:COG4987 330 GGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLLPQSPIVPEGiTVAD--LVGRgrfPHQSvmkgwskkDyEAVAEALEMMNITEFADR-------NIDE----LSGGQ 146
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLREnlRLAR---PDAT--------D-EELWAALERVGLGDWLAAlpdgldtWLGEggrrLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 147 RQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLsARYADYLFTVKNGQLIAEGAP 226
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAG-LERMDRILVLEDGRIVEQGTH 553
|
....*..
gi 1752086653 227 IEIITAD 233
Cdd:COG4987 554 EELLAQN 560
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-232 |
2.35e-35 |
|
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: 132.12 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 11 IQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKS-TLLKTMaRLIKP----TGGDVLLDGKSIHKMAPKQLAKV----L 81
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSERELRRIrgnrI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 82 GLLPQSPIV---PEgITVADLVGRGRFPHQsvmkGWSKKDYEA-VAEALEMMNITEfADRNID----ELSGGQRQRVWIA 153
Cdd:COG4172 95 AMIFQEPMTslnPL-HTIGKQIAEVLRLHR----GLSGAAARArALELLERVGIPD-PERRLDayphQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 154 MALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-220 |
3.30e-35 |
|
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: 125.44 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQ 86
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:cd03301 80 NYAL--------------YPHMTVydniafglkLRKVPKDEIDErVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-231 |
4.98e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 4.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIK--P---TGGDVLLDGKSIH--KMAPKQLA 78
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIYdpDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KVLGLLPQSPiVPegitvadlvgrgrFPHqSV---------MKGWSKKDY--EAVAEALEMMNI-TEFADR---NIDELS 143
Cdd:COG1117 92 RRVGMVFQKP-NP-------------FPK-SIydnvayglrLHGIKSKSEldEIVEESLRKAALwDEVKDRlkkSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 144 GGQRQRVWIAMALAQQTDILFLDEPTTYLDI--TYQVEilDLLTDLNKRYgtTIVMVLHdiNLS--ARYADYLFTVKNGQ 219
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPisTAKIE--ELILELKKDY--TIVIVTH--NMQqaARVSDYTAFFYLGE 230
|
250
....*....|..
gi 1752086653 220 LIAEGAPIEIIT 231
Cdd:COG1117 231 LVEFGPTEQIFT 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-229 |
7.39e-35 |
|
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: 125.14 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLL 84
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLVG-------RGRFPHQSVMKgwskkdyEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:cd03296 80 FQHYALFRHMTVFDNVAfglrvkpRSERPPEAEIR-------AKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-234 |
9.20e-35 |
|
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: 124.56 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-LGLLP 85
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QspivpegitvadlvGRGRFPH-------QSVMKGWSKKDYEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:TIGR03410 82 Q--------------GREIFPRltveenlLTGLAALPRRSRKIPDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADL 234
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-202 |
9.86e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 125.36 E-value: 9.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlAKVL---GLLPQspivpegI 94
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-GVVFqkdALLPW-------L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVADLVGrgrFPHQsvMKGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLD 173
Cdd:COG4525 92 NVLDNVA---FGLR--LRGVPKAERRARAEElLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180
....*....|....*....|....*....
gi 1752086653 174 ITYQVEILDLLTDLNKRYGTTIVMVLHDI 202
Cdd:COG4525 167 ALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-220 |
1.03e-34 |
|
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: 122.71 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiT 95
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADlvgrgrfphqsvmkgwskkdyeavaealemmNItefadrnideLSGGQRQRVWIAMALAQQTDILFLDEPTTYLDIT 175
Cdd:cd03246 92 IAE-------------------------------NI----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752086653 176 YQVEILDLLTDLNKRyGTTIVMVLHDINLSARyADYLFTVKNGQL 220
Cdd:cd03246 131 GERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-229 |
1.13e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.90 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH-KMAPKQLA---KVLGLLPQspivpegitv 96
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKplrKKVGIVFQ---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 adlvgrgrFP-HQ----SVMK---------GWSKKDYEAVA-EALEMMNITE-FADRNIDELSGGQRQRVWIAMALAQQT 160
Cdd:PRK13634 93 --------FPeHQlfeeTVEKdicfgpmnfGVSEEDAKQKArEMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 161 DILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-224 |
2.91e-34 |
|
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: 122.71 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKqlAKVLGLLPQ 86
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVpegitVADLVGRGRFPHQSVMKGwskKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:cd03268 80 APGF-----YPNLTARENLRLLARLLG---IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKrYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-231 |
2.95e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.87 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIK-----PTGGDVLLDGKSIHKMAPKQLAKVL 81
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 82 GLLPQSPIVPEGITVADLVGRGRFPHQSVMkgwSKKDYEA-VAEALEMMNITEFADRNID----ELSGGQRQRVWIAMAL 156
Cdd:PRK14247 85 QMVFQIPNPIPNLSIFENVALGLKLNRLVK---SKKELQErVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRygTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-201 |
3.24e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 129.03 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkmapkqlaKVLGLLPQS 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PIVPEGITVADLVGRGRFPHQSVMK------------------------------GWskkDYEA-VAEALEMMNIT-EFA 135
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAeleeleaklaepdedlerlaelqeefealgGW---EAEArAEEILSGLGFPeEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 136 DRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDItyqvEILDLLTDLNKRYGTTIVMVLHD 201
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-229 |
3.46e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.84 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGksiHKMAPKQLAKVlGLLPQ 86
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRI-GYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 spivpEgitvadlvgRGRFPHQSVM---------KGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:COG4152 79 -----E---------RGLYPKMKVGeqlvylarlKGLSKAEAKRRADEwLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-223 |
5.99e-34 |
|
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: 123.38 E-value: 5.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 3 THTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-- 80
Cdd:TIGR02769 9 THTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 -LGLLPQSPI--VPEGITVADLVGRgRFPHQSVMKGWSKKdyEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:TIGR02769 89 dVQLVFQDSPsaVNPRMTVRQIIGE-PLRHLTSLDESEQK--ARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-231 |
1.49e-33 |
|
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: 124.44 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPT------GGDVLLDGKSIHKMAPKQLAkvLGLLPQSPivpegitv 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlGGEVLQDSARGIFLPPHRRR--IGYVFQEA-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 adlvgrgR-FPHQSV-------MK-GWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:COG4148 87 -------RlFPHLSVrgnllygRKrAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 168 PTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-203 |
2.37e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 123.30 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvlgLLPQSPIV---PEG---- 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP---LRRRMQMVfqdPYAslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 -ITVADLVGrgrFPHQsVMKGWSKKDYEA-VAEALEM--MNiTEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:COG4608 111 rMTVGDIIA---EPLR-IHGLASKAERRErVAELLELvgLR-PEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190
....*....|....*....|....*....|....
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRYGTTIVMVLHDIN 203
Cdd:COG4608 186 SALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-232 |
2.37e-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: 126.72 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIkPTGGDVLLDGKSIHKMAPKQLakvLGLLPQSPIV---PEG---- 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAL---RPLRRRMQVVfqdPFGslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 -ITVADLVGRGRFPHQsvmKGWSKKDYEA-VAEALEMMNIT-EFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:COG4172 378 rMTVGQIIAEGLRVHG---PGLSAAERRArVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 171 YLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-224 |
2.94e-33 |
|
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: 120.08 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhKMAPKQLakvLGLLPQ 86
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR---IGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SpivpegitvadlvgRGRFPHQSVM---------KGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:cd03269 78 E--------------RGLYPKMKVIdqlvylaqlKGLKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-231 |
7.54e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.81 E-value: 7.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHkmAPKqlAKVLGLLPQ 86
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPK--VDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVadlvgrgrFPH----QSVM------KGWSKKDYEAVAEAL-EMMNITEFADRNIDELSGGQRQRVWIAMA 155
Cdd:PRK09493 79 AGMVFQQFYL--------FPHltalENVMfgplrvRGASKEEAEKQARELlAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-220 |
8.22e-33 |
|
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: 119.05 E-value: 8.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTI-LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LG 82
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVPEGITVADLVGrgrFPHQSVMKG---WSKKdyeaVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVA---FALEVTGVPpreIRKR----VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-207 |
1.06e-32 |
|
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: 118.49 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAK----VLGLL 84
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrreKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVAD-----LVGRgrfphqsvmKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:TIGR03608 82 FQNFALIENETVEEnldlgLKYK---------KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSAR 207
Cdd:TIGR03608 153 PPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-237 |
1.24e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.23 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 4 HTFETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLG 82
Cdd:PRK13647 3 NIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSP--IVPEGiTVADLVGRGrfphqSVMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:PRK13647 83 LVFQDPddQVFSS-TVWDDVAFG-----PVNMGLDKDEVERrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKE 237
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-224 |
1.37e-32 |
|
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: 118.55 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIiGANGCGKSTLLKTMARLIKPTGGDVLLDG-------KSIHkMAPKQlaKVLGLLPQSpivpegit 95
Cdd:cd03297 16 KIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN-LPPQQ--RKIGLVFQQ-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 vADLvgrgrFPHQSV-------MKGWS-KKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:cd03297 84 -YAL-----FPHLNVrenlafgLKRKRnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 168 PTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-246 |
1.47e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.36 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ--LA 78
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KVLgllpQSPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQ 148
Cdd:PRK09452 90 TVF----QSYAL--------------FPHMTVfenvafglrMQKTPAAEITPrVMEALRMVQLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 149 RVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIE 228
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
250 260
....*....|....*....|....*
gi 1752086653 229 I-------ITADLIKETFQLDCQVI 246
Cdd:PRK09452 232 IyeepknlFVARFIGEINIFDATVI 256
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-229 |
1.56e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 121.75 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTF-ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaK 79
Cdd:PRK11432 1 MTQKNFvVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLLPQSPIVpegitvadlvgrgrFPHQSV---------MKGWSKKDY-EAVAEALEMMNITEFADRNIDELSGGQRQR 149
Cdd:PRK11432 79 DICMVFQSYAL--------------FPHMSLgenvgyglkMLGVPKEERkQRVKEALELVDLAGFEDRYVDQISGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-224 |
1.85e-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: 117.98 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKqlAKVLGLLPQSPIVPEGITVADLVGR 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 103 GRFPHQSVmkgwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILD 182
Cdd:cd03298 94 GLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752086653 183 LLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-229 |
2.21e-32 |
|
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: 121.06 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQSPIVpegitvadlvgrgrFPHQSV----- 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYAL--------------FPHMTVeenva 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 111 ----MKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLT 185
Cdd:TIGR01187 65 fglkMRKVPRAEIKPrVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752086653 186 DLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-241 |
2.58e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.46 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAP----KQLAKVLGLL---PQSPIVPEg 93
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVfqfPESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 iTVADLVGrgrFPHQSVmkGWSKKDYEAVA-EALEMMNITE-FADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:PRK13649 102 -TVLKDVA---FGPQNF--GVSQEEAEALArEKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 172 LDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQL 241
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQL 244
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-219 |
3.51e-32 |
|
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: 117.35 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLLPQS-PIVPEgIT 95
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrrIGVVFQDfRLLPD-RT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVGrgrFPHQsvMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDI 174
Cdd:TIGR02673 96 VYENVA---LPLE--VRGKKEREIQRrVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752086653 175 TYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:TIGR02673 171 DLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-215 |
4.64e-32 |
|
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: 123.17 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTVADLV 100
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 GRGRfPHQSVmkgwskkdyEAVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:TIGR02857 417 RLAR-PDASD---------AEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752086653 170 TYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSARyADYLFTV 215
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.92e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.18 E-value: 4.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKT-ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPK--QL 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 78 AKVLGLLPQSP-------IVPEGITVADLvgRGRFPHQSVmkgwskkdYEAVAEALEMMNITEFADRNIDELSGGQRQRV 150
Cdd:PRK13636 81 RESVGMVFQDPdnqlfsaSVYQDVSFGAV--NLKLPEDEV--------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-224 |
7.47e-32 |
|
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: 116.92 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTI--LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGL 83
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPI-----VPEGITVADLVGrgrfphqsvmkgwskkDYEAVAEALEMMNITEFA-------DRNIDE----LSGGQR 147
Cdd:cd03245 83 VPQDVTlfygtLRDNITLGAPLA----------------DDERILRAAELAGVTDFVnkhpnglDLQIGErgrgLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 148 QRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSArYADYLFTVKNGQLIAEG 224
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-224 |
1.19e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 117.25 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIK-----PTGGDVLLDGKSIH--KMAPKQLAK 79
Cdd:PRK14267 6 ETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYspDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLLPQSPIVPEGITVADLVGRGrFPHQSVMKGWSKKDyEAVAEALEMMNI-TEFADRNID---ELSGGQRQRVWIAMA 155
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELD-ERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgtTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-220 |
1.71e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 116.70 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPK-----QLAKvlgL 83
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDtrlmfQDAR---L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSpivpegiTVADLVGRGrfphqsvMKG-WSkkdyeavAEALEMMNITEFADRNID---ELSGGQRQRVWIAMALAQQ 159
Cdd:PRK11247 93 LPWK-------KVIDNVGLG-------LKGqWR-------DAALQALAAVGLADRANEwpaALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-224 |
2.47e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.43 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDN-KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPE 92
Cdd:COG1132 348 SYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 GiTVADLVGRGRfPHQSVmkgwskkdyEAVAEALEMMNITEFADR-------NIDE----LSGGQRQRVWIAMALAQQTD 161
Cdd:COG1132 428 G-TIRENIRYGR-PDATD---------EEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 162 ILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHdiNLS-ARYADYLFTVKNGQLIAEG 224
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH--RLStIRNADRILVLDDGRIVEQG 556
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-239 |
2.61e-31 |
|
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: 115.72 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-LGLL 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVAD---LVGRGRfphqsvmkGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMALAQQT 160
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIR--------GLSKKEREEKLEElLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 161 DILFLDEPTTYLD-ITYQvEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETF 239
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQ-DIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-224 |
3.25e-31 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 115.51 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGI 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVADlvgrgRFPHQSVMKGWSKKDY-EAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLD 173
Cdd:cd03267 111 PVID-----SFYLLAAIYDLPPARFkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 174 ITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-223 |
6.73e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.49 E-value: 6.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LGL 83
Cdd:PRK10584 13 KKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQS-PIVP-----EGITVADLVgRGRFPHQSvmkgwskkdYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:PRK10584 93 VFQSfMLIPtlnalENVELPALL-RGESSRQS---------RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQLIAE 223
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-249 |
6.87e-31 |
|
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: 114.49 E-value: 6.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA--KVLGLLPQSpIVPEGITVAd 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPWL-TVRENIALA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 99 lvgrgrfpHQSVMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQ 177
Cdd:TIGR01184 79 --------VDRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 178 VEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGqliaEGAPI-EIITADLIKETFQLDcqVINDP 249
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG----PAANIgQILEVPFPRPRDRLE--VVEDP 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
7.94e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.62 E-value: 7.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGY--DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KVLGLLPQSP---IVpeGITVADLVGRGrFPHQSVMkgwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMA 155
Cdd:PRK13648 83 KHIGIVFQNPdnqFV--GSIVKYDVAFG-LENHAVP---YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-229 |
8.07e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSI--HKMAPKQLAKVLGLLPQSP---IVPE 92
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyqLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 giTVADLVGRGrfphqSVMKGWSKKD-YEAVAEALEMMNIT--EFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:PRK13637 100 --TIEKDIAFG-----PINLGLSEEEiENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-236 |
1.20e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlAKVLG--LLPQSP-IVPEgITVA 97
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAGiaIIHQELnLVPN-LSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 98 DLVGRGRFPHQSVMKGWsKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITyQ 177
Cdd:COG1129 98 ENIFLGREPRRGGLIDW-RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER-E 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 178 VEIL-DLLTDLNKRyGTTIVMVLHDINLSARYADYlFTV-KNGQLIAEGAPIEIITADLIK 236
Cdd:COG1129 176 VERLfRIIRRLKAQ-GVAIIYISHRLDEVFEIADR-VTVlRDGRLVGTGPVAELTEDELVR 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-230 |
1.50e-30 |
|
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: 113.79 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNK---TILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGL 83
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGiTVADLVGRGRFPHQSVMkgwskkdyeaVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVWI 152
Cdd:cd03249 82 VSQEPVLFDG-TIAENIRYGKPDATDEE----------VEEAAKKANIHDFImslpdgyDTLVGErgsqLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 153 AMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHdiNLSA-RYADYLFTVKNGQLIAEGAPIEII 230
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAH--RLSTiRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-229 |
2.17e-30 |
|
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: 115.98 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGK-----------SIHKMApkqlakvLGLLPQSpivp 91
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflPPEKRR-------IGYVFQE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 egitvADLvgrgrFPHQSVMK----GWSKKDYEAV----AEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:TIGR02142 84 -----ARL-----FPHLSVRGnlryGMKRARPSERrisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-223 |
3.50e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.99 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV----LG-- 82
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGfi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 -----LLPQSPIVpEGITVADLVGRgrfphqsvmkgwsKKDYEAVAEALEMMNITEFADRN---IDELSGGQRQRVWIAM 154
Cdd:PRK11629 93 yqfhhLLPDFTAL-ENVAMPLLIGK-------------KKPAEINSRALEMLAAVGLEHRAnhrPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLfTVKNGQLIAE 223
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-247 |
4.90e-30 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 112.72 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIkPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITVADLVGRgrfpHQSVmKGWS 115
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL----HQPD-KTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 116 KKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ-------QTDILFLDEPTTYLDITyQVEILDLLTDLN 188
Cdd:PRK03695 101 EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA-QQAALDRLLSEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 189 KRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETFQLDCQVIN 247
Cdd:PRK03695 180 CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-232 |
7.90e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.45 E-value: 7.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIK------PTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPI 89
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 VPEGITVADLVGrgrFPHQSVMKGWSKKDYEAVAEALEMMNI-TEFADR---NIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:PRK14246 101 PFPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRygTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-223 |
1.03e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.47 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 4 HTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA---KV 80
Cdd:PRK10419 11 HHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LGLLPQSPI--VPEGITVADLVGRgrfP--HqsvMKGWSKKDYEA-VAEALEMMNIT-EFADRNIDELSGGQRQRVWIAM 154
Cdd:PRK10419 91 IQMVFQDSIsaVNPRKTVREIIRE---PlrH---LLSLDKAERLArASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-230 |
1.31e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.75 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILN---------DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAK 79
Cdd:PRK10070 23 KYIEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 V----LGLLPQSPIVPEGITVADLVGRGrfphQSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMA 155
Cdd:PRK10070 103 VrrkkIAMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-262 |
1.67e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.98 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 lGLLPQ-SPIVPEGITVADLVGRGRFPHQSvmkgwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:PRK13537 83 -GVVPQfDNLDPDFTVRENLLVFGRYFGLS-----AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITAdliketf 239
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES------- 228
|
250 260
....*....|....*....|....*..
gi 1752086653 240 QLDCQVI----NDPVSNTPLIVPIGRH 262
Cdd:PRK13537 229 EIGCDVIeiygPDPVALRDELAPLAER 255
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-229 |
1.84e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.10 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMapKQLAKV---LGLLPQSP----- 88
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLWDIrnkAGMVFQNPdnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 --IV-------PEGITVADLVGRGRfphqsvmkgwskkdyeaVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:PRK13633 100 atIVeedvafgPENLGIPPEEIRER-----------------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-201 |
2.76e-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: 115.54 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGL 83
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVpEGITVAD--LVGRGRFPHqsvmkgwskkdyEAVAEALEMMNITEFADRNID-----------ELSGGQRQRV 150
Cdd:TIGR02868 414 CAQDAHL-FDTTVREnlRLARPDATD------------EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHD 201
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-242 |
9.93e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.48 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 10 NIQSGYDNKT-----ILNDVNLSIPSNQISIIIGANGCGKSTLLK-TMARLIKPTGGDVLLDGK---SIHKMAP-KQLAK 79
Cdd:PRK13645 11 NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQlTNGLIISETGQTIVGDYAipaNLKKIKEvKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLLPQspiVPEGITVADLVGRGrFPHQSVMKGWSKKD-YEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:PRK13645 91 EIGLVFQ---FPEYQLFQETIEKD-IAFGPVNLGENKQEaYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKE 237
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
....*
gi 1752086653 238 TFQLD 242
Cdd:PRK13645 247 KIEID 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-221 |
1.82e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLdGKSIHkmapkqlakvLGLLP 85
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIV-PEGITVADlvgrgrfphqsVMKGWSKKDYEAVAEA-LEMMNIT-EFADRNIDELSGGQRQRVWIAMALAQQTDI 162
Cdd:COG0488 385 QHQEElDPDKTVLD-----------ELRDGAPGGTEQEVRGyLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 163 LFLDEPTTYLDItyqvEILDLLTDLNKRYGTTIVMVLHDinlsaRY-----ADYLFTVKNGQLI 221
Cdd:COG0488 454 LLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-232 |
2.03e-28 |
|
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: 113.42 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGY--DNKTILNDVNLSI-PSNQISIIiGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLG 82
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIrPGEKVAII-GRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVPEGiTVADLVGRGRfPHQSvmkgwskkDyEAVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVW 151
Cdd:TIGR03375 543 YVPQDPRLFYG-TLRDNIALGA-PYAD--------D-EEILRAAELAGVTEFVrrhpdglDMQIGErgrsLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDL-VDRIIVMDNGRIVADGPKDQVLE 688
|
.
gi 1752086653 232 A 232
Cdd:TIGR03375 689 A 689
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-236 |
2.43e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGG-----DVLLDGKSIHKMApKQLAKVLGLL---PQSPIVPE 92
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEI-KPVRKKVGVVfqfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 GITVADLVGRGRFphqsvmkGWSKKDYEAVA-EALEMMNIT-EFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:PRK13643 101 TVLKDVAFGPQNF-------GIPKEKAEKIAaEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 171 YLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT-ADLIK 236
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQeVDFLK 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-230 |
3.55e-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: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYD-NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLP 85
Cdd:cd03253 2 EFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 Q-SPIVPEgiTVADLVGRGRFphqsvmkGWSKKDYEAVAEAL----EMMNITEFADRNIDE----LSGGQRQRVWIAMAL 156
Cdd:cd03253 82 QdTVLFND--TIGYNIRYGRP-------DATDEEVIEAAKAAqihdKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHdiNLSARY-ADYLFTVKNGQLIAEGAPIEII 230
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH--RLSTIVnADKIIVLKDGRIVERGTHEELL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-230 |
5.88e-28 |
|
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: 106.93 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT-ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLP 85
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIVPEGiTVADLVGRGRfphqsvmkgwSKKDYEAVAEALEMMNITEFADR-----------NIDELSGGQRQRVWIAM 154
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-237 |
8.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGD---VLLDGKSIHKMAPKQLAKVLGLLPQSP---IVp 91
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREKVGIVFQNPdnqFV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 eGITVADLVGRG----RFPHQSVMKgwskkdyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:PRK13640 99 -GATVGDDVAFGlenrAVPRPEMIK--------IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 168 PTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEIIT-ADLIKE 237
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSkVEMLKE 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-224 |
9.69e-28 |
|
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: 104.70 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYD--NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGL 83
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD-LEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGiTVADLVGRgrfphqsvmkgwskkdyeavaealemmnitefadrnidELSGGQRQRVWIAMALAQQTDIL 163
Cdd:cd03247 80 LNQRPYLFDT-TLRNNLGR--------------------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDInLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-223 |
1.07e-27 |
|
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: 104.05 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlAKVLGLlp 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 qspivpegitvadlvgrgRFPHQsvmkgwskkdyeavaealemmnitefadrnideLSGGQRQRVWIAMALAQQTDILFL 165
Cdd:cd03216 78 ------------------AMVYQ---------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYlFTV-KNGQLIAE 223
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADR-VTVlRDGRVVGT 163
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-203 |
2.27e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.87 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP---TGGDVLLDGKSIHKMAPKQlaKVLGLLP 85
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIVpegitvadlvgrgrFPHQSV-----------MKGWSKKDyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAM 154
Cdd:COG4136 83 QDDLL--------------FPHLSVgenlafalpptIGRAQRRA--RVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDIN 203
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-229 |
3.28e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.81 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQSP 88
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVPEGITVADLVGRGrfphqsvMK--GWSKKD-YEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:PRK11000 85 ALYPHLSVAENMSFG-------LKlaGAKKEEiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLfTVKNGQLIAE-GAPIEI 229
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKI-VVLDAGRVAQvGKPLEL 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-224 |
3.65e-27 |
|
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: 104.37 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmAPKQLAKVLGLLPQSPIVPEGITVADLV 100
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 GR-GRFpHQsvMKGWSKKDyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVE 179
Cdd:cd03266 100 EYfAGL-YG--LKGDELTA--RLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752086653 180 ILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03266 175 LREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-254 |
3.95e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT-----ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLL-DGKSIHKMAP------ 74
Cdd:PRK13631 23 RVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNhelitn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 75 ---------KQLAKVLGLLPQspiVPEGITVADLVgrgrfpHQSVMKG---WSKKDYEAVAEA---LEMMNITE-FADRN 138
Cdd:PRK13631 103 pyskkiknfKELRRRVSMVFQ---FPEYQLFKDTI------EKDIMFGpvaLGVKKSEAKKLAkfyLNKMGLDDsYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 139 IDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDlNKRYGTTIVMVLHDINLSARYADYLFTVKNG 218
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1752086653 219 QLIAEGAPIEIITADLIKETFQLD----CQVINDPVSNTP 254
Cdd:PRK13631 253 KILKTGTPYEIFTDQHIINSTSIQvprvIQVINDLIKKDP 292
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-229 |
4.21e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 2 TTHTFETKNIQSGYD---NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA 78
Cdd:PRK13650 1 MSNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KVLGLLPQSP---IVpeGITVADLVGRGR----FPHQSvMKgwskkdyEAVAEALEMMNITEFADRNIDELSGGQRQRVW 151
Cdd:PRK13650 81 HKIGMVFQNPdnqFV--GATVEDDVAFGLenkgIPHEE-MK-------ERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSArYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-229 |
5.25e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQ 86
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVG-------RGRFPHQSVMKgwsKKdyeaVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:PRK10851 82 HYALFRHMTVFDNIAfgltvlpRRERPNAAAIK---AK----VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-224 |
6.99e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKS------IHKMAPKQLAKV 80
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LGLLPQSpivpegitvadlvgRGRFPHQSVMK----------GWSKKdyEAVAEA---LEMMNITEFADRNIDELSGGQR 147
Cdd:COG4161 84 VGMVFQQ--------------YNLWPHLTVMEnlieapckvlGLSKE--QAREKAmklLARLRLTDKADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 148 QRVWIAMALAQQTDILFLDEPTTYLD--ITYQ-VEILDLLTDLnkryGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDpeITAQvVEIIRELSQT----GITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-200 |
7.70e-27 |
|
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: 103.89 E-value: 7.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLI---KPTGGDVLLDGKsihKMAPKQLAKVLGLLPQSPIVPEGITV 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 AD-LVGRGRFPHQSVMKGwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDIT 175
Cdd:cd03234 99 REtLTYTAILRLPRKSSD-AIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....*
gi 1752086653 176 YQVEILDLLTDLNKRyGTTIVMVLH 200
Cdd:cd03234 178 TALNLVSTLSQLARR-NRIVILTIH 201
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-230 |
8.44e-27 |
|
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: 108.68 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTV 96
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVgrGRFPhqsvmkgwsKKDYEAVAEALEMMNITEFADR-------NIDE----LSGGQRQRVWIAMALAQQTDILFL 165
Cdd:COG4618 423 AENI--ARFG---------DADPEKVVAAAKLAGVHEMILRlpdgydtRIGEggarLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLsARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSL-LAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-238 |
1.73e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.70 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARL--IKP---TGGDVLLDGKSIHkmAPK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIY--SPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 76 ----QLAKVLGLLPQSPiVPEGITVADLVGRG-RfphqsvMKGWSKKDY--EAVAEALEMMNI-TEFADRNIDE---LSG 144
Cdd:PRK14239 79 tdtvDLRKEIGMVFQQP-NPFPMSIYENVVYGlR------LKGIKDKQVldEAVEKSLKGASIwDEVKDRLHDSalgLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 145 GQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgtTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
250
....*....|....
gi 1752086653 225 APIEIITADLIKET 238
Cdd:PRK14239 230 DTKQMFMNPKHKET 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-229 |
2.03e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.53 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 22 NDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvLGL--------LPQSPIVPEG 93
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVvrtfqhvrLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVAD--LVGRGRFPHQSVMKGWSKKDYEAVAEA---LEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:PRK11300 101 LLVAQhqQLKTGLFSGLLKTPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
15-220 |
2.10e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 102.25 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQSPIVPEGI 94
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVADLVGRGRFPHQSVmkgwSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDI 174
Cdd:TIGR01277 86 TVRQNIGLGLHPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752086653 175 TYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-230 |
2.77e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.80 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 4 HTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-LG 82
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVPEGITVADLVgrgrfphQSV--MKGWSKKDYEAVAEAL-EMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:COG1137 82 YLPQEASIFRKLTVEDNI-------LAVleLRKLSKKEREERLEELlEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 160 TDILFLDE------PTTYLDItyQVEILDL--------LTDLNKRYGTTIVmvlhdinlsaryaDYLFTVKNGQLIAEGA 225
Cdd:COG1137 155 PKFILLDEpfagvdPIAVADI--QKIIRHLkergigvlITDHNVRETLGIC-------------DRAYIISEGKVLAEGT 219
|
....*
gi 1752086653 226 PIEII 230
Cdd:COG1137 220 PEEIL 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-224 |
3.58e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSI---HKMAPKQLAKV- 80
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 --LGLLPQSpivpegitvadlvgRGRFPHQSVMK----------GWSKKdyEAVAEALEMMN---ITEFADRNIDELSGG 145
Cdd:PRK11124 82 rnVGMVFQQ--------------YNLWPHLTVQQnlieapcrvlGLSKD--QALARAEKLLErlrLKPYADRFPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 146 QRQRVWIAMALAQQTDILFLDEPTTYLD--ITYQveILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDpeITAQ--IVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
.
gi 1752086653 224 G 224
Cdd:PRK11124 223 G 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-230 |
3.68e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.01 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT-----ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH-KMAPKQLAKV 80
Cdd:PRK13651 4 KVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKnKKKTKEKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LG-LLPQSPIVPEGITVADLvgRGR------FPH-----QSVMK---------GWSKKD-YEAVAEALEMMNITE-FADR 137
Cdd:PRK13651 84 LEkLVIQKTRFKKIKKIKEI--RRRvgvvfqFAEyqlfeQTIEKdiifgpvsmGVSKEEaKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 138 NIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKN 217
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|...
gi 1752086653 218 GQLIAEGAPIEII 230
Cdd:PRK13651 241 GKIIKDGDTYDIL 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-202 |
3.75e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.86 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 10 NIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHkmAPKQLAKVL----GLLP 85
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGVVfqneGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSpivpegiTVADLVGRGRfphqsVMKGWSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:PRK11248 84 WR-------NVQDNVAFGL-----QLAGVEKMQRLEIAhQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDI 202
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-224 |
4.48e-26 |
|
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: 101.92 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT--ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:cd03251 2 EFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGiTVADLVGRGRFphqsvmkgwsKKDYEAVAEALEMMNITEFADR-------NIDE----LSGGQRQRVWIA 153
Cdd:cd03251 82 SQDVFLFND-TVAENIAYGRP----------GATREEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 154 MALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgTTIVmVLHdiNLSA-RYADYLFTVKNGQLIAEG 224
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAH--RLSTiENADRIVVLEDGKIVERG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-230 |
4.62e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 2 TTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARL--IKPTG---GDVLLDGKSIH--KMAP 74
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLYapDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 75 KQLAKVLGLLPQSPiVPEGITVADLVGRGrfPHQSVMKGwsKKDyEAVAEALEMMNI-TEFADR---NIDELSGGQRQRV 150
Cdd:PRK14243 87 VEVRRRIGMVFQKP-NPFPKSIYDNIAYG--ARINGYKG--DMD-ELVERSLRQAALwDEVKDKlkqSGLSLSGGQQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgtTIVMVLHDINLSARYADY--LFTVK-------NGQLI 221
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMtaFFNVEltegggrYGYLV 238
|
....*....
gi 1752086653 222 aEGAPIEII 230
Cdd:PRK14243 239 -EFDRTEKI 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-200 |
4.79e-26 |
|
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: 100.70 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYdNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA--RLIKPTGGDVLLDGKSIHKMAPKqlaKVLG 82
Cdd:cd03213 10 TVTVKSSPSKS-GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSFR---KIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVpegitvadlvgrgrFPHQSVmkgwskkdYEAVAEALEMMNItefadrnidelSGGQRQRVWIAMALAQQTDI 162
Cdd:cd03213 86 YVPQDDIL--------------HPTLTV--------RETLMFAAKLRGL-----------SGGERKRVSIALELVSNPSL 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLH 200
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-262 |
5.61e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMApkQLAKV 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 -LGLLPQSPIVPEGITV-ADLVGRGRFphqsvmKGWSKKDYEAVAEAL-EMMNITEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:PRK13536 115 rIGVVPQFDNLDLEFTVrENLLVFGRY------FGMSTREIEAVIPSLlEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPieiitADLIKE 237
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP-----HALIDE 262
|
250 260
....*....|....*....|....*....
gi 1752086653 238 tfQLDCQVIN----DPVSNTPLIVPIGRH 262
Cdd:PRK13536 263 --HIGCQVIEiyggDPHELSSLVKPYARR 289
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-203 |
7.88e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 103.24 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMApKQLAKVLGL----------- 83
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGVvfgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPqspivpegitVAD---LVGRgrfphqsvMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:COG4586 111 LP----------AIDsfrLLKA--------IYRIPDAEYKKrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDIN 203
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-174 |
1.65e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA--RLIKPTGGDVLLDGKSIHKMAPKQLAKV-LGL 83
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARAgIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGITVADL----VGRGRFPHQSVMKgwSKKDYEAVAEALEMMNitEFADRNIDE-LSGGQRQRVWIAMALAQ 158
Cdd:COG0396 82 AFQYPVEIPGVSVSNFlrtaLNARRGEELSARE--FLKLLKEKMKELGLDE--DFLDRYVNEgFSGGEKKRNEILQMLLL 157
|
170
....*....|....*.
gi 1752086653 159 QTDILFLDEPTTYLDI 174
Cdd:COG0396 158 EPKLAILDETDSGLDI 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-229 |
1.96e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.50 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETkniQSGydNKTILNDVNLSIPSNQISIIIGANGCGKS-TLLKTMARLIKP--TGGDVLLDGKSIHKMAPKQLAKV- 80
Cdd:PRK09473 21 TFST---PDG--DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 ---LGLLPQSPIV---PEgITVADLVGRGRFPHqsvmKGWSKKdyEAVAEALEMMNITEF--ADRNID----ELSGGQRQ 148
Cdd:PRK09473 96 aeqISMIFQDPMTslnPY-MRVGEQLMEVLMLH----KGMSKA--EAFEESVRMLDAVKMpeARKRMKmyphEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 149 RVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIE 228
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
.
gi 1752086653 229 I 229
Cdd:PRK09473 249 V 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-229 |
3.04e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.94 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKT---ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLG 82
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVP-EGITVADLVGRGR----FPHQSVMKgwskkdyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDVAFGMenqgIPREEMIK--------RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-232 |
3.86e-25 |
|
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: 103.58 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTV 96
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGR-GRFPHqsvmkgwSKKDYEA--VAEALEM-MNITEFADRNIDE----LSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:TIGR01842 409 AENIARfGENAD-------PEKIIEAakLAGVHELiLRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRYGTTIVmVLHDINLSARyADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGC-VDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-203 |
4.13e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.40 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVpEGIT 95
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL-FGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVgrgRFPHQSVMKgwsKKDYEAVAEALEMMNITE-FADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDI 174
Cdd:PRK10247 97 VYDNL---IFPWQIRNQ---QPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*....
gi 1752086653 175 TYQVEILDLLTDLNKRYGTTIVMVLHDIN 203
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-229 |
9.79e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.31 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH--KMAPKQLAKVLGLLPQSPivPE 92
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQDP--EQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 GITVADLVGRGRFPHQSVmkGWSKKDY-EAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNL--GVPEAEItRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 172 LDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-232 |
1.10e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 12 QSGYDNKTILNDVNLSIPSNQiSI-IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkMAPkqlakVLGLlpQSPIV 90
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSA-----LLEL--GAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 91 PEgITVAD---LVGRgrfphqsvMKGWSKKDYEAVAEAlemmnITEFAD--RNIDE----LSGGQRQRVWIAMALAQQTD 161
Cdd:COG1134 101 PE-LTGREniyLNGR--------LLGLSRKEIDEKFDE-----IVEFAElgDFIDQpvktYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 162 ILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-237 |
1.18e-24 |
|
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: 97.21 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARL--IKPTGGDVLLDGKSIHKMAPKQLAKV-LGL 83
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLgIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGITVADLVgrgrfphqsvmkgwskkdyeavaealemmnitefadRNIDE-LSGGQRQRVWIAMALAQQTDI 162
Cdd:cd03217 82 AFQYPPEIPGVKNADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLsARY--ADYLFTVKNGQLIAEGaPIEIitADLIKE 237
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRL-LDYikPDRVHVLYDGRIVKSG-DKEL--ALEIEK 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-223 |
1.76e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPI------ 89
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMmgtaps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 --VPEGITVADLVGRGRfphqSVMKGWSKKDYEAVAEALEMMNItEFADR---NIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:COG1101 97 mtIEENLALAYRRGKRR----GLRRGLTKKRRELFRELLATLGL-GLENRldtKVGLLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-231 |
2.00e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH----KMAPKQLAKVLGLLPQSPIVP--EGI 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPEAQlfENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVADL-VGRGRFphqsvmkGWSKKdyEAVAEALEMMN----ITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:PRK13641 103 VLKDVeFGPKNF-------GFSED--EAKEKALKWLKkvglSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 170 TYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-238 |
2.31e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.63 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 10 NIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARL-IKPTG----GDVLLDGKSIHKMAPK-QLAKVLGL 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIFNYRDVlEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPiVPEGITVADLVGRGRFPHQSVmkgwSKKDYEAVAEA--LEMMNITEFADRNID---ELSGGQRQRVWIAMALAQ 158
Cdd:PRK14271 106 LFQRP-NPFPMSIMDNVLAGVRAHKLV----PRKEFRGVAQArlTEVGLWDAVKDRLSDspfRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgtTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKET 238
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-231 |
3.68e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTG-----GDVLLDGKSIH--KMAPKQLAK 79
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYerRVNLNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLL-PQSPIVPegITVADLVGRGrfphqSVMKGWSKKdyeavaeaLEMMNITEFADRNID--------------ELSG 144
Cdd:PRK14258 89 QVSMVhPKPNLFP--MSVYDNVAYG-----VKIVGWRPK--------LEIDDIVESALKDADlwdeikhkihksalDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 145 GQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKN-----GQ 219
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250
....*....|..
gi 1752086653 220 LIAEGAPIEIIT 231
Cdd:PRK14258 234 LVEFGLTKKIFN 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-224 |
4.74e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTV 96
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGRG--RFPHQSVMkgwskkdyeAVAEALEMMN-ITEFA---DRNIDE----LSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:TIGR00958 572 RENIAYGltDTPDEEIM---------AAAKAANAHDfIMEFPngyDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 167 EPTTYLDityqVEILDLLTDLNKRYGTTIVMVLHDINLsARYADYLFTVKNGQLIAEG 224
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRASRTVLLIAHRLST-VERADQILVLKKGSVVEMG 695
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-233 |
4.83e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 100.56 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGY--DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:TIGR02203 332 EFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGiTVADLVGRGRfPHQSVMkgwskkdyEAVAEALEMMNITEFADR-----------NIDELSGGQRQRVWIA 153
Cdd:TIGR02203 412 SQDVVLFND-TIANNIAYGR-TEQADR--------AEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 154 MALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-225 |
4.83e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLI---KPTGGDVLLDGKSIHKMApkQLAKVL-------GLLPQSPIV 90
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREG--RLARDIrksrantGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 91 PEGITVAD--LVGR-GRFPH-QSVMKGWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:PRK09984 98 VNRLSVLEnvLIGAlGSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGA 225
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-200 |
6.09e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLdgksihkmaPkQLAKVLgLLPQSPIVPEGiT 95
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------P-AGARVL-FLPQRPYLPLG-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVgrgRFPHQSvmkgwSKKDYEAVAEALEMMNITEFADRnIDE-------LSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:COG4178 442 LREAL---LYPATA-----EAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|..
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKryGTTIVMVLH 200
Cdd:COG4178 513 TSALDEENEAALYQLLREELP--GTTVISVGH 542
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-219 |
1.04e-23 |
|
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: 93.28 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihkmapkqlakVLGLLPQsp 88
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 ivpegitvadlvgrgrfphqsvmkgwskkdyeavaealemmnitefadrnideLSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 169 TTYLDItyqvEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:cd03221 98 TNHLDL----ESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-224 |
1.40e-23 |
|
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: 94.91 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkmapkqLAKVLGLlpQSPIVPEg 93
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLGL--GGGFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVAD---LVGRgrfphqsvMKGWSKKD-YEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:cd03220 99 LTGREniyLNGR--------LLGLSRKEiDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
36-231 |
1.93e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.03 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlaKVLGLLPQSPIVPEGITVADLVGRGRFPHQSVmkgwS 115
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIGLGLNPGLKL----N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 116 KKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTI 195
Cdd:PRK10771 104 AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752086653 196 VMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:PRK10771 184 LMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-229 |
2.10e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.60 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQL---AKVLGLLPQSPIVPEG 93
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVADLVG-----RGRFP----HQSVMKgwskkdyeavaeALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:PRK11831 99 MNVFDNVAyplreHTQLPapllHSTVMM------------KLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 165 LDEPTTYLD-ITYQVeILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK11831 167 FDEPFVGQDpITMGV-LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-230 |
7.07e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.50 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 12 QSGYdNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVP 91
Cdd:TIGR01193 482 SYGY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 EGiTVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNI---TEFADRNIDeLSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:TIGR01193 561 SG-SILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRygtTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEII 230
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-220 |
7.67e-23 |
|
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: 93.30 E-value: 7.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTVADL 99
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 V--GRGRFPHQSVMkgwskkdyEAVAEALEMMNITEFA---DRNIDE----LSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:cd03248 108 IayGLQSCSFECVK--------EAAQKAHAHSFISELAsgyDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752086653 171 YLDITYQVEILDLLTDLNKRygTTIVMVLHDINLSARyADYLFTVKNGQL 220
Cdd:cd03248 180 ALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-229 |
7.81e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKT-ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ--LAKV----- 80
Cdd:PRK11650 7 QAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdIAMVfqnya 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 LgllpqspivpegitvadlvgrgrFPHQSV---M------KGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRV 150
Cdd:PRK11650 87 L-----------------------YPHMSVrenMayglkiRGMPKAEIEErVAEAARILELEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 151 wiAM--ALAQQTDILFLDEPTTYLD----ITYQVEILdlltDLNKRYGTTIVMVLHDiNLSA-RYADYLFTVKNGQLIAE 223
Cdd:PRK11650 144 --AMgrAIVREPAVFLFDEPLSNLDaklrVQMRLEIQ----RLHRRLKTTSLYVTHD-QVEAmTLADRVVVMNGGVAEQI 216
|
....*.
gi 1752086653 224 GAPIEI 229
Cdd:PRK11650 217 GTPVEV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-219 |
8.13e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKS-TLLKTMARLIKP----TGGDVLLDGKSIHKMAPKQLAKVLG----LLPQSP 88
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVpeGITVADLVGRGRFPHQSVMKGWSKKdyEAVAEA---LEMMNITEFADRNID---ELSGGQRQRVWIAMALAQQTDI 162
Cdd:PRK15134 102 MV--SLNPLHTLEKQLYEVLSLHRGMRRE--AARGEIlncLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-229 |
8.14e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.46 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSI-HKMAPK---QLAKVLGLLPQspiVPEGITV 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKyirPVRKRIGMVFQ---FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGRGRF--PHQSVMKGWSKKDYeavaeALEMMNITEFAdRNIDELS-----GGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:PRK13646 100 EDTVEREIIfgPKNFKMNLDEVKNY-----AHRLLMDLGFS-RDVMSQSpfqmsGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEI 229
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-232 |
1.23e-22 |
|
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: 92.93 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:cd03252 2 TFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGiTVADLVGRGRfphqsvmkgwSKKDYEAVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVWIA 153
Cdd:cd03252 82 LQENVLFNR-SIRDNIALAD----------PGMSMERVIEAAKLAGAHDFIselpegyDTIVGEqgagLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 154 MALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-227 |
1.83e-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: 96.62 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhKMAPKQLAKVLGLLPQSPIVPEGITVADLV 100
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 grgRFPHQSVMKGWSKKDYEAVAeALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEI 180
Cdd:TIGR01257 1025 ---LFYAQLKGRSWEEAQLEMEA-MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752086653 181 LDLLtdLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPI 227
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-210 |
2.05e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.26 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLlktmARLI----KPTGGDVLLDGKSIHKMAP---KQLAKVLGLLPQSP----- 88
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL----ARLLtmieTPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPygsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 -------IVPEGITV-ADLvgrgrfphqsvmkgwSKKdyEAVAEALEMMNI----TEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:PRK11308 107 prkkvgqILEEPLLInTSL---------------SAA--ERREKALAMMAKvglrPEHYDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYAD 210
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIAD 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-236 |
2.22e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 -LGLLPQSPIVPEGITVADLVGRGRFPHQSVMkGWSKKDYEAVAEALEMMNITEFADRNIDE----LSGGQRQRVWIAMA 155
Cdd:PRK09700 81 gIGIIYQELSVIDELTVLENLYIGRHLTKKVC-GVNIIDWREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 156 LAQQTDILFLDEPTTYLdITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLI 235
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
.
gi 1752086653 236 K 236
Cdd:PRK09700 239 R 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-212 |
4.18e-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: 91.70 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 27 SIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhkmAPKqlakvlgllPQSPIVPEGITVADLVgrgrfp 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYK---------PQYIKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 107 hQSVMKGWSKKDYEAVaEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDityqVEILDLLTD 186
Cdd:cd03237 83 -SSITKDFYTHPYFKT-EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|
gi 1752086653 187 LNKRYG----TTIVMVLHDINLsaryADYL 212
Cdd:cd03237 157 VIRRFAenneKTAFVVEHDIIM----IDYL 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-230 |
7.73e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKS----TLLKTMARLIKPTGGDVLLDGKSIhkmAPKQL--AKVLGLL--PQSPIVPEgI 94
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALrgRKIATIMqnPRSAFNPL-H 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVAD-----LVGRGRFPHQSVMKgwskkdyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:PRK10418 97 TMHTharetCLALGKPADDATLT--------AALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 170 TYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIaEGAPIEII 230
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV-EQGDVETL 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-218 |
8.76e-22 |
|
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: 90.08 E-value: 8.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMArlikptggdvlldgksihkmapKQLAKVLGLLPQSPIVPEGITVADLV 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL----------------------GEMQTLEGKVHWSNKNESEPSFEATR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 GRGRFP-HQSVMKGW----------------SKKDYEAVAEA---------LEMMNITEFADRNIDeLSGGQRQRVWIAM 154
Cdd:cd03290 75 SRNRYSvAYAAQKPWllnatveenitfgspfNKQRYKAVTDAcslqpdidlLPFGDQTEIGERGIN-LSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 155 ALAQQTDILFLDEPTTYLDI-----TYQVEILDLLTDlNKRygtTIVMVLHDINLSArYADYLFTVKNG 218
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQD-DKR---TLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-237 |
1.07e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 90.86 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA--RLIKPTGGDVLLDGKSIHKMAPKQLA 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 79 KvLG--LLPQSPIVPEGITVADLVgrgRFPHQSVMKGWSKKD------YEAVAEALEMMNITE-FADRNIDE-LSGGQRQ 148
Cdd:CHL00131 83 H-LGifLAFQYPIEIPGVSNADFL---RLAYNSKRKFQGLPEldplefLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 149 RVWI-AMALAqQTDILFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLsARY--ADYLFTVKNGQLIAEGa 225
Cdd:CHL00131 159 RNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRL-LDYikPDYVHVMQNGKIIKTG- 234
|
250
....*....|..
gi 1752086653 226 pieiiTADLIKE 237
Cdd:CHL00131 235 -----DAELAKE 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-228 |
1.25e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.64 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNI----QSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV-- 80
Cdd:PRK10535 6 ELKDIrrsyPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 --LGLLPQSPIVPEGITVADLVgrgRFPhqSVMKGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMALA 157
Cdd:PRK10535 86 ehFGFIFQRYHLLSHLTAAQNV---EVP--AVYAGLERKQRLLRAQElLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIE 228
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
5-224 |
1.31e-21 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 93.65 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:TIGR01846 457 TFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVV 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGiTVADLVGRGRfPHQSVmkgwskkdyEAVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVWIA 153
Cdd:TIGR01846 537 LQENVLFSR-SIRDNIALCN-PGAPF---------EHVIHAAKLAGAHDFIselpqgyNTEVGEkganLSGGQRQRIAIA 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 154 MALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINlSARYADYLFTVKNGQLIAEG 224
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESG 673
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-224 |
6.33e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.65 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGG-----DVLLDG-KSI--HKMAPKQ 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLsqQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 77 LAKVLGLLPQSpivpegitvadlvgRGRFPHQSVM----------KGWSKKDYEAVA-EALEMMNITEFADRNIDELSGG 145
Cdd:PRK11264 83 LRQHVGFVFQN--------------FNLFPHRTVLeniiegpvivKGEPKEEATARArELLAKVGLAGKETSYPRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 146 QRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDL--NKRygtTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
.
gi 1752086653 224 G 224
Cdd:PRK11264 226 G 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-226 |
9.46e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.25 E-value: 9.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihkmapkqlakVLGLLPQS- 87
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-----------RIGYVPQKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 ---PIVPegITVadlvgrGRFphQSVMKGWSKKDyeaVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:PRK09544 77 yldTTLP--LTV------NRF--LRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVkNGQLIAEGAP 226
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTP 204
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
7-224 |
1.04e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 91.16 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYD--NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:TIGR03796 479 ELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQ----------------SPIVPEgitvADLVGRGRFP--HQSVMkgwSKKD-YEA-VAEAlemmnitefaDRNideLSG 144
Cdd:TIGR03796 559 DQdiflfegtvrdnltlwDPTIPD----ADLVRACKDAaiHDVIT---SRPGgYDAeLAEG----------GAN---LSG 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 145 GQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLtdlnKRYGTTIVMVLHdiNLSA-RYADYLFTVKNGQLIAE 223
Cdd:TIGR03796 619 GQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAH--RLSTiRDCDEIIVLERGKVVQR 692
|
.
gi 1752086653 224 G 224
Cdd:TIGR03796 693 G 693
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-232 |
1.05e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.42 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 24 VNLSIPSNQISIIIGANGCGKSTLLKTMARLI----KPTGGDVLLDGKSIHKMAPKQLAKVLG----LLPQSPIVpeGIT 95
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPMT--SLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVGRGRFPHQSVMKGWSKKD-YEAVAEALEMMNITEFADRnID----ELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHQGGNKKTrRQRAIDLLNQVGIPDPASR-LDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 171 YLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
33-232 |
1.37e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.93 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 33 ISIIiGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhKMAP-----------KQLAKV---LGLLPQSpivpegitvad 98
Cdd:COG4598 37 ISII-GSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPdrdgelvpadrRQLQRIrtrLGMVFQS----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 99 lvgrgrF---PHQSVM----------KGWSKKDYEAVAEA-LEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:COG4598 104 ------FnlwSHMTVLenvieapvhvLGRPKAEAIERAEAlLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:COG4598 178 FDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-239 |
1.49e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLA-KVLGL 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGITVADLVgrgrFPHQSVMKGWSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDI 162
Cdd:PRK10895 83 LPQEASIFRRLSVYDNL----MAVLQIRDDLSAEQREDRAnELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 163 LFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLIKETF 239
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-224 |
1.59e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIkPTGGDVLLDGKSIHKMAPKQL------AKVLGLLPQSPI 89
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvrhrIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 VPEgITVADLVGRGRFPHQSVMKGWSKKdyEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:PRK15134 376 NPR-LNVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-234 |
1.99e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-LAKVLGLLPQSPIVPEGITVADL 99
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VGRGRFPHQSVMKGWSKkdyeAVAEALEMMNITEFA---DRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLdiTY 176
Cdd:COG3845 101 IVLGLEPTKGGRLDRKA----ARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 177 QvEILDLLTDLN--KRYGTTIVMVLHDINLSARYADYLfTV-KNGQLIAEGAPIEIITADL 234
Cdd:COG3845 175 Q-EADELFEILRrlAAEGKSIIFITHKLREVMAIADRV-TVlRRGKVVGTVDTAETSEEEL 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-232 |
2.98e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.91 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDV-----LLDGKS-----IHKMAPKQLAKVLG----LLPQSP 88
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSrqvieLSEQSAAQMRHVRGadmaMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVPEG--ITVADLVGRGRFPHQsvmkGWSKKdyEAVAEALEMMNITEFAD------RNIDELSGGQRQRVWIAMALAQQT 160
Cdd:PRK10261 114 MTSLNpvFTVGEQIAESIRLHQ----GASRE--EAMVEAKRMLDQVRIPEaqtilsRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 161 DILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-219 |
4.44e-20 |
|
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: 85.21 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 12 QSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkmapkqlakvLGLLPQSPIVP 91
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 EGiTVAD--LVGrgrfphqsvmKGWSKKDYEAVAEA------LEMMN---ITEFADRNIDeLSGGQRQRVWIAMALAQQT 160
Cdd:cd03250 79 NG-TIREniLFG----------KPFDEERYEKVIKAcalepdLEILPdgdLTEIGEKGIN-LSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 161 DILFLDEPTTYLDItyQVE--ILD--LLTDLNKryGTTIVMVLHDINLsARYADYLFTVKNGQ 219
Cdd:cd03250 147 DIYLLDDPLSAVDA--HVGrhIFEncILGLLLN--NKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-229 |
4.66e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.56 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH---------K 71
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 72 MAPKQ----LAKVLGLLPQSPIVPEGITVADLVGRGrfPHQSVmkGWSKKD-YEAVAEALEMMNITEFA-DRNIDELSGG 145
Cdd:PRK10619 81 VADKNqlrlLRTRLTMVFQHFNLWSHMTVLENVMEA--PIQVL--GLSKQEaRERAVKYLAKVGIDERAqGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 146 QRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGA 225
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
....
gi 1752086653 226 PIEI 229
Cdd:PRK10619 236 PEQL 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-202 |
6.57e-20 |
|
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: 88.69 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmapkqlakvlgllPQSpIVPE-GITVadlvgrgrfphQSVMKGW 114
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK-------------PQY-ISPDyDGTV-----------EEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 115 SKKDYEAV---AEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRY 191
Cdd:COG1245 426 NTDDFGSSyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
170
....*....|.
gi 1752086653 192 GTTIVMVLHDI 202
Cdd:COG1245 506 GKTAMVVDHDI 516
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-200 |
9.20e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 9.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGllPQSPIVPEgITV 96
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPA-LTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVgrgRFphqsvmkgWSK---KDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLD 173
Cdd:PRK13539 91 AENL---EF--------WAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*...
gi 1752086653 174 ITYQVEILDLLTD-LNKryGTTIVMVLH 200
Cdd:PRK13539 160 AAAVALFAELIRAhLAQ--GGIVIAATH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-230 |
9.34e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.88 E-value: 9.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP----TGGDVLLDGKSIHKMAPKQLAKVLG------------- 82
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGreiamifqepssc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPIVPEGI-TVADLVGRGRFPHQsvmKGWSK------------KDYEAVaealemMNITEFadrnidELSGGQRQR 149
Cdd:COG4170 102 LDPSAKIGDQLIeAIPSWTFKGKWWQR---FKWRKkraiellhrvgiKDHKDI------MNSYPH------ELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIaEGAPIEI 229
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV-ESGPTEQ 245
|
.
gi 1752086653 230 I 230
Cdd:COG4170 246 I 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-200 |
1.01e-19 |
|
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: 83.36 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA--------RLIKPTGGDVLLdgksihkmapkqlakvlglLPQS 87
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLF-------------------LPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PIVPEGiTVADLVgrgRFPhqsvmkgWSkkdyeavaealemmnitefadrniDELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:cd03223 73 PYLPLG-TLREQL---IYP-------WD------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 1752086653 168 PTTYLDITYQVEILDLLTDLnkryGTTIVMVLH 200
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-205 |
1.20e-19 |
|
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: 84.08 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmapkqlakvlgllpQ 86
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--------------Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADlvgrgrfpHQSVMKG---------WSKKDY--EAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMA 155
Cdd:cd03231 68 RDSIARGLLYLG--------HAPGIKTtlsvlenlrFWHADHsdEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLS 205
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-220 |
1.35e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ---LAKVLGLLPQSPIVPEGITVA 97
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 98 DLVGrgrFPhqSVMKGWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITY 176
Cdd:PRK10908 98 DNVA---IP--LIIAGASGDDIRRrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752086653 177 QVEILDLLTDLNkRYGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:PRK10908 173 SEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-202 |
1.44e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.56 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKmapkqlakvlgllPQSpIVPE-GITVADLVGrgrfphqSVMKGW 114
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYK-------------PQY-IKPDyDGTVEDLLR-------SITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 115 SKKDYEAvaEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEIldllTDLNKRY--- 191
Cdd:PRK13409 429 GSSYYKS--EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV----AKAIRRIaee 502
|
170
....*....|..
gi 1752086653 192 -GTTIVMVLHDI 202
Cdd:PRK13409 503 rEATALVVDHDI 514
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-233 |
1.60e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.59 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIkPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGi 94
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVADlvgrgrfphqSVMKGWSKKDYEAVAEALEMMNITEFADRN-------IDE----LSGGQRQRVWIAMALAQQTDIL 163
Cdd:PRK11174 438 TLRD----------NVLLGNPDASDEQLQQALENAWVSEFLPLLpqgldtpIGDqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSARYaDYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-208 |
2.11e-19 |
|
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: 87.30 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLS-IPSNQISIIiGANGCGKSTLLKTMARLIKPTGGDVLldgksihkmaPKQLAKVlGLLPQSPIVPEGIT 95
Cdd:TIGR03719 17 KKEILKDISLSfFPGAKIGVL-GLNGAGKSTLLRIMAGVDKDFNGEAR----------PQPGIKV-GYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVGRG---------RFPHQSVMKGWSKKDYEAVAE-------------ALEMMNITEFA---------DRNIDELSG 144
Cdd:TIGR03719 85 VRENVEEGvaeikdaldRFNEISAKYAEPDADFDKLAAeqaelqeiidaadAWDLDSQLEIAmdalrcppwDADVTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 145 GQRQRVWIAMALAQQTDILFLDEPTTYLDityqVEILDLLTDLNKRYGTTIVMVLHDinlsaRY 208
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD-----RY 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-202 |
2.94e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.53 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 22 NDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLLPQSPIV---PEgIT 95
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLAslnPR-MT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVG---RGRFPHQSvmkgwskkDYEAVAEALEMMN----ITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:PRK15079 117 IGEIIAeplRTYHPKLS--------RQEVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190
....*....|....*....|....*....|....
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDI 202
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-226 |
4.09e-19 |
|
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: 82.93 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTVa 97
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 98 dlvgrgRF---PHqsvmkgwSKKDYEAVAEALEMMNITEFA-------DRNIDE----LSGGQRQRVWIAMALAQQTDIL 163
Cdd:cd03244 95 ------RSnldPF-------GEYSDEELWQALERVGLKEFVeslpgglDTVVEEggenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLTdlNKRYGTTIVMVLHDINLSARYaDYLFTVKNGQLIAEGAP 226
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-233 |
4.49e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKT--ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:PRK11160 342 NNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIV-----PEGITVADlvgrgrfphqsvmkgwSKKDYEAVAEALEMMNITEFADRN------IDE----LSGGQRQRVW 151
Cdd:PRK11160 422 RVHLfsatlRDNLLLAA----------------PNASDEALIEVLQQVGLEKLLEDDkglnawLGEggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSARYaDYLFTVKNGQLIAEGAPIEIIT 231
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA 562
|
..
gi 1752086653 232 AD 233
Cdd:PRK11160 563 QQ 564
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-202 |
5.57e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.02 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 25 NLSIPSN-QISIIIGANGCGKSTLLKTMARLIKPTGGDV------------------------LLDG--KSIHK-----M 72
Cdd:PRK13409 92 GLPIPKEgKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtelqnyfkkLYNGeiKVVHKpqyvdL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 73 APKQL-AKVLGLLPQspiVPEgitvadlvgRGRFphqsvmkgwskkdyEAVAEALEMMNITefaDRNIDELSGGQRQRVW 151
Cdd:PRK13409 172 IPKVFkGKVRELLKK---VDE---------RGKL--------------DEVVERLGLENIL---DRDISELSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDI 202
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-208 |
6.72e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 85.56 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLS-IPSNQISIIiGANGCGKSTLLKTMARLIKPTGGD-VLLDGKSIhkmapkqlakvlGLLPQSPIVPEGI 94
Cdd:PRK11819 19 KKQILKDISLSfFPGAKIGVL-GLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKV------------GYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVADLVGRG---------RFPHQSVMKGWSKKDYEAVAE-------------ALEMMNITEFA---------DRNIDELS 143
Cdd:PRK11819 86 TVRENVEEGvaevkaaldRFNEIYAAYAEPDADFDALAAeqgelqeiidaadAWDLDSQLEIAmdalrcppwDAKVTKLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 144 GGQRQRVWIAMALAQQTDILFLDEPTTYLDityqVEILDLLTDLNKRYGTTIVMVLHDinlsaRY 208
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD-----RY 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-205 |
7.95e-19 |
|
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: 81.64 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPkQLAKVLGLLPQ 86
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVgrgRFPHQsvmkgWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:TIGR01189 81 LPGLKPELSALENL---HFWAA-----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLS 205
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-219 |
9.07e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.10 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKS----IHKMAPKQL----AKVLGLLPQ----SP 88
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREIlalrRRTIGYVSQflrvIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVPEGITVAD-LVGRGrFPHQsvmkgwskkdyEAVAEALEMmniteFADRNIDE---------LSGGQRQRVWIAMALAQ 158
Cdd:COG4778 107 RVSALDVVAEpLLERG-VDRE-----------EARARAREL-----LARLNLPErlwdlppatFSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 159 QTDILFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQ 219
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-223 |
2.00e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMapkQLAKV 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 lgLLPQSPIVPEGITVadlVGRGRFPHQSVMKGW--SKKDY-EAVAEALEMM-NITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:PRK11614 78 --MREAVAIVPEGRRV---FSRMTVEENLAMGGFfaERDQFqERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-202 |
2.96e-18 |
|
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: 83.68 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 25 NLSIP-SNQISIIIGANGCGKSTLLKTMARLIKPTGGDV------------------------LLDG--KSIHK-----M 72
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGeiKVAHKpqyvdL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 73 APKQLakvlgllpqspivpEGiTVADLVgrgrfphqsvmkgwSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVW 151
Cdd:COG1245 172 IPKVF--------------KG-TVRELL--------------EKVDERGKLdELAEKLGLENILDRDISELSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDI 202
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-201 |
4.32e-18 |
|
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: 83.45 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLdGKSIHkmapkqlakvLGLLPQ 86
Cdd:TIGR03719 324 EAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SpivPEGITvadlvgrgrfPHQSVmkgwskkdYEAVAEALEMMNI--TEFADR---------------NIDELSGGQRQR 149
Cdd:TIGR03719 393 S---RDALD----------PNKTV--------WEEISGGLDIIKLgkREIPSRayvgrfnfkgsdqqkKVGQLSGGERNR 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLDityqVEILDLLTDLNKRYGTTIVMVLHD 201
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-212 |
4.47e-18 |
|
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: 80.87 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 26 LSIP-SNQISIIIGANGCGKSTLLKTMARLIKPTGG--------DVLLD---GKSIHKMAPKQLAKVLgllpqSPIV-PE 92
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwDEILDefrGSELQNYFTKLLEGDV-----KVIVkPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 GItvaDLVgrgrfPHQ---SVMKGWSKKD----YEAVAEALEMMNITefaDRNIDELSGGQRQRVWIAMALAQQTDILFL 165
Cdd:cd03236 95 YV---DLI-----PKAvkgKVGELLKKKDergkLDELVDQLELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYL 212
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-223 |
4.63e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-----LA------KVLGLLPQSPI 89
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagIAyvpedrKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 VpEGITVADLVGRGRFphqsvmkGW--SKKDYEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:COG1129 348 R-ENITLASLDRLSRG-------GLldRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRyGTTIVMV---LHDInlsARYADYLFTVKNGQLIAE 223
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVIsseLPEL---LGLSDRILVMREGRIVGE 475
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-228 |
6.82e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPT------GGDVLLDGKSIHKMAPKQlaKVLGLLPQSpivpegitv 96
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQkgrivlNGRVLFDAEKGICLPPEK--RRIGYVFQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLvgrgrFPHQSVMK----GWSKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYL 172
Cdd:PRK11144 85 ARL-----FPHYKVRGnlryGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 173 DITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGaPIE 228
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG-PLE 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-241 |
2.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-LAKVLGLLPQ 86
Cdd:PRK13644 5 ENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVP-EGITVADLVGRGR----FPHQSVMKgwskkdyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTD 161
Cdd:PRK13644 85 NPETQfVGRTVEEDLAFGPenlcLPPIEIRK--------RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 162 ILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPiEIITADLIKETFQL 241
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEP-ENVLSDVSLQTLGL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-196 |
5.46e-17 |
|
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: 80.25 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYD-NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQS 87
Cdd:COG5265 361 ENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PiVPEGITVADLVGRGRfPHQSvmkgwskkdYEAVAEALEMMNITEFADR-------NIDE----LSGGQRQRVWIAMAL 156
Cdd:COG5265 441 T-VLFNDTIAYNIAYGR-PDAS---------EEEVEAAARAAQIHDFIESlpdgydtRVGErglkLSGGEKQRVAIARTL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYgTTIV 196
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGR-TTLV 548
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-249 |
7.88e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKS-----IHKMAPKQLAKVL----GLLP 85
Cdd:PRK11701 16 YGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAERRRLLrtewGFVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIvpEGITVAdlVGRGRFPHQSVMK-GWskKDYEAV-AEALEMMNITEFADRNIDEL----SGGQRQRVWIAMALAQQ 159
Cdd:PRK11701 96 QHPR--DGLRMQ--VSAGGNIGERLMAvGA--RHYGDIrATAGDWLERVEIDAARIDDLpttfSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGapieiitadliketf 239
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG--------------- 234
|
250
....*....|
gi 1752086653 240 qLDCQVINDP 249
Cdd:PRK11701 235 -LTDQVLDDP 243
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-233 |
1.02e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTI--LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvlgll 84
Cdd:PRK11176 343 EFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 pQSPIVPEGI-----TVADLVGRGRFPHqsvmkgWSKKDYEAVAEALEMMNITEFADRNIDE--------LSGGQRQRVW 151
Cdd:PRK11176 418 -QVALVSQNVhlfndTIANNIAYARTEQ------YSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 152 IAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHdiNLSA-RYADYLFTVKNGQLIAEGAPIEII 230
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH--RLSTiEKADEILVVEDGEIVERGTHAELL 566
|
...
gi 1752086653 231 TAD 233
Cdd:PRK11176 567 AQN 569
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-198 |
1.05e-16 |
|
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: 75.55 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-LAKVLGLlpqspiVPEgitvaDL 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAY------VPE-----DR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VGRGRFPHQSVMkgwskkdyeavaealEMMNITEFadrnideLSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVE 179
Cdd:cd03215 85 KREGLVLDLSVA---------------ENIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170
....*....|....*....
gi 1752086653 180 ILDLLTDLNKRyGTTIVMV 198
Cdd:cd03215 143 IYRLIRELADA-GKAVLLI 160
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-232 |
1.35e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.92 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 24 VNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP----TGGDVLLDGKSIHKMAPKQLAKVLG-------LLPQSPIVPe 92
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGhnvsmifQEPQSCLDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 gitvADLVGRGRFphQSVmKGWSKKD--YEAVA----EALEMMNITEFADRNiD-------ELSGGQRQRVWIAMALAQQ 159
Cdd:PRK15093 105 ----SERVGRQLM--QNI-PGWTYKGrwWQRFGwrkrRAIELLHRVGIKDHK-DamrsfpyELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITA 232
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-220 |
1.45e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAP---KQL--- 77
Cdd:PRK10522 322 TLELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedyRKLfsa 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 78 --------AKVLGllpqspivPEGITVADlvgrgrfphqsvmkgwskKDYEAVAEALEMMNITEFADRNID--ELSGGQR 147
Cdd:PRK10522 402 vftdfhlfDQLLG--------PEGKPANP------------------ALVEKWLERLKMAHKLELEDGRISnlKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 148 QRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDiNLSARYADYLFTVKNGQL 220
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-224 |
1.69e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLLPQSPIV---PEgITVADLVGRGRFPHqS 109
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPYAsldPR-QTVGDSIMEPLRVH-G 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 110 VMKGwsKKDYEAVAEALEMMNIT-EFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLN 188
Cdd:PRK10261 433 LLPG--KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQ 510
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752086653 189 KRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEG 224
Cdd:PRK10261 511 RDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-233 |
1.88e-16 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 78.46 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITVADL 99
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VGRGRFPHQSVMkgwskkdyeavaEALEMMNITEFADRN-------IDE----LSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:TIGR03797 548 AGGAPLTLDEAW------------EAARMAGLAEDIRAMpmgmhtvISEgggtLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 169 TTYLDITYQVEILDLLTDLNkryGTTIVmVLHdiNLSA-RYADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:TIGR03797 616 TSALDNRTQAIVSESLERLK---VTRIV-IAH--RLSTiRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-233 |
2.41e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 29 PSNQISIIiGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTVadlvgrgRFPhq 108
Cdd:PLN03232 1261 PSEKVGVV-GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TV-------RFN-- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 109 svMKGWSKKDYEAVAEALEMMNITEFADRNI-----------DELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDItyQ 177
Cdd:PLN03232 1330 --IDPFSEHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDV--R 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 178 VEILDLLTDLNKRYGTTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-235 |
2.99e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARlIKPTG---GDVLLDGKSIHKMAPKQL 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 78 -AKVLGLLPQSPIVPEGITVADLVGRGRFPHQSVMKGWSKKdYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMAL 156
Cdd:PRK13549 80 eRAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAM-YLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 157 AQQTDILFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEgAPIEIITADLI 235
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTEDDI 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-200 |
4.28e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIkPTG----GDVLLDGksiHKMAPKQLAKVLGLLPQSPIVPEG 93
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS-PKGvkgsGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVAD-LVGRGRFP-HQSVMKgwsKKDYEAVAEALEMMNITEFADRNIDE------LSGGQRQRVWIAMALAQQTDILFL 165
Cdd:TIGR00955 114 LTVREhLMFQAHLRmPRRVTK---KEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190
....*....|....*....|....*....|....*
gi 1752086653 166 DEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLH 200
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-221 |
6.28e-16 |
|
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: 73.82 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 11 IQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA--RLIKPTGGDVLLDGKSIhkmaPKQLAKVLGLLPQSP 88
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPL----DKNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVPEGITvadlvgrgrfphqsvmkgwskkdyeaVAEALEMmnitefaDRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:cd03232 89 VHSPNLT--------------------------VREALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 169 TTYLDITYQVEILDLLTDLnKRYGTTIVMVLH--DINLSARYADYLFTVKNGQLI 221
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHqpSASIFEKFDRLLLLKRGGKTV 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-237 |
6.62e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH-KMAPKQLAKVLGLLPQS-PIVPEgITVAD 98
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQElHLVPE-MTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 99 LVGRGRFPHQSvmkGW--SKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITy 176
Cdd:PRK11288 99 NLYLGQLPHKG---GIvnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR- 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 177 QVEIL-DLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITAD-LIKE 237
Cdd:PRK11288 175 EIEQLfRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDqLVQA 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-235 |
7.19e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.79 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARlIKPTG---GDVLLDGKSIHKMAPKQL-AKVLG 82
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTeRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQS-PIVPEgITVADLVGRGrfpHQSVMKGWSKKDYEAVAEALEMMNITEFAD----RNIDELSGGQRQRVWIAMALA 157
Cdd:TIGR02633 82 IIHQElTLVPE-LSVAENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQLDAdnvtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLI 235
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-224 |
8.91e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.54 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT-ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLP 85
Cdd:PRK13657 336 EFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPivpeGI---TVAD--LVGRGRFPHqsvmkgwskkdyEAVAEALEMMNITEFADRNID-----------ELSGGQRQR 149
Cdd:PRK13657 416 QDA----GLfnrSIEDniRVGRPDATD------------EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLnkRYGTTIVMVLHdiNLSA-RYADYLFTVKNGQLIAEG 224
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAH--RLSTvRNADRILVFDNGRVVESG 551
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-226 |
1.20e-15 |
|
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: 75.99 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 24 VNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkmapkqlakvlgllpqsPIVPEgiTVADLvgRG 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--------------------PVTAD--NREAY--RQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 104 RF------PH--QSVMKGWSKKDYEAVAEALEMMNI---TEFADRNID--ELSGGQRQRVWIAMALAQQTDILFLDE--- 167
Cdd:COG4615 407 LFsavfsdFHlfDRLLGLDGEADPARARELLERLELdhkVSVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEwaa 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 168 ---PtTYLDITYQvEILDLLtdlnKRYGTTIVMVLHDinlsARY---ADYLFTVKNGQLIAEGAP 226
Cdd:COG4615 487 dqdP-EFRRVFYT-ELLPEL----KARGKTVIAISHD----DRYfdlADRVLKMDYGKLVELTGP 541
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-174 |
1.30e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLdGKSIhkmapkQLAKVlgllPQ 86
Cdd:PRK11819 326 EAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------KLAYV----DQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SpivPEGITvadlvgrgrfPHQSVmkgwskkdYEAVAEALEMMNI--TEFADR---------------NIDELSGGQRQR 149
Cdd:PRK11819 395 S---RDALD----------PNKTV--------WEEISGGLDIIKVgnREIPSRayvgrfnfkggdqqkKVGVLSGGERNR 453
|
170 180
....*....|....*....|....*
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLDI 174
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-226 |
1.36e-15 |
|
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: 73.22 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGY--DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:cd03369 8 EVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLvgrGRFPHQSvmkgwskkDYEaVAEALEmmnITEFAdrniDELSGGQRQRVWIAMALAQQTDILF 164
Cdd:cd03369 88 PQDPTLFSGTIRSNL---DPFDEYS--------DEE-IYGALR---VSEGG----LNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLNKryGTTIVMVLHDINLSARYaDYLFTVKNGQLIAEGAP 226
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-230 |
1.93e-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: 75.61 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDV-------LLDGKSIHKMAPKQLAKVLGLLPQSpivpeg 93
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 itvadlvgRGRFPHQSVMKGWSKK------DYEAVAEA---LEMMNITEFADRNI-----DELSGGQRQRVWIAMALAQQ 159
Cdd:TIGR03269 374 --------YDLYPHRTVLDNLTEAiglelpDELARMKAvitLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-235 |
1.99e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQlAKVLG--LL 84
Cdd:PRK15439 13 CARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVpegitvadlvgrgrFPHQSVMK----GWSK--KDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQ 158
Cdd:PRK15439 92 PQEPLL--------------FPNLSVKEnilfGLPKrqASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 159 QTDILFLDEPTTYLDityQVEILDLLTDLNK--RYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLI 235
Cdd:PRK15439 158 DSRILILDEPTASLT---PAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-178 |
5.05e-15 |
|
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: 74.56 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGY--DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKpTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ 86
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 SPIVPEGITVADLVgrgrfPHQSvmkgWSKKDYEAVAEALEMMNITE-FADRnID--------ELSGGQRQRVWIAMALA 157
Cdd:TIGR01271 1300 KVFIFSGTFRKNLD-----PYEQ----WSDEEIWKVAEEVGLKSVIEqFPDK-LDfvlvdggyVLSNGHKQLMCLARSIL 1369
|
170 180
....*....|....*....|..
gi 1752086653 158 QQTDILFLDEPTTYLD-ITYQV 178
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDpVTLQI 1391
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-217 |
5.29e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.68 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKT---ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLL-DGKSIHKMAPKQLAKVLG 82
Cdd:PTZ00265 384 QFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 83 LLPQSPI-----VPEGI-----TVADLVGRGRFPHQSVMKGWS-------------------------------KKDYEA 121
Cdd:PTZ00265 464 VVSQDPLlfsnsIKNNIkyslySLKDLEALSNYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsneliemRKNYQT 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 122 VAEAlEMMNITE-----------------FADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLL 184
Cdd:PTZ00265 544 IKDS-EVVDVSKkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|...
gi 1752086653 185 TDLNKRYGTTIVMVLHDINlSARYADYLFTVKN 217
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-178 |
9.91e-15 |
|
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: 72.19 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGY--DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKpTGGDVLLDGKSIHKMAPKQLAKVLGLL 84
Cdd:cd03289 4 TVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVADLVGRGRfphqsvmkgWSKKDYEAVAEALEMMNITEFADRNID--------ELSGGQRQRVWIAMAL 156
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGK---------WSDEEIWKVAEEVGLKSVIEQFPGQLDfvlvdggcVLSHGHKQLMCLARSV 153
|
170 180
....*....|....*....|...
gi 1752086653 157 AQQTDILFLDEPTTYLD-ITYQV 178
Cdd:cd03289 154 LSKAKILLLDEPSAHLDpITYQV 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-201 |
1.17e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.45 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMArlikptgGDVLLDGKSIhkmapkQLAK--VLGLLPQSPIVPEGITVA 97
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRI------IYEQdlIVARLQQDPPRNVEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 98 DLVGRG---------RFPHQS--VMKGWSKKD---YEAVAEALEMMNITEF--------------ADRNIDELSGGQRQR 149
Cdd:PRK11147 85 DFVAEGieeqaeylkRYHDIShlVETDPSEKNlneLAKLQEQLDHHNLWQLenrinevlaqlgldPDAALSSLSGGWLRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 150 VWIAMALAQQTDILFLDEPTTYLDItyqvEILDLLTDLNKRYGTTIVMVLHD 201
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-234 |
2.46e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPivpegitVADLVGR 102
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-------STSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 103 GR------FPHQSVMKGWSKKDYEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDIT 175
Cdd:PRK15112 104 QRisqildFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 176 YQVEILDLLTDLNKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADL 234
Cdd:PRK15112 184 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-200 |
3.60e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSgydnKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTG--GDVLLDGKSIhkmaPKQLAKVLGLL 84
Cdd:PLN03211 74 ETRQIQE----RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVAD---LVGRGRFPhqsvmKGWSKKDYEAVAEA------LEMMNITEFADRNIDELSGGQRQRVWIAMA 155
Cdd:PLN03211 146 TQDDILYPHLTVREtlvFCSLLRLP-----KSLTKQEKILVAESviselgLTKCENTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLH 200
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-200 |
4.49e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIK--PTGGDVLLDGKSIhkmapkqlakvlgllpqspivPEGIT 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF---------------------GREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVGRgrfphqsvmkgwsKKDyeaVAEALEMMNITEFAD-----RNIDELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:COG2401 102 LIDAIGR-------------KGD---FKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|
gi 1752086653 171 YLDITYQVEILDLLTDLNKRYGTTIVMVLH 200
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-224 |
4.75e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 1 MTTHTFETKNIQSGY-DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAK 79
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 VLGLLPQSPIVPEGiTVADLVGRGRfphqsvmkgwsKKDYEAVAEALEMMNITEFAdRNIDE------------LSGGQR 147
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTLGR-----------DISEEQVWQALETVQLAELA-RSLPDglytplgeqgnnLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 148 QRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRygTTIVMVLHdiNLSARY-ADYLFTVKNGQLIAEG 224
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH--RLSTIVeADTILVLHRGQAVEQG 556
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-201 |
4.76e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGK------SIHKMApkqlak 79
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevayfDQHRAE------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 80 vlgLLPQSpivpegiTVADLVGRGRfphQSVMKGWSKKdyeavaEALEMMNITEF----ADRNIDELSGGQRQRVWIAMA 155
Cdd:PRK11147 394 ---LDPEK-------TVMDNLAEGK---QEVMVNGRPR------HVLGYLQDFLFhpkrAMTPVKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752086653 156 LAQQTDILFLDEPTTYLDItyqvEILDLLTDLNKRYGTTIVMVLHD 201
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-232 |
5.10e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.52 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITVADL 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VGRGRFPHQSVmkgWSkkdyeavaeALEMMNITEFADRNIDE-----------LSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:TIGR00957 1381 DPFSQYSDEEV---WW---------ALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 169 TTYLDItyqvEILDLL-TDLNKRYGT-TIVMVLHDINLSARYADYLFTVKnGQLIAEGAPIEIITA 232
Cdd:TIGR00957 1449 TAAVDL----ETDNLIqSTIRTQFEDcTVLTIAHRLNTIMDYTRVIVLDK-GEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-174 |
5.56e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSI-PSNQISIIiGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTVad 98
Cdd:PLN03130 1254 VLHGLSFEIsPSEKVGIV-GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TV-- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 99 lvgrgRFPhqsvMKGWSKKDYEAVAEALEMMNITEFADRNI-----------DELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:PLN03130 1330 -----RFN----LDPFNEHNDADLWESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
....*..
gi 1752086653 168 PTTYLDI 174
Cdd:PLN03130 1401 ATAAVDV 1407
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-173 |
2.01e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITVADLvgr 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENL--- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 103 gRFPHQsvMKGWSkkDYEAVAEALEMMNITEFADRNIDELSGGQRQRVwiamALA----QQTDILFLDEPTTYLD 173
Cdd:PRK13538 96 -RFYQR--LHGPG--DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRV----ALArlwlTRAPLWILDEPFTAID 161
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-235 |
5.43e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIH-KMAPKQLAKVLGLLPQSPIVPEGITVADL 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VGRGRFPhqsvMKGW---SKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDity 176
Cdd:PRK10982 94 MWLGRYP----TKGMfvdQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT--- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 177 QVEILDLLTDLNK--RYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEgAPIEIITADLI 235
Cdd:PRK10982 167 EKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT-QPLAGLTMDKI 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-230 |
7.11e-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: 67.91 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLktmaRLIKPTGGDVLLDGKSIHKMApkQLAKVLGLLPQ 86
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLM----HVLRGMDQYEPTSGRIIYHVA--LCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 S------PIVPEGIT--VADLVG-----RGRFPHQ-------------------SVMKGWSKKDY---EAVAEALEMMNI 131
Cdd:TIGR03269 76 SkvgepcPVCGGTLEpeEVDFWNlsdklRRRIRKRiaimlqrtfalygddtvldNVLEALEEIGYegkEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 132 TEFADRNID---ELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSARY 208
Cdd:TIGR03269 156 VQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|..
gi 1752086653 209 ADYLFTVKNGQLIAEGAPIEII 230
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-201 |
9.22e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVlldgksihKMAPKqlAKVlGLLPQ 86
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN--ANI-GYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 87 --SPIVPEGITVADLVGRGRFPhqsvmkgwsKKDYEAVAEALEMMNIT-EFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:PRK15064 390 dhAYDFENDLTLFDWMSQWRQE---------GDDEQAVRGTLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752086653 164 FLDEPTTYLDItyqvEILDLLTDLNKRYGTTIVMVLHD 201
Cdd:PRK15064 461 VMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHD 494
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-198 |
1.90e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-LAK--------------VLGLlp 85
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANgivyisedrkrdglVLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 qspIVPEGITVADL----VGRGRFPHQsvmkgwskKDYEAVAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALAQQT 160
Cdd:PRK10762 346 ---SVKENMSLTALryfsRAGGSLKHA--------DEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752086653 161 DILFLDEPTTYLDITYQVEILDLLTDLnKRYGTTIVMV 198
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILV 451
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-199 |
6.45e-12 |
|
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: 63.05 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 8 TKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTG---GDVLLDGKSIHKMAPKqlakvlgll 84
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEK--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 pqspivpegitvadlvgrgrFPHQSVMKGwskkdyeavAEALEMMNIT-----EFA-----DRNIDELSGGQRQRVWIAM 154
Cdd:cd03233 81 --------------------YPGEIIYVS---------EEDVHFPTLTvretlDFAlrckgNEFVRGISGGERKRVSIAE 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752086653 155 ALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVL 199
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-220 |
7.13e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLldgksihkmAPKQLAKVlgllPQSP-----IVPE 92
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERSIAYV----PQQAwimnaTVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 GITVADLVGRGRFpHQSVMKGWSKKDYEAVAEALEmmniTEFADRNIDeLSGGQRQRVWIAMALAQQTDILFLDEPTTYL 172
Cdd:PTZ00243 740 NILFFDEEDAARL-ADAVRVSQLEADLAQLGGGLE----TEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752086653 173 DITYQVEILDLLTdLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQL 220
Cdd:PTZ00243 814 DAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-201 |
7.82e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 37 IGANGCGKSTLLKTMARLIKPTGGDVLLDgksihkmaPKQlakVLGLLPQSPIVPEGITVADLVGRGRFPHQSVMK---- 112
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLD--------PNE---RLGKLRQDQFAFEEFTVLDTVIMGHTELWEVKQerdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 113 -----GWSKKDYEAVAEaLEMmnitEFAD--------RNIDELSG-----------------GQRQRVWIAMALAQQTDI 162
Cdd:PRK15064 102 iyalpEMSEEDGMKVAD-LEV----KFAEmdgytaeaRAGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752086653 163 LFLDEPTTYLDITyqvEILDLLTDLNKRyGTTIVMVLHD 201
Cdd:PRK15064 177 LLLDEPTNNLDIN---TIRWLEDVLNER-NSTMIIISHD 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-220 |
1.24e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 11 IQSGYDNKTILNDVNLS-IPSNQISIIiGANGCGKSTLLKTMARLIKPTGGDV-LLDGKSIHKMAPKQL-------AKVL 81
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNlVPGSRIGLL-GRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLeflradeSPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 82 GLLPQSPIVPEGiTVADLVGRGRFPHQSVmkgwskkdyeavaealemmniTEFADRnideLSGGQRQRVWIAMALAQQTD 161
Cdd:PRK10636 397 HLARLAPQELEQ-KLRDYLGGFGFQGDKV---------------------TEETRR----FSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 162 ILFLDEPTTYLDITYQVEILDLLTDlnkrYGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-198 |
1.49e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIqSGYDNKTIlNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAP-----KQLAKV 80
Cdd:PRK09700 266 FEVRNV-TSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 L------GLLPQSPIvPEGITVADLVGRGRFphQSVMKGWSKKDYEAVAEAL-EMMNIT-EFADRNIDELSGGQRQRVWI 152
Cdd:PRK09700 344 TesrrdnGFFPNFSI-AQNMAISRSLKDGGY--KGAMGLFHEVDEQRTAENQrELLALKcHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752086653 153 AMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMV 198
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMV 465
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-198 |
1.59e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 22 NDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-LAKVLGLLP----QSPIVPeGITV 96
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCPedrkAEGIIP-VHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGRGRFPHQSVMKGWSKKDYEA--VAEALEMMNI-TEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLD 173
Cdd:PRK11288 349 ADNINISARRHHLRAGCLINNRWEAenADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180
....*....|....*....|....*
gi 1752086653 174 ITYQVEILDLLTDLNKRyGTTIVMV 198
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQ-GVAVLFV 452
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-221 |
1.62e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARlIKPTG---GDVLLDG-----KSIHkmAPKQLAKV-----LGLLPQS 87
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFDGevcrfKDIR--DSEALGIViihqeLALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PIVpEGITVADLVGRGRFPHqsvmkgWSKKDYEAvAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDE 167
Cdd:NF040905 94 SIA-ENIFLGNERAKRGVID------WNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 168 PTTYLDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLI 221
Cdd:NF040905 166 PTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-173 |
1.97e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.43 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKV---LGLLPQspivpeg 93
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIghnLGLKLE------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVADlvgrgrfphqsVMKGWSK--KDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:PRK13541 85 MTVFE-----------NLKFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
..
gi 1752086653 172 LD 173
Cdd:PRK13541 154 LS 155
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-221 |
2.66e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 5 TFETKN----IQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP---TGGDVLLDGKSIHkmapKQL 77
Cdd:TIGR00956 759 IFHWRNltyeVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 78 AKVLGLLPQSPIVPEGITVADLV---GRGRFPhQSVMKgWSKKDY-EAVAEALEMmniTEFADRNIDE----LSGGQRQR 149
Cdd:TIGR00956 835 QRSIGYVQQQDLHLPTSTVRESLrfsAYLRQP-KSVSK-SEKMEYvEEVIKLLEM---ESYADAVVGVpgegLNVEQRKR 909
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 150 VWIAMALAQQTD-ILFLDEPTTYLDITYQVEILDLLTDLNKrYGTTIVMVLH--DINLSARYADYLFTVKNGQLI 221
Cdd:TIGR00956 910 LTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHqpSAILFEEFDRLLLLQKGGQTV 983
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-235 |
2.91e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPK--QLAKV------LGLLPQspivpe 92
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssQEAGIgiihqeLNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 gITVADLVGRGR-FPHQSVMKGWsKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:PRK10762 94 -LTIAENIFLGReFVNRFGRIDW-KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 172 LDITYQVEILDLLTDLnKRYGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLI 235
Cdd:PRK10762 172 LTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLI 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-233 |
3.63e-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: 63.04 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHkmAPKQlAKVlgllpQSPIVPEGITvadlv 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY--VPQQ-AWI-----QNDSLRENIL----- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 grgrFPHQsvmkgWSKKDYEAVAEA------LEMM---NITEFADRNIDeLSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:TIGR00957 721 ----FGKA-----LNEKYYQQVLEAcallpdLEILpsgDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 172 LDITYQVEILD-LLTDLNKRYGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEIITAD 233
Cdd:TIGR00957 791 VDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQRD 852
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-212 |
6.24e-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: 62.07 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISI--------------IIGANGCGKSTLLKTMARLIkPTGGDVLldgksiHKMAPKQLAKVl 81
Cdd:TIGR00954 449 DNGIKFENIPLVTPNGDVLIeslsfevpsgnnllICGPNGCGKSSLFRILGELW-PVYGGRL------TKPAKGKLFYV- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 82 gllPQSPIVPEGiTVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITEfadRNI---------DELSGGQRQRVWI 152
Cdd:TIGR00954 521 ---PQRPYMTLG-TLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILE---REGgwsavqdwmDVLSGGEKQRIAM 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 153 AMALAQQTDILFLDEPTTYLdityQVEILDLLTDLNKRYGTTIVMVLHDINLsARYADYL 212
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSL-WKYHEYL 648
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-224 |
9.09e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 17 NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTV 96
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 97 ADLVGRGRfphqsvmKGWSKKDYEAVAEaleMMNI------------TEFADRNIdELSGGQRQRVWIAMALAQQTDILF 164
Cdd:PRK10789 406 ANNIALGR-------PDATQQEIEHVAR---LASVhddilrlpqgydTEVGERGV-MLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 165 LDEPTTYLDITYQVEILDLLTDLnkRYGTTIVMVLHdiNLSA-RYADYLFTVKNGQLIAEG 224
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQW--GEGRTVIISAH--RLSAlTEASEILVMQHGHIAQRG 531
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-220 |
1.11e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 23 DVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQ-LAKVLGLLPQ----------SPIVP 91
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEdrqssglyldAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 EgiTVADLVGRGRFphqsvmkgWSKKDYE-AVAEAL-EMMNIT-EFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:PRK15439 361 N--VCALTHNRRGF--------WIKPAREnAVLERYrRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-231 |
1.15e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 115 SKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLnKRYGT 193
Cdd:NF000106 117 SRKDARARAdELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGA 195
|
90 100 110
....*....|....*....|....*....|....*...
gi 1752086653 194 TIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIIT 231
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-173 |
2.26e-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: 60.80 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 36 IIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhKMAPKQLAKVLGLLPQSPIVPEGITvadlvGRGRFPHQSVMKGWS 115
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAIDDLLT-----GREHLYLYARLRGVP 2043
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 116 KKDYEAVAE-ALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLD 173
Cdd:TIGR01257 2044 AEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-235 |
2.51e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTiLNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQ-------S 87
Cdd:PRK10938 14 SDTKT-LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQrnntdmlS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 88 PIVPE-GITVADLVGRGrfphqsvmkgwsKKDYEAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLD 166
Cdd:PRK10938 93 PGEDDtGRTTAEIIQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 167 EPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAEGAPIEIITADLI 235
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALV 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-182 |
5.81e-10 |
|
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: 58.33 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkmapkqlakvLGLLPQ-SPIVPEGItvad 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQfSWIMPGTI---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 99 lvgrgrfpHQSVMKGWSKKD--YEAVAEALEM-MNITEFADRN---IDE----LSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:cd03291 115 --------KENIIFGVSYDEyrYKSVVKACQLeEDITKFPEKDntvLGEggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170
....*....|....
gi 1752086653 169 TTYLDITYQVEILD 182
Cdd:cd03291 187 FGYLDVFTEKEIFE 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-229 |
7.00e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 10 NIQSGY---DNKT---ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMarlikptggdvlldgksIHKMAPKQLAKV--- 80
Cdd:PLN03232 616 SIKNGYfswDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-----------------LGELSHAETSSVvir 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 81 --LGLLPQSPIVPEGITVADLVGRGRFPHQsvmKGWSKKDYEAVAEALEMM---NITEFADRNIDeLSGGQRQRVWIAMA 155
Cdd:PLN03232 679 gsVAYVPQVSWIFNATVRENILFGSDFESE---RYWRAIDVTALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 156 LAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARyADYLFTVKNGQLIAEGAPIEI 229
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAEL 826
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-182 |
7.33e-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: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKsihkmapkqlakvLGLLPQSPIVPEGiTVADl 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG-TIKD- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 vgrgrfphqSVMKGWSKKD--YEAVAEALEMM-NITEFADRN---IDE----LSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:TIGR01271 506 ---------NIIFGLSYDEyrYTSVIKACQLEeDIALFPEKDktvLGEggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170
....*....|...
gi 1752086653 170 TYLDITYQVEILD 182
Cdd:TIGR01271 577 THLDVVTEKEIFE 589
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-232 |
8.63e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQisiiiGANGcGKSTLLKTmarlikptGGDVLLDGKSIHKMAPKQLAKVLGLLPQSP 88
Cdd:PTZ00265 1240 QDYQGDEEQNVGMKNVNEFSLTKE-----GGSG-EDSTVFKN--------SGKILLDGVDICDYNLKDLRNLFSIVSQEP 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 IVpEGITVadlvgrgrfpHQSVMKGWSKKDYEAVAEALEMMNITEFA-------DRNI----DELSGGQRQRVWIAMALA 157
Cdd:PTZ00265 1306 ML-FNMSI----------YENIKFGKEDATREDVKRACKFAAIDEFIeslpnkyDTNVgpygKSLSGGQKQRIAIARALL 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 158 QQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDInLSARYADYLFTVKN----GQLI-AEGAPIEIITA 232
Cdd:PTZ00265 1375 REPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNNpdrtGSFVqAHGTHEELLSV 1453
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-169 |
1.36e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 22 NDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhkmAPKQLA--KVLGLLPQSPIVPEGITV-AD 98
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIAtrRRVGYMSQAFSLYGELTVrQN 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 99 LVGRGRFPHQsvmkgwSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:NF033858 360 LELHARLFHL------PAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-211 |
2.74e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 10 NIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPI 89
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 VPEGITVADLVGRGRFPHQSVmkgwskkdyeAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPT 169
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAV----------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752086653 170 TYLDityQVEILDLLTDL--NKRYGTTIVMVLHDiNLSARYADY 211
Cdd:PRK13540 156 VALD---ELSLLTIITKIqeHRAKGGAVLLTSHQ-DLPLNKADY 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-212 |
3.01e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 28 IPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIhkmapkqlakvlgllpqsPIVPEGItvadlvgrgrfph 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------------VYKPQYI------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 108 qsvmkgwskkdyeavaealemmnitefadrnidELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDL 187
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*
gi 1752086653 188 NKRYGTTIVMVLHDINLsaryADYL 212
Cdd:cd03222 118 SEEGKKTALVVEHDLAV----LDYL 138
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-203 |
3.27e-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: 54.30 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 30 SNQISIIIGANGCGKSTLLKTMARLIKPTGGDVL-LDGKSIHKMAPKQLAKVLGllpqspivpegitvadlvgrgrfphq 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 109 svmkgwskkdyeavaealemmnitefaDRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDL----- 183
Cdd:smart00382 55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180
....*....|....*....|
gi 1752086653 184 LTDLNKRYGTTIVMVLHDIN 203
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEK 127
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-203 |
4.15e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihkmapKQLAKVLGLLPQSpivpEGITVADLV 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA------ALIAISSGLNGQL----TGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 GrgrfphqsVMKGWSKKDY-EAVAEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVE 179
Cdd:PRK13545 110 G--------LMMGLTKEKIkEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|....
gi 1752086653 180 ILDLLTDLnKRYGTTIVMVLHDIN 203
Cdd:PRK13545 182 CLDKMNEF-KEQGKTIFFISHSLS 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-174 |
7.94e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMA--RLIKPTGGDVLLDGKSIHKMAPKQLA-KVLGLLP 85
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 QSPIVPEGI-------TVADLVGRGRfpHQSVMKGWSKKDYeaVAEALEMMNITE-FADRNIDE-LSGGQRQRVWIAMAL 156
Cdd:PRK09580 85 QYPVEIPGVsnqfflqTALNAVRSYR--GQEPLDRFDFQDL--MEEKIALLKMPEdLLTRSVNVgFSGGEKKRNDILQMA 160
|
170
....*....|....*...
gi 1752086653 157 AQQTDILFLDEPTTYLDI 174
Cdd:PRK09580 161 VLEPELCILDESDSGLDI 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-230 |
1.99e-08 |
|
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: 53.76 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDN--KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVpe 92
Cdd:cd03288 29 YENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 93 gitvadLVGRGRFPHQSVMKGWSKKDYEAVaEALEMMNITEFADRNIDEL--------SGGQRQRVWIAMALAQQTDILF 164
Cdd:cd03288 107 ------FSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLDAVvteggenfSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 165 LDEPTTYLDITYQvEILD--LLTDLNKRygtTIVMVLHDINlSARYADYLFTVKNGQLIAEGAPIEII 230
Cdd:cd03288 180 MDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLL 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-208 |
2.77e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLI----KPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEg 93
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPH- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 94 ITVA---DLVGRGRFPhQSVMKGWSKKDYEAVAEALEMMNI-------TEFADRNIDELSGGQRQRVWIAMALAQQTDIL 163
Cdd:TIGR00956 153 LTVGetlDFAARCKTP-QNRPDGVSREEYAKHIADVYMATYglshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752086653 164 FLDEPTTYLDITYQVEILDLLtdlnkrygTTIVMVLHDINLSARY 208
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRAL--------KTSANILDTTPLVAIY 268
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-226 |
2.96e-08 |
|
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: 53.39 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLL-KTMARLIKPtggdvLLDGKsihKMAPKQLAKVLGL--------LPQSPIvp 91
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLYPALAR-----RLHLK---KEQPGNHDRIEGLehidkvivIDQSPI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 eGIT----------VADLV---------GRgRFPHQSV---MKGWSkkdyeaVAEALEMmNITE----FAD--------- 136
Cdd:cd03271 81 -GRTprsnpatytgVFDEIrelfcevckGK-RYNRETLevrYKGKS------IADVLDM-TVEEalefFENipkiarklq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 137 -------------RNIDELSGGQRQRVWIAMALAQQTD---ILFLDEPTTYL---DITYQVEILDLLTDLnkryGTTIVM 197
Cdd:cd03271 152 tlcdvglgyiklgQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQRLVDK----GNTVVV 227
|
250 260 270
....*....|....*....|....*....|....*
gi 1752086653 198 VLHDINLsARYADYLFT------VKNGQLIAEGAP 226
Cdd:cd03271 228 IEHNLDV-IKCADWIIDlgpeggDGGGQVVASGTP 261
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-198 |
3.54e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKvLGL--LPQSP--- 88
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR-LGVayIPEDRlgr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 89 -IVPEgITVADLVGRGRFPHQSVMKGW--SKKDYEAVAEALemmnITEF------ADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:COG3845 346 gLVPD-MSVAENLILGRYRRPPFSRGGflDRKAIRAFAEEL----IEEFdvrtpgPDTPARSLSGGNQQKVILARELSRD 420
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMV 198
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLI 458
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-212 |
3.77e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.94 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTmarlikptggdvlldgkSIHKMAPKQLAKVLGLLPQSPIVpegitvadLV 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------------GLYASGKARLISFLPKFSRNKLI--------FI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 101 GRGRFphqsvmkgwskkdyeAVAEALEMMNItefaDRNIDELSGGQRQRVWIAMALAQQTD--ILFLDEPTTYLD--ITY 176
Cdd:cd03238 66 DQLQF---------------LIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHqqDIN 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 1752086653 177 Q-VEILDLLTDLnkryGTTIVMVLHDINLSaRYADYL 212
Cdd:cd03238 127 QlLEVIKGLIDL----GNTVILIEHNLDVL-SSADWI 158
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-217 |
4.76e-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: 51.84 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 9 KNIQSGYDNKTILNDvnlsipsNQISIIIGANGCGKSTLLK--TMARL-IKPTGGDvllDGKSIHKMAPKQlakvlgllp 85
Cdd:cd03240 7 RNIRSFHERSEIEFF-------SPLTLIVGQNGAGKTTIIEalKYALTgELPPNSK---GGAHDPKLIREG--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 86 qspivpEGITVADLVGRGRfphqsvmkgwSKKDYEAVAEaLEMMN---------ITEFADRNIDELSGGQRQ------RV 150
Cdd:cd03240 68 ------EVRAQVKLAFENA----------NGKKYTITRS-LAILEnvifchqgeSNWPLLDMRGRCSGGEKVlasliiRL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 151 WIAMALAQQTDILFLDEPTTYLD---ITYQveILDLLTDLNKRYGTTIVMVLHDINLsARYADYLFTVKN 217
Cdd:cd03240 131 ALAETFGSNCGILALDEPTTNLDeenIEES--LAEIIEERKSQKNFQLIVITHDEEL-VDAADHIYRVEK 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-230 |
4.94e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 20 ILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGiTVADL 99
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 100 VgrGRFPHQSVMKGWSkkdyeavaeALEMMNI-------TEFADRNIDE----LSGGQRQRVWIAMALAQQ-TDILFLDE 167
Cdd:PTZ00243 1404 V--DPFLEASSAEVWA---------ALELVGLrervaseSEGIDSRVLEggsnYSVGQRQLMCMARALLKKgSGFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 168 PTTYLDITYQVEILDLLTDLNKRYgtTIVMVLHDINLSARYaDYLFTVKNGQLIAEGAPIEII 230
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELV 1532
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-198 |
5.32e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIqSGYD----NKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMarlikpTG-------GDVLLDGKSIHKMAP 74
Cdd:PRK13549 260 LEVRNL-TAWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCL------FGaypgrweGEIFIDGKPVKIRNP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 75 KQ-LAKVLGLLP----QSPIVP-----EGITVADLvgrGRFPHQSVmkgwskkdyeaVAEALEMMNITEFADR------- 137
Cdd:PRK13549 333 QQaIAQGIAMVPedrkRDGIVPvmgvgKNITLAAL---DRFTGGSR-----------IDDAAELKTILESIQRlkvktas 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086653 138 ---NIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMV 198
Cdd:PRK13549 399 pelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-174 |
1.08e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 16 DNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQspIVPEGIT 95
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG--LKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADL----VGRGRFPHQsvMKGwskkdyeavaEALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTY 171
Cdd:PRK13543 100 LENLhflcGLHGRRAKQ--MPG----------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
...
gi 1752086653 172 LDI 174
Cdd:PRK13543 168 LDL 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-224 |
1.31e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP-TGGDVLLDGKsihkmapkqLAKVlgllPQ-SPIVpeGIT 95
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT---------VAYV----PQvSWIF--NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 96 VADLVGRGRfPHQSVmKGWSKKDYEAVAEALEMM---NITEFADRNIDeLSGGQRQRVWIAMALAQQTDILFLDEPTTYL 172
Cdd:PLN03130 695 VRDNILFGS-PFDPE-RYERAIDVTALQHDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 173 DITYQVEILD--LLTDLNkryGTTIVMVLHDIN-LSarYADYLFTVKNGQLIAEG 224
Cdd:PLN03130 772 DAHVGRQVFDkcIKDELR---GKTRVLVTNQLHfLS--QVDRIILVHEGMIKEEG 821
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-220 |
1.84e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTIL-NDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihKMAPKQLAKVLGL-LPQSPI-- 89
Cdd:PLN03073 517 GYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV--RMAVFSQHHVDGLdLSSNPLly 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 90 -------VPEGITVADLvgrGRFPHQSVMkgwskkdyeavaeALEMMNItefadrnideLSGGQRQRVWIAMALAQQTDI 162
Cdd:PLN03073 595 mmrcfpgVPEQKLRAHL---GSFGVTGNL-------------ALQPMYT----------LSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 163 LFLDEPTTYLDITyQVEIldLLTDLNKRYGtTIVMVLHDINLSARYADYLFTVKNGQL 220
Cdd:PLN03073 649 LLLDEPSNHLDLD-AVEA--LIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-223 |
2.44e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLLKTM-ARLIKPTGGDVLLDGKSIHKMAPKQ-LAKVLGLLPQSP----IVP--- 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQaIRAGIAMVPEDRkrhgIVPilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 --EGITVADLvgrGRFPHQSVMKgwSKKDYEAVAEALEMMNITEFA-DRNIDELSGGQRQRVWIAMALAQQTDILFLDEP 168
Cdd:TIGR02633 356 vgKNITLSVL---KSFCFKMRID--AAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752086653 169 TTYLDITYQVEILDLLTDLNKRyGTTIVMVLHDINLSARYADYLFTVKNGQLIAE 223
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-170 |
3.28e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 15 YDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMArlikptGGDVLLDGkSIHkmapkqlakVLG-----------L 83
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIA------GARKIQQG-RVE---------VLGgdmadarhrraV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 84 LPQSPIVPEGItvadlvGRGRFPHQSVMK---------GWSKKDYEA-VAEALEMMNITEFADRNIDELSGGQRQRVWIA 153
Cdd:NF033858 75 CPRIAYMPQGL------GKNLYPTLSVFEnldffgrlfGQDAAERRRrIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170
....*....|....*..
gi 1752086653 154 MALAQQTDILFLDEPTT 170
Cdd:NF033858 149 CALIHDPDLLILDEPTT 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-201 |
4.37e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 18 KTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihkmapkQLAKVLGLLPQSPiVPEGITVA 97
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNW-------QLAWVNQETPALP-QPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 98 DLVGRGRFPHQSVMKGWSKKDYEAVA------EALEMMNITEFA--------------DRNIDELSGGQRQRVWIAMALA 157
Cdd:PRK10636 86 DGDREYRQLEAQLHDANERNDGHAIAtihgklDAIDAWTIRSRAasllhglgfsneqlERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752086653 158 QQTDILFLDEPTTYLDityqveiLDLLTDLN---KRYGTTIVMVLHD 201
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD-------LDAVIWLEkwlKSYQGTLILISHD 205
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-202 |
1.15e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 14 GYDNKTI--LNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLDGKSihkmapkqlakvlgllpqSPIVP 91
Cdd:PRK13546 31 KHKNKTFfaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV------------------SVIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 92 EGITVADLVGRGRFPHQSVMKGWSKKDYEAVA-EALEMMNITEFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTT 170
Cdd:PRK13546 93 SAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|..
gi 1752086653 171 YLDITYQVEILDLLTDLnKRYGTTIVMVLHDI 202
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNL 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-198 |
1.41e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752086653 138 NIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRyGTTIVMV 198
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIII 447
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-230 |
2.09e-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: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 142 LSGGQRQRVWIAMALAQQTD---ILFLDEPTTYL---DITYQVEILDLLTDLnkryGTTIVMVLHDINLsARYADYLFT- 214
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDV-IKTADYIIDl 904
|
90 100
....*....|....*....|.
gi 1752086653 215 -----VKNGQLIAEGAPIEII 230
Cdd:TIGR00630 905 gpeggDGGGTVVASGTPEEVA 925
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-224 |
5.37e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 7 ETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARliKPTGGDVLLDGKsIHKMAPKQ--LAKVLGLL 84
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKKQetFARISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 85 PQSPIVPEGITVAD-LVGRG--RFPHQsVMKGWSKKDYEAVAEALEMMNITE--FADRNIDELSGGQRQRVWIAMALAQQ 159
Cdd:PLN03140 959 EQNDIHSPQVTVREsLIYSAflRLPKE-VSKEEKMMFVDEVMELVELDNLKDaiVGLPGVTGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086653 160 TDILFLDEPTTYLDITYQVEILDLLTDlNKRYGTTIVMVLH--DINLSARYADYLFTVKNGQLIAEG 224
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSG 1103
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-224 |
8.29e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNQISIIIGANGCGKSTLlktMARLIKPTGGDVLLDGKS------IHKMAPKQLAKVLGLLPqspivpegi 94
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL---AFDTIYAEGQRRYVESLSayarqfLGQMDKPDVDSIEGLSP--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 95 TVA-DLVGRGRFPHQSVMKGWSKKDY-------EAVAEALEMMNITEFA----DRNIDELSGGQRQRVWIAMAL-AQQTD 161
Cdd:cd03270 79 AIAiDQKTTSRNPRSTVGTVTEIYDYlrllfarVGIRERLGFLVDVGLGyltlSRSAPTLSGGEAQRIRLATQIgSGLTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752086653 162 ILF-LDEPTTYL---DITYQVEILDLLTDLnkryGTTIVMVLHDINLsARYADYLFTV------KNGQLIAEG 224
Cdd:cd03270 159 VLYvLDEPSIGLhprDNDRLIETLKRLRDL----GNTVLVVEHDEDT-IRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
52-229 |
1.09e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 52 ARLiKPTGGDVLLDGKSIHKMAPKQLAKVLGLLPQSPIVPEGITVADLVgrgrfphqsvMKGWSKKDYEAVAEALEMMNI 131
Cdd:TIGR00630 414 TRL-KPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEV----------LKEIRERLGFLIDVGLDYLSL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 132 tefaDRNIDELSGGQRQRVWIAMAL-AQQTDILF-LDEPTTYL---DITYQVEILDLLTDLnkryGTTIVMVLHDINlSA 206
Cdd:TIGR00630 483 ----SRAAGTLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGLhqrDNRRLINTLKRLRDL----GNTLIVVEHDED-TI 553
|
170 180
....*....|....*....|....*....
gi 1752086653 207 RYADYLFT------VKNGQLIAEGAPIEI 229
Cdd:TIGR00630 554 RAADYVIDigpgagEHGGEVVASGTPEEI 582
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-216 |
1.80e-05 |
|
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: 43.89 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 22 NDVNLsiPSNQISIIIGANGCGKSTLLKTMArlikptggdvlldgksihkmapkqlakvLGLLpqspivpegitvadlvg 101
Cdd:cd03227 14 NDVTF--GEGSLTIITGPNGSGKSTILDAIG----------------------------LALG----------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 102 rGRFPHQSVMKGWSKKDYEAVAEAlemmnitEFADRnIDELSGGQRQRVWIAMALA----QQTDILFLDEPTTYLDITYQ 177
Cdd:cd03227 47 -GAQSATRRRSGVKAGCIVAAVSA-------ELIFT-RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752086653 178 VEILDLLTDLNKRYGTTIVmVLHDINLSARyADYLFTVK 216
Cdd:cd03227 118 QALAEAILEHLVKGAQVIV-ITHLPELAEL-ADKLIHIK 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-173 |
2.01e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 6 FETKNIQSGYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKtmarLIK---PTG--GDVLL------DGKSIHKMAp 74
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITgdhPQGysNDLTLfgrrrgSGETIWDIK- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 75 KQLAKVLGLLPQSPIVpeGITVADLVGRGRFPHQSVMKGWSKKDYEAVAEALEMMNITE-FADRNIDELSGGQRQRVWIA 153
Cdd:PRK10938 336 KHIGYVSSSLHLDYRV--STSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIV 413
|
170 180
....*....|....*....|
gi 1752086653 154 MALAQQTDILFLDEPTTYLD 173
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLD 433
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
142-230 |
4.47e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 142 LSGGQRQRVWIAMALA--QQTDILF-LDEPTTYL---DITYQVEILDLLTDLnkryGTTIVMVLHdiNLSA-RYADYLFT 214
Cdd:COG0178 827 LSGGEAQRVKLASELSkrSTGKTLYiLDEPTTGLhfhDIRKLLEVLHRLVDK----GNTVVVIEH--NLDViKTADWIID 900
|
90 100
....*....|....*....|..
gi 1752086653 215 V------KNGQLIAEGAPIEII 230
Cdd:COG0178 901 LgpeggdGGGEIVAEGTPEEVA 922
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
142-229 |
1.52e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 142 LSGGQRQRVWIAMALAQ----QTdILFLDEPTTYL---DITYQVEILDLLTDLnkryGTTIVMVLHdiNLSA-RYADYLF 213
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKrstgKT-LYILDEPTTGLhfeDIRKLLEVLHRLVDK----GNTVVVIEH--NLDViKTADWII 903
|
90 100
....*....|....*....|..
gi 1752086653 214 T------VKNGQLIAEGAPIEI 229
Cdd:PRK00349 904 DlgpeggDGGGEIVATGTPEEV 925
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
135-215 |
3.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 135 ADRNIDELSGGQRQ------RVWIAMALAQQTDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVmVLHDINLSARy 208
Cdd:PRK03918 782 KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVII-VSHDEELKDA- 859
|
....*..
gi 1752086653 209 ADYLFTV 215
Cdd:PRK03918 860 ADYVIRV 866
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-200 |
3.71e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 3.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752086653 133 EFADRNIDELSGGQRQRVWIAMALAQQTDILFLDEPTTYLDITyqvEILDLLTDLNKrYGTTIVMVLH 200
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH---AVLWLETYLLK-WPKTFIVVSH 399
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
6-57 |
6.20e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 6.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1752086653 6 FETKNIQSgYDNKTILNDVNLSIPSNQISIIIGANGCGKSTLLKTMARLIKP 57
Cdd:COG1106 5 FSIENFRS-FKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNL 55
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-196 |
1.34e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 21 LNDVNLSIPSNqISIIIGANGCGKSTLLKTMARLIKPT------------GGDVLLDGKSI----------------HKM 72
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSssrkfdeedfylGDDPDLPEIEIeltfgsllsrllrlllKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 73 APKQLAKVLGLLpQSPIVPEGITVADLV---GRGRFPHQSVMKGWSKKDYEAVAEALEMMnITEFADRNIDELSGGQRQr 149
Cdd:COG3593 93 DKEELEEALEEL-NEELKEALKALNELLseyLKELLDGLDLELELSLDELEDLLKSLSLR-IEDGKELPLDRLGSGFQR- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086653 150 vWIAMALAQQ---------TDILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIV 196
Cdd:COG3593 170 -LILLALLSAlaelkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-216 |
1.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 140 DELSGGQRQ------RVWIAMALAQQTD------ILFLDEPTTYLDITYQVEILDLLTDLNKRYGTTIVMVLHDINLSAR 207
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEGIEgdaplpPLILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELVGA 859
|
....*....
gi 1752086653 208 yADYLFTVK 216
Cdd:PRK02224 860 -ADDLVRVE 867
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-230 |
1.60e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086653 136 DRNIDELSGGQRQRVWIAMAL-AQQTDILF-LDEPTTYL---DITYQVEILDLLTDLnkryGTTIVMVLHD---InlsaR 207
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLATQIgSGLVGVLYvLDEPSIGLhqrDNDRLIETLKRLRDL----GNTVIVVEHDedtI----R 551
|
90 100
....*....|....*....|....*....
gi 1752086653 208 YADYLFT------VKNGQLIAEGAPIEII 230
Cdd:COG0178 552 AADYIIDigpgagEHGGEVVAQGTPEEIL 580
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
30-83 |
1.73e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.92 E-value: 1.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086653 30 SNQISIIIGANGCGKSTLLKTMARLIKPTGGDVLLdgksihkMAP-----KQLAKVLGL 83
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVL-------AAPtgkaaKRLSESTGI 62
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
23-55 |
1.99e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 1.99e-03
10 20 30
....*....|....*....|....*....|...
gi 1752086653 23 DVNLSIPSNqISIIIGANGCGKSTLLKTMARLI 55
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTLLEAIALAL 49
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
16-52 |
6.08e-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: 6.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1752086653 16 DNKTILNDVNLSipSNQISIIIGANGCGKSTLLKTMA 52
Cdd:cd03243 16 GETFVPNDINLG--SGRLLLITGPNMGGKSTYLRSIG 50
|
|
| |
