|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
43-300 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 560.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 43 SKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIY 122
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 123 DPNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAYGPKLHGLaRDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQ 202
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGI-KSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 203 QRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|....*...
gi 447014717 283 FTQPDHQLTEAYITGRFG 300
Cdd:COG1117 241 FTNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
52-299 |
1.67e-167 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 464.46 E-value: 1.67e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 52 KISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNLDVVLL 131
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPKSIFDNVAYGPKLHGLaRDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTI 211
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGI-KDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 212 AVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLT 291
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239
|
....*...
gi 447014717 292 EAYITGRF 299
Cdd:TIGR00972 240 EDYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
53-282 |
7.32e-144 |
|
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: 403.87 E-value: 7.32e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNLDVVLLR 132
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFPKSIFDNVAYGPKLHGLaRDKYDLEEIVENSLRKAGLWEEVKDRLNqpGTGLSGGQQQRLCIARTIA 212
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
43-300 |
9.05e-141 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 397.62 E-value: 9.05e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 43 SKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIY 122
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 123 DPNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAYGPKLHGLardKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQ 202
Cdd:PRK14243 81 APDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGY---KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 203 QRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHL---------GDL 273
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYL 237
|
250 260
....*....|....*....|....*..
gi 447014717 274 IEVNSTEKVFTQPDHQLTEAYITGRFG 300
Cdd:PRK14243 238 VEFDRTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
49-300 |
1.28e-126 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 361.02 E-value: 1.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 49 TEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNLDV 128
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLLRAQVGMVFQKPNPFPKSIFDNVAYGPKLHGLaRDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIA 208
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI-KDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDH 288
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
250
....*....|..
gi 447014717 289 QLTEAYITGRFG 300
Cdd:PRK14239 241 KETEDYISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-300 |
1.22e-110 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 320.64 E-value: 1.22e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNLDVVLLR 132
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTI 211
Cdd:PRK14267 85 REVGMVFQYPNPFPHlTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 212 AVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLT 291
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 447014717 292 EAYITGRFG 300
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
52-298 |
1.00e-98 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 290.28 E-value: 1.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 52 KISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYdpNLDVVLL 131
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIART 210
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQL 290
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*...
gi 447014717 291 TEAYITGR 298
Cdd:PRK14247 241 TEKYVTGR 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
53-300 |
3.85e-93 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 276.53 E-value: 3.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNLDVVLLR 132
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFPKSIFDNVAYGPKLHGLaRDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIA 212
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGW-RPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELIS--ELSDQYTIVIVTHSMQQAARVSDRTAYFH-----LGDLIEVNSTEKVFTQ 285
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNS 246
|
250
....*....|....*
gi 447014717 286 PDHQLTEAYITGRFG 300
Cdd:PRK14258 247 PHDSRTREYVLSRLG 261
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
53-295 |
4.06e-81 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 244.90 E-value: 4.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVVLLR 132
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL-EEPDS----GTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFP-KSIFDNVAYGP-KLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQ-PGTgLSGGQQQRLCIAR 209
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPiKVKKMSKA--EAEERAMELLERVGL----ADKADAyPAQ-LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDH 288
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
....*..
gi 447014717 289 QLTEAYI 295
Cdd:COG1126 230 ERTRAFL 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-298 |
2.12e-78 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 238.79 E-value: 2.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 59 HVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKITLDNKNIYdpNLDVVLLRAQVGM 137
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF--QIDAIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 138 VFQKPNPFPK-SIFDNVAYGPKLHGLaRDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPE 216
Cdd:PRK14246 95 VFQQPNPFPHlSIYDNIAYPLKSHGI-KEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 217 VILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYIT 296
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVI 253
|
..
gi 447014717 297 GR 298
Cdd:PRK14246 254 GR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
80-300 |
1.75e-75 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 232.29 E-value: 1.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 80 VIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNlDVVLLRAQVGMVFQKPNPFPKSIFDNVAYGPKL 159
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 160 HGLARDKyDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELI 239
Cdd:PRK14271 128 HKLVPRK-EFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 240 SELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYITGRFG 300
Cdd:PRK14271 207 RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
53-271 |
2.10e-67 |
|
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: 209.31 E-value: 2.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVVLLR 132
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-EEPDS----GTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFP-KSIFDNVAYGP-KLHGlaRDKYDLEEIVENSLRKAGLweevKDRLNQ-PGTgLSGGQQQRLCIAR 209
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPiKVKG--MSKAEAEERALELLEKVGL----ADKADAyPAQ-LSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELS-DQYTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAeEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
39-295 |
4.84e-64 |
|
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: 209.76 E-value: 4.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 39 EPHASKKPNSTEIKISAQDAHVYY-----GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGK 113
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL-LRPTS----GS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 114 ITLDNKNIYD-PNLDVVLLRAQVGMVFQKP----NPFpKSIFDNVAYGPKLHGLARDKyDLEEIVENSLRKAGLWEEVKD 188
Cdd:COG1123 322 ILFDGKDLTKlSRRSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRA-ERRERVAELLERVGLPPDLAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 189 RLnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTA 266
Cdd:COG1123 400 RY--PHE-LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVA 476
|
250 260
....*....|....*....|....*....
gi 447014717 267 YFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANPQHPYTRALL 505
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
53-287 |
2.30e-59 |
|
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: 189.08 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYY-GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndtidGC--RVTGKITLDNKNIYDPNLdvV 129
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-------GLlkPTSGEVLVDGKDITKKNL--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQVGMVFQkpNP----FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRlnQPGTgLSGGQQQRL 205
Cdd:COG1122 72 ELRRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGLPRE--EIRERVEEALELVGL-EHLADR--PPHE-LSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
...
gi 447014717 285 QPD 287
Cdd:COG1122 224 DYE 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
62-271 |
2.03e-57 |
|
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: 182.39 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVVLLRAQVGMVFQK 141
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDS----GSILIDGEDLTDLEDELPPLRRRIGMVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFP-KSIFDNVAYGpklhglardkydleeivenslrkaglweevkdrlnqpgtgLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:cd03229 85 FALFPhLTVLENIALG----------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
47-264 |
5.35e-57 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 184.14 E-value: 5.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 47 NSTEIKISAQDAHVYY----GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT---LnrmnDTIDGcrvtGKITLDNK 119
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagL----EKPTS----GEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 120 NIYDPNLDVvllraqvGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDKYdlEEIVENSLRKAGLwEEVKDRLnqPGTgLS 198
Cdd:COG1116 74 PVTGPGPDR-------GVVFQEPALLPwLTVLDNVALGLELRGVPKAER--RERARELLELVGL-AGFEDAY--PHQ-LS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 199 GGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLADR 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
53-264 |
2.23e-56 |
|
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: 181.13 E-value: 2.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNldv 128
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL-ERPTS----GEVLVDGEPVTGPG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vllrAQVGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQ-PGTgLSGGQQQRLC 206
Cdd:cd03293 73 ----PDRGYVFQQDALLPwLTVLDNVALGLELQGVPKA--EARERAEELLELVGL----SGFENAyPHQ-LSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 207 IARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADR 201
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
53-286 |
8.48e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 178.75 E-value: 8.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT---LnrmnDTIDGcrvtGKITLDNKNIYD--PNld 127
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagF----ETPDS----GRILLDGRDVTGlpPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 vvllRAQVGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLC 206
Cdd:COG3842 76 ----KRNVGMVFQDYALFPhLTVAENVAFGLRMRGVPKA--EIRARVAELLELVGL-EGLADRY--PHQ-LSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 207 IARTIAVSPEVILMDEPCSALDpiatAKV-EELISELSD-----QYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTE 280
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALD----AKLrEEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
....*.
gi 447014717 281 KVFTQP 286
Cdd:COG3842 222 EIYERP 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
53-265 |
9.41e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.23 E-value: 9.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIydPNLDVVLLR 132
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-DPPTS----GEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFPKSIFDNVAYGPKLHGLARDkydlEEIVENSLRKAGLWEEVkdrLNQPGTGLSGGQQQRLCIARTIA 212
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRERKFD----RERALELLERLGLPPDI---LDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRT 265
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRV 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
62-271 |
1.16e-53 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 173.81 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFE--AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNKNIYDpnLDVVLLRAQVGMVF 139
Cdd:cd03225 9 YPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT-----SGEVLVDGKDLTK--LSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWeevkDRLNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:cd03225 82 QNPDDqfFGPTVEEEVAFGLENLGLPEE--EIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
62-276 |
2.06e-53 |
|
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: 173.47 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIydpnLDVVLLRAQVGMVFQK 141
Cdd:cd03259 10 YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-ERPDS----GEILIDGRDV----TGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:cd03259 81 YALFPhLTVAENIAFGLKLRGVPKA--EIRARVRELLELVGL-EGLLNRY--PHE-LSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEV 276
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
62-289 |
3.98e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 171.04 E-value: 3.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVVLLRAQVGMVFQK 141
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-EEITS----GDLIVDGLKVNDPKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPK-SIFDNVAYGP-KLHGLARDkyDLEEIVENSLRKAGLWEevkdRLNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:PRK09493 86 FYLFPHlTALENVMFGPlRVRGASKE--EAEKQARELLAKVGLAE----RAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQ 289
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
53-275 |
6.20e-52 |
|
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: 169.99 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYY----GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIYDPNLDV 128
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLLR-AQVGMVFQKP----NPFpKSIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRL-NQpgtgLSGGQQ 202
Cdd:cd03257 77 RKIRrKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYpHE----LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 203 QRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
48-287 |
2.59e-51 |
|
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: 169.00 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 48 STEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT---LNRmndtIDgcrvTGKITLDNKNIYDP 124
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLiigLLR----PD----SGEILVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 125 NLD-VVLLRAQVGMVFQKPNPF-PKSIFDNVAYGPKLHG-LARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGtGLSGGQ 201
Cdd:COG1127 73 SEKeLYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTdLSEA--EIRELVLEKLELVGL-PGAADKM--PS-ELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 202 QQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNST 279
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
....*...
gi 447014717 280 EKVFTQPD 287
Cdd:COG1127 227 EELLASDD 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
53-290 |
4.42e-51 |
|
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: 168.06 E-value: 4.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT---LNRmndtidgcRVTGKITLDNKNIYDPNLDVV 129
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLivgLLR--------PDSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 L-LRAQVGMVFQKPNPF-PKSIFDNVAYGPKLHGlARDKYDLEEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCI 207
Cdd:cd03261 73 YrLRRRMGMLFQSGALFdSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGL-RGAEDLY--PAE-LSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
....*
gi 447014717 286 PDHQL 290
Cdd:cd03261 228 DDPLV 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
53-287 |
4.72e-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: 175.48 E-value: 4.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYY--GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtiDGCRVTGKITLDNKNIYDpnLDVVL 130
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP--HGGRISGEVLLDGRDLLE--LSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMVFQKP--NPFPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIA 208
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRA--EARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
.
gi 447014717 287 D 287
Cdd:COG1123 235 Q 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
53-294 |
3.30e-50 |
|
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: 166.37 E-value: 3.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNKNIYDpnLDVVLLR 132
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDLAS--LSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPN-PFPKSIFDNVAYG--PKLHGLARDKYDLEEIVENSLRKAGLwEEVKDR-LNQpgtgLSGGQQQRLCIA 208
Cdd:COG1120 75 RRIAYVPQEPPaPFGLTVRELVALGryPHLGLFGRPSAEDREAVEEALERTGL-EHLADRpVDE----LSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTqP 286
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT-P 228
|
....*...
gi 447014717 287 DHqLTEAY 294
Cdd:COG1120 229 EL-LEEVY 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
63-295 |
5.16e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 168.72 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdtidgcRVT-GKITLDNKNIYD-PNLDVVLLRAQVGMVFQ 140
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE------RPTsGSVLVDGVDLTAlSERELRAARRKIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:COG1135 90 HFNLLSsRTVAENVALPLEIAGVPKA--EIRKRVAELLELVGLSDKADAYPSQ----LSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
53-269 |
1.29e-49 |
|
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: 163.81 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndTIDgcRVT-GKITLDNKNIYDPNLD 127
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLD--RPTsGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 --VVLLRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQR 204
Cdd:cd03255 75 elAAFRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKK--ERRERAEELLERVGL----GDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMqQAARVSDRTAYFH 269
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELR 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
53-295 |
1.42e-49 |
|
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: 164.59 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYG----DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDV 128
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-----WSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vlLRAQVGMVFQKP----NPFpKSIFDNVAYGPKLHGLArdkyDLEEIVENSLRKAGLWEEVKDRLnqPGTgLSGGQQQR 204
Cdd:COG1124 77 --FRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLP----DREERIAELLEQVGLPPSFLDRY--PHQ-LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*..
gi 447014717 283 FTQPDH----QLTEAYI 295
Cdd:COG1124 227 LAGPKHpytrELLAASL 243
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
46-287 |
1.63e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 164.97 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 46 PNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrMNDTIDgcrvTGKITLDNKNI-YDP 124
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCIN-LLETPD----SGEIRVGGEEIrLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 125 NLD----------VVLLRAQVGMVFQKPNPFP-KSIFDNVAYGPkLHGLARDKYDLEEIVENSLRKAGLWeevkDRLNQP 193
Cdd:COG4598 77 DRDgelvpadrrqLQRIRTRLGMVFQSFNLWShMTVLENVIEAP-VHVLGRPKAEAIERAEALLAKVGLA----DKRDAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 194 GTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGD 272
Cdd:COG4598 152 PAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEgRTMLVVTHEMGFARDVSSHVVFLHQGR 231
|
250
....*....|....*
gi 447014717 273 LIEVNSTEKVFTQPD 287
Cdd:COG4598 232 IEEQGPPAEVFGNPK 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
53-275 |
2.42e-49 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 163.29 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidGC--RVT-GKITLDNKNIY--- 122
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL--------GGldRPTsGEVLIDGQDISsls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 123 DPNLDvvLLRAQ-VGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGG 200
Cdd:COG1136 77 ERELA--RLRRRhIGFVFQFFNLLPElTALENVALPLLLAGVSRK--ERRERARELLERVGL----GDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 201 QQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARvSDRTAYFHLGDLIE 275
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
53-298 |
1.59e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVvllR 132
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL-LRPTS----GEVRVLGEDVARDPAEV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLWeevkDRLNQPGTGLSGGQQQRLCIARTI 211
Cdd:COG1131 73 RRIGYVPQEPALYPDlTVRENLRFFARLYGL--PRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 212 AVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVftqPDHQL 290
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL---KARLL 223
|
250
....*....|
gi 447014717 291 TEAYI--TGR 298
Cdd:COG1131 224 EDVFLelTGE 233
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
60-286 |
2.47e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 163.34 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMND-TidgcrvTGKITLDNKNIYDpnLDVVLLRAQVGMV 138
Cdd:COG1125 10 RYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEpT------SGRILIDGEDIRD--LDPVELRRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 FQKPNPFP-KSIFDNVAYGPKLHGLARDKYDleEIVENSLRKAGLW-EEVKDRL-NQpgtgLSGGQQQRLCIARTIAVSP 215
Cdd:COG1125 82 IQQIGLFPhMTVAENIATVPRLLGWDKERIR--ARVDELLELVGLDpEEYRDRYpHE----LSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:COG1125 156 PILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
53-286 |
3.74e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 163.78 E-value: 3.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT---LnrmnDTIDgcrvTGKITLDNKNIYdpnLDVV 129
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagL----ETPD----SGRIVLNGRDLF---TNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQVGMVFQKPNPFPK-SIFDNVAYGpkLHGLARDKYDLEEIVENSLRKAGLwEEVKDRL-NQpgtgLSGGQQQRLCI 207
Cdd:COG1118 72 PRERRVGFVFQHYALFPHmTVAENIAFG--LRVRPPSKAEIRARVEELLELVQL-EGLADRYpSQ----LSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 208 ARTIAVSPEVILMDEPCSALDpiatAKV----EELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEK 281
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALD----AKVrkelRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
....*
gi 447014717 282 VFTQP 286
Cdd:COG1118 221 VYDRP 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
60-295 |
5.17e-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: 5.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDpnLDVVLLRAQVGMVF 139
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-----TSGEIFIDGEDIRE--QDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFP-KSIFDNVAYGPKLHGLARDKYDleEIVENSLRKAGLWE-EVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEV 217
Cdd:cd03295 82 QQIGLFPhMTVEENIALVPKLLKWPKEKIR--ERADELLALVGLDPaEFADRY--PHE-LSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
53-286 |
9.32e-48 |
|
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: 159.67 E-value: 9.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDgcrvTGKITLDNKNIYD-PNLD 127
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPT----SGSVLVDGTDLTLlSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 VVLLRAQVGMVFQKPNPF-PKSIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLC 206
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGVPKAE--IEERVLELLELVGLEDKADAYPAQ----LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 207 IARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
..
gi 447014717 285 QP 286
Cdd:cd03258 231 NP 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
68-295 |
1.92e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.83 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLD-NKNIYDPNLDVVLLRAQVGMVFQKPNPFP 146
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtARSLSQQKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 -KSIFDNVAYGPKL-HGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK11264 99 hRTVLENIIEGPVIvKGEPKE--EATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 225 SALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
65-287 |
7.79e-46 |
|
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: 156.07 E-value: 7.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNR-MNDTidgcrvTGKITLDNKNIY-DPNLDVVLLRAQVGMVFQKP 142
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT------SGTVTIDGRDITaKKKKKLKDLRKKVGLVFQFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 NP--FPKSIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLWEEVKDRlnQPGTgLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:TIGR04521 92 EHqlFEETVYKDIAFGPKNLGL--SEEEAEERVKEALELVGLDEEYLER--SPFE-LSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
53-288 |
8.04e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.93 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT---LnrmnDTIDGcrvtGKITLDNKniydpnlDVV 129
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagL----EDPTS----GEILIGGR-------DVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQ---VGMVFQkpNP--FP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQ 203
Cdd:COG3839 69 DLPPKdrnIAMVFQ--SYalYPhMTVYENIAFPLKLRKVPKA--EIDRRVREAAELLGL-EDLLDRK--PKQ-LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 204 RLCIARTIAVSPEVILMDEPCSALDpiatAKV-EELISELSD-----QYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVN 277
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLD----AKLrVEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
250
....*....|.
gi 447014717 278 STEKVFTQPDH 288
Cdd:COG3839 217 TPEELYDRPAN 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
62-286 |
1.01e-45 |
|
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: 154.32 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYD--PNldvvllRAQVGMVF 139
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-ETPTS----GEILLDGKDITNlpPH------KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFPK-SIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVI 218
Cdd:cd03300 79 QNYALFPHlTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
67-297 |
1.09e-45 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 158.09 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtIDGCRvtGKITLDNKNI--YDPNLDVVLLRAQVGMVFQKPNP 144
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRL---IEPTA--GQIFIDGENImkQSPVELREVRRKKIGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 145 FP-KSIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLwEEVKDRLNQPgtgLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:TIGR01186 83 FPhMTILQNTSLGPELLGW--PEQERKEKALELLKLVGL-EEYEHRYPDE---LSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 224 CSALDPIATAKVEELISELSD--QYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYITG 297
Cdd:TIGR01186 157 FSALDPLIRDSMQDELKKLQAtlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
61-253 |
1.13e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.26 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcrVT-GKITLDNKNIYDPNLDVvlLRAQVGMVF 139
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD------PTsGRILIDGVDIRDLTLES--LRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFPKSIFDNVAYGpklhglaRDKYDLEEIVEnSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIARTIA 212
Cdd:COG1132 421 QDTFLFSGTIRENIRYG-------RPDATDEEVEE-AAKAAQAHEFIEAlpdgydtVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
53-288 |
4.10e-45 |
|
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: 155.21 E-value: 4.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYY----GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtiDGCRVTGKITLDNKNIYDpnLDV 128
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--PPGITSGEILFDGEDLLK--LSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLLRA----QVGMVFQKP----NPFpKSIFDNVAYGPKLHGLARDKyDLEEIVENSLRKAGLwEEVKDRLNQ-PGTgLSG 199
Cdd:COG0444 78 KELRKirgrEIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKA-EARERAIELLERVGL-PDPERRLDRyPHE-LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 200 GQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVN 277
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|.
gi 447014717 278 STEKVFTQPDH 288
Cdd:COG0444 234 PVEELFENPRH 244
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
60-264 |
9.60e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 152.13 E-value: 9.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtIDGcrvtGKITLDNKNIydPNL---DVVLLRAQVG 136
Cdd:COG3638 11 RYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE-PTS----GEILVDGQDV--TALrgrALRRLRRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 137 MVFQKPNPFPK-SIFDNV-----AYGPKLHGLARdKYDLEEIVE--NSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIA 208
Cdd:COG3638 84 MIFQQFNLVPRlSVLTNVlagrlGRTSTWRSLLG-LFPPEDRERalEALERVGL----ADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYADR 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-286 |
2.69e-44 |
|
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: 151.64 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 38 FEPHASKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtIDGCRvtGKITLD 117
Cdd:cd03294 10 FGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL---IEPTS--GKVLID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 118 NKNIydPNLDVVLLRA----QVGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDKYdlEEIVENSLRKAGL--WEEVKdrl 190
Cdd:cd03294 85 GQDI--AAMSRKELRElrrkKISMVFQSFALLPhRTVLENVAFGLEVQGVPRAER--EERAAEALELVGLegWEHKY--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 191 nqPGTgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSD--QYTIVIVTHSMQQAARVSDRTAYF 268
Cdd:cd03294 158 --PDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGDRIAIM 234
|
250
....*....|....*...
gi 447014717 269 HLGDLIEVNSTEKVFTQP 286
Cdd:cd03294 235 KDGRLVQVGTPEEILTNP 252
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
68-225 |
4.42e-44 |
|
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: 147.41 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNKNIYDPNLDvvLLRAQVGMVFQKPNPFP- 146
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDDERK--SLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 147 KSIFDNVAYGPKLHGLARDKYDleEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKD--ARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
66-253 |
7.64e-44 |
|
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: 158.84 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIydPNLDVVLLRAQVGMVFQKPNPF 145
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP-----TSGRILIDGIDL--RQIDPASLRRQIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PKSIFDNVAygpklhgLARDKYDLEEIVEnSLRKAGLWEEVK---DRLNQP----GTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:COG2274 562 SGTIRENIT-------LGDPDATDEEIIE-AARLAGLHDFIEalpMGYDTVvgegGSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190
....*....|....*....|....*....|....*
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
53-294 |
5.34e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 5.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIYDPnldvvllR 132
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-----PTSGTVRLFGKPPRRA-------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPN---PFPKSIFDNVAYG--PKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCI 207
Cdd:COG1121 75 RRIGYVPQRAEvdwDFPITVRDVVLMGryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHlGDLIEVNSTEKVFTQP 286
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPE 229
|
....*...
gi 447014717 287 DhqLTEAY 294
Cdd:COG1121 230 N--LSRAY 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
53-264 |
3.10e-42 |
|
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: 143.29 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDF--EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVvl 130
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-----TSGEILIDGVDLRDLDLES-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMVFQKPNPFPKSIFDNVaygpklhglardkydleeivenslrkaglweevkdrlnqpgtgLSGGQQQRLCIART 210
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVsDR 264
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA-DR 163
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
49-297 |
1.20e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 144.73 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 49 TEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIY-----D 123
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG-----SIVVNGQTINlvrdkD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 124 PNLDVV------LLRAQVGMVFQKPNPFPK-SIFDNVAYGPkLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNqpgTG 196
Cdd:PRK10619 77 GQLKVAdknqlrLLRTRLTMVFQHFNLWSHmTVLENVMEAP-IQVLGLSKQEARERAVKYLAKVGIDERAQGKYP---VH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 197 LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250 260
....*....|....*....|..
gi 447014717 276 VNSTEKVFTQPDHQLTEAYITG 297
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQFLKG 254
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
60-293 |
1.37e-41 |
|
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: 143.86 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMND------TIDGCRVTGKITLDNKNiydpnldvvlLRA 133
Cdd:cd03256 9 TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEptsgsvLIDGTDINKLKGKALRQ----------LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 QVGMVFQKPNPFPK-SIFDNV-----AYGPKLHGLARdKYDLEEIVE--NSLRKAGLweevKDRLNQPGTGLSGGQQQRL 205
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVlsgrlGRRSTWRSLFG-LFPKEEKQRalAALERVGL----LDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISEL--SDQYTIVIVTHSMQQAARVSDRtayfhlgdLIEVNSTEKVF 283
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADR--------IVGLKDGRIVF 225
|
250
....*....|
gi 447014717 284 TQPDHQLTEA 293
Cdd:cd03256 226 DGPPAELTDE 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
67-287 |
2.21e-41 |
|
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: 144.11 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKITLDNKNIYDpnldvvlLRAQVGMVFQKP-NP 144
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGkVTVDGLDTLDEENLWE-------IRKKVGMVFQNPdNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 145 FPKSIF-DNVAYGPKLHGLARDKydLEEIVENSLRKAGLWeevkDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:TIGR04520 90 FVGATVeDDVAFGLENLGVPREE--MRKRVDEALKLVGME----DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 224 CSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:TIGR04520 164 TSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
42-275 |
2.22e-41 |
|
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: 150.29 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 42 ASKKPNSTEIKISAQDAHVYYGD-FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNKN 120
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 121 IydPNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAygpklhgLARDKYDLEEIVEnSLRKAGLWEEVK---DRLNQP---- 193
Cdd:COG4988 401 L--SDLDPASWRRQIAWVPQNPYLFAGTIRENLR-------LGRPDASDEELEA-ALEAAGLDEFVAalpDGLDTPlgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 194 GTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARvSDRTAYFHLGDL 273
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRI 549
|
..
gi 447014717 274 IE 275
Cdd:COG4988 550 VE 551
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
54-271 |
9.33e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 138.92 E-value: 9.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 54 SAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIydPNLDVVLLRA 133
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 QVGMVFQkpnpfpksifdnvaygpklhglardkydleeivenslrkaglweevkdrlnqpgtgLSGGQQQRLCIARTIAV 213
Cdd:cd00267 74 RIGYVPQ--------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
60-295 |
5.04e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 142.63 E-value: 5.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMND------TIDGCRVTgkiTLDNKniydpnlDVVLLRA 133
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERptsgrvLVDGQDLT---ALSEK-------ELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 QVGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIA 212
Cdd:PRK11153 83 QIGMIFQHFNLLSsRTVFDNVALPLELAGTPKA--EIKARVTELLELVGL-SDKADRY--PAQ-LSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQL 290
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
....*
gi 447014717 291 TEAYI 295
Cdd:PRK11153 237 TREFI 241
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
53-253 |
5.54e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.03 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYY-GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtidgCRVT-GKITLDNKNIYD-PNLDVV 129
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE------ERPTsGQVLVNGQDLSRlKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQVGMVFQK----PNpfpKSIFDNVAYGPKLHGlaRDKYDLEEIVENSLRKAGLweevKDRLNQ-PGTgLSGGQQQR 204
Cdd:COG2884 76 YLRRRIGVVFQDfrllPD---RTVYENVALPLRVTG--KSRKEIRRRVREVLDLVGL----SDKAKAlPHE-LSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTH 253
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATH 195
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
62-286 |
9.33e-40 |
|
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: 139.01 E-value: 9.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDvvllRAQVGMVFQK 141
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSG-----TILFGGEDATDVPVQ----ERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPK-SIFDNVAYGPKLHGLAR--DKYDLEEIVENSLRKAGLwEEVKDRL-NQpgtgLSGGQQQRLCIARTIAVSPEV 217
Cdd:cd03296 83 YALFRHmTVFDNVAFGLRVKPRSErpPEAEIRAKVHELLKLVQL-DWLADRYpAQ----LSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 218 ILMDEPCSALDpiatAKV-EEL---ISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:cd03296 158 LLLDEPFGALD----AKVrKELrrwLRRLHDElhVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
60-296 |
1.34e-39 |
|
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: 138.59 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPN-LDVVLLRAQVGMV 138
Cdd:TIGR02315 10 VYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-----SSGSILLEGTDITKLRgKKLRKLRRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 FQKPNPFP-KSIFDNV-----AYGPKLHGLARdKYDLEEIVE--NSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIART 210
Cdd:TIGR02315 85 FQHYNLIErLTVLENVlhgrlGYKPTWRSLLG-RFSEEDKERalSALERVGLADKAYQRADQ----LSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISELS--DQYTIVIVTHSMQQAARVSDRtayfhlgdLIEVNSTEKVFTQPDH 288
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINkeDGITVIINLHQVDLAKKYADR--------IVGLKAGEIVFDGAPS 231
|
....*...
gi 447014717 289 QLTEAYIT 296
Cdd:TIGR02315 232 ELDDEVLR 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
53-282 |
2.08e-39 |
|
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: 137.95 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdtidgcRVT-GKITLDNKNI--YDPNLdvv 129
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL------RPTsGSVLFDGEDItgLPPHE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 llRAQVGMV--FQKPNPFPK-SIFDNVA--------YGPKLHGLARDKYDLEEIVENSLRKAGLWeevkDRLNQPGTGLS 198
Cdd:cd03219 72 --IARLGIGrtFQIPRLFPElTVLENVMvaaqartgSGLLLARARREEREARERAEELLERVGLA----DLADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 199 GGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLI--- 274
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVIaeg 225
|
250
....*....|.
gi 447014717 275 ---EVNSTEKV 282
Cdd:cd03219 226 tpdEVRNNPRV 236
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
53-287 |
2.43e-39 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 140.94 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIYD--PNldvvl 130
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLER-----QTAGTIYQGGRDITRlpPQ----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 lRAQVGMVFQKPNPFPK-SIFDNVAYGpkLHGLARDKYDLEEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIAR 209
Cdd:TIGR03265 75 -KRDYGIVFQSYALFPNlTVADNIAYG--LKNRGMGRAEVAERVAELLDLVGL-PGSERKY--PGQ-LSGGQQQRVALAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 210 TIAVSPEVILMDEPCSALDpiatAKV-EELISELSD-----QYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVF 283
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALD----ARVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
....
gi 447014717 284 TQPD 287
Cdd:TIGR03265 224 RHPA 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
53-267 |
5.35e-39 |
|
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: 136.41 E-value: 5.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIydPNLDV-VLL 131
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDI--TGLPPhERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDLEEIVEnslrkagLWEEVKDRLNQPGTGLSGGQQQRLCIART 210
Cdd:cd03224 74 RAGIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRtAY 267
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADR-AY 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
66-287 |
7.01e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 138.26 E-value: 7.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVVLLRAQVGMVFQKP--N 143
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP-----TSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPeyQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 PFPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGL-WEEVKDRlnQPgTGLSGGQQQRLCIARTIAVSPEVILMDE 222
Cdd:PRK13637 96 LFEETIEKDIAFGPINLGLSEE--EIENRVKRAMNIVGLdYEDYKDK--SP-FELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 223 PCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
61-286 |
8.43e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 136.68 E-value: 8.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDPNlDVVLLRAQVGMVFQ 140
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEK-AIRLLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPK-SIFDNVAYGP-KLHGL----ARDKYDleEIVEnSLR---KAGLWeevkdrlnqPgTGLSGGQQQRLCIARTI 211
Cdd:COG4161 90 QYNLWPHlTVMENLIEAPcKVLGLskeqAREKAM--KLLA-RLRltdKADRF---------P-LHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 212 AVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEvNSTEKVFTQP 286
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHFTQP 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
41-264 |
9.87e-39 |
|
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: 143.37 E-value: 9.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 41 HASKKPNSTEIKISAQDAHVYY--GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDN 118
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-----QSGSITLGG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 119 KNIYDPNLDVvlLRAQVGMVFQKPNPFPKSIFDNVAygpklhgLARDKYDLEEIVEnSLRKAGL--W-EEVKDRLNQP-- 193
Cdd:COG4987 397 VDLRDLDEDD--LRRRIAVVPQRPHLFDTTLRENLR-------LARPDATDEELWA-ALERVGLgdWlAALPDGLDTWlg 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 194 --GTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVsDR 264
Cdd:COG4987 467 egGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DR 538
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
53-294 |
1.03e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.30 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtiDGCRvTGKITLDNkNIYD----PNL-D 127
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL----EMPR-SGTLNIAG-NHFDfsktPSDkA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 VVLLRAQVGMVFQKPNPFPK-SIFDNVAYGP-KLHGLARD--KYDLEEIVEnSLRkaglWEEVKDRLNQPgtgLSGGQQQ 203
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPHlTVQQNLIEAPcRVLGLSKDqaLARAEKLLE-RLR----LKPYADRFPLH---LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 204 RLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEvNSTEKV 282
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVE-QGDASC 227
|
250
....*....|..
gi 447014717 283 FTQPDhqlTEAY 294
Cdd:PRK11124 228 FTQPQ---TEAF 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
53-271 |
2.68e-38 |
|
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: 132.91 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTL--NRMNDTidgcrvtGKITLDNKNIYDPNLDVvl 130
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgLLKPDS-------GEIKVLGKDIKKEPEEV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 lRAQVGMVFQKPNPFPK-SIFDNVAYgpklhglardkydleeivenslrkaglweevkdrlnqpgtglSGGQQQRLCIAR 209
Cdd:cd03230 72 -KRRIGYLPEEPSLYENlTVRENLKL------------------------------------------SGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY-TIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNG 171
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
67-293 |
3.87e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 137.17 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPN-LDVVLLRAQVGMVFQKP--- 142
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSG-----EILFDGQDITGLSgRELRPLRRRMQMVFQDPyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 -NPfPKSIFDNVAYGPKLHGLArDKYDLEEIVENSLRKAGLWEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:COG4608 108 lNP-RMTVGDIIAEPLRIHGLA-SKAERRERVAELLELVGLRPEHADRY--PHE-FSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 222 EPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEA 293
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQA 256
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
62-286 |
4.56e-38 |
|
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: 134.39 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEaIKGIDLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDGCRV--TGKITLDNKNIYDPNLDvvllRAQVGMVF 139
Cdd:cd03299 10 WKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLL-------ETIAGFIKpdSGKILLNGKDITNLPPE----KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFP-KSIFDNVAYGPKLhgLARDKYDLEEIVENSLRKAGLwEEVKDRlnQPGTgLSGGQQQRLCIARTIAVSPEVI 218
Cdd:cd03299 78 QNYALFPhMTVYKNIAYGLKK--RKVDKKEIERKVLEIAEMLGI-DHLLNR--KPET-LSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
49-292 |
3.00e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.60 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 49 TEIKISAQDAHVYYGDFE--AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDpnl 126
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 127 dvvlLRAQVGMVFQKP-NPFPKS-IFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQR 204
Cdd:PRK13635 79 ----VRRQVGMVFQNPdNQFVGAtVQDDVAFGLENIGVPRE--EMVERVDQALRQVGM----EDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKV 282
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
250
....*....|
gi 447014717 283 FTQpDHQLTE 292
Cdd:PRK13635 228 FKS-GHMLQE 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
62-295 |
3.80e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.80 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFeaIKGIDLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDGCRV--TGKITLDNKNI--YDPnldvvllrAQ--V 135
Cdd:COG3840 11 YGDF--PLRFDLTIAAGERVAILGPSGAGKSTLL-------NLIAGFLPpdSGRILWNGQDLtaLPP--------AErpV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 136 GMVFQKPNPFPK-SIFDNVAYG--PKLHGLARDKYDLEEIvensLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIA 212
Cdd:COG3840 74 SMLFQENNLFPHlTVAQNIGLGlrPGLKLTAEQRAQVEQA----LERVGL-AGLLDRL--PGQ-LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 213 VSPEVILMDEPCSALDPiatAKVEE---LISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:COG3840 146 RKRPILLLDEPFSALDP---ALRQEmldLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
....*...
gi 447014717 288 HQLTEAYI 295
Cdd:COG3840 223 PPALAAYL 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
62-276 |
4.78e-37 |
|
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: 131.22 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtIDGcrvtGKITLDNKniydpnlDVVLLRAQ---VGMV 138
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE-PTS----GRIYIGGR-------DVTDLPPKdrdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 FQKPNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPgTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:cd03301 78 FQNYALYPhMTVYDNIAFGLKLRKVPKD--EIDERVREVAELLQI-EHLLDRK--P-KQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 218 ILMDEPCSALDpiatAKV-EELISELSD-----QYTIVIVTHSMQQAARVSDRTAYFHLGDLIEV 276
Cdd:cd03301 152 FLMDEPLSNLD----AKLrVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
67-266 |
1.11e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 134.85 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcrVT-GKITLDNKNIYdpNLDVVLLRA----QVGMVFQK 141
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE------PTaGEVLIDGEDIT--KLSKKELRElrrkKMSMVFQH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 ----PNpfpKSIFDNVAYGPKLHGLARDKYdlEEIVENSLRKAGL--WEEVKdrlnqPGTgLSGGQQQRLCIARTIAVSP 215
Cdd:COG4175 114 fallPH---RTVLENVAFGLEIQGVPKAER--RERAREALELVGLagWEDSY-----PDE-LSGGMQQRVGLARALATDP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 216 EVILMDEPCSALDPiatakveeLI-SELSDQY---------TIVIVTHSMQQAARVSDRTA 266
Cdd:COG4175 183 DILLMDEAFSALDP--------LIrREMQDELlelqaklkkTIVFITHDLDEALRLGDRIA 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
53-264 |
2.75e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.01 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD-FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKiTLDNKNIYDpnldvvl 130
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrVKVMGR-EVNAENEKW------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMVFQKPNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEeVKDRlnqPGTGLSGGQQQRLCIA 208
Cdd:PRK13647 77 VRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLDKD--EVERRVEEALKAVRMWD-FRDK---PPYHLSYGQKKRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQ 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
64-276 |
4.64e-36 |
|
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: 129.20 E-value: 4.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDvvLLRAQVGMVFQKPN 143
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSG-----EILLDGVDIRDLNLR--WLRSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 PFPKSIFDNVAYGpklhglaRDKYDLEEIVENSlRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIARTIAVSPE 216
Cdd:cd03249 88 LFDGTIAENIRYG-------KPDATDEEVEEAA-KKANIHDFIMSlpdgydtLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 217 VILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMqQAARVSDRTAYFHLGDLIEV 276
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQ 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
61-267 |
1.66e-35 |
|
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: 126.99 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIydPNLDvvlLRAQVGMVFQ 140
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPI--KAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNP--FPKSIFDNVAYGpklhglARDKYDLEEIVENSLRKAGLWEEvKDRLNQpgtGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:cd03226 79 DVDYqlFTDSVREELLLG------LKELDAGNEQAETVLKDLDLYAL-KERHPL---SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAY 267
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLL 198
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
53-287 |
2.27e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 128.66 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD-FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDVVLL 131
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSG-----EVLIKGEPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIAR 209
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGLSKE--EVEKRVKEALKAVGM----EGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
39-293 |
2.77e-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: 133.27 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 39 EPHASKKP--NSTEIKISAQDAHVYY-----------GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTi 105
Cdd:COG4172 260 EPRGDPRPvpPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 106 dgcrvTGKITLDNKNIYDPNLDVVL-LRAQVGMVFQkpNPF----PK-SIFDNVAYGPKLHGLARDKYDLEEIVENSLRK 179
Cdd:COG4172 339 -----EGEIRFDGQDLDGLSRRALRpLRRRMQVVFQ--DPFgslsPRmTVGQIIAEGLRVHGPGLSAAERRARVAEALEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 180 AGLWEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQ 257
Cdd:COG4172 412 VGLDPAARHRY--PHE-FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAV 488
|
250 260 270
....*....|....*....|....*....|....*.
gi 447014717 258 AARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEA 293
Cdd:COG4172 489 VRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
62-280 |
4.39e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 126.33 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGkitldnkniYDPNLDVVLLRAQVGMVFQ 140
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGrATVAG---------HDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPK-SIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLWEeVKDRLNQPgtgLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:cd03265 81 DLSVDDElTGWENLYIHARLYGVPGAE--RRERIDELLDFVGLLE-AADRLVKT---YSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTE 280
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
61-253 |
1.39e-34 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 124.07 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndtiDGCRVT-GKITLDNKNIYDPNLDVVLLRAQVGMVF 139
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN------GLLRPQsGAVLIDGEPLDYSRKGLLERRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:TIGR01166 75 QDPDDqlFAADVDQDVAFGPLNLGLSEA--EVERRVREALTAVGA----SGLRERPTHCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTH 253
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTH 185
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
61-280 |
2.34e-34 |
|
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: 126.74 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGkitldnkniYDPNLDVVLLRAQVGMVF 139
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtARVAG---------YDVVREPRKVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFPK-SIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVI 218
Cdd:TIGR01188 73 QYASVDEDlTGRENLEMMGRLYGLPKDE--AEERAEELLELFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPDVL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 219 LMDEPCSALDPIATAKVEELISEL-SDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTE 280
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIRALkEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
54-268 |
2.53e-34 |
|
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: 124.18 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 54 SAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNIYDPNLDVVLLRA 133
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI------------LGLLKPTSGSIRVFGKPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 QVGMVFQKPN---PFPKSIFDNVAYG--PKLHGLARDKYDLEEIVENSLRKAGLwEEVKDRlnQPGTgLSGGQQQRLCIA 208
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGlyGHKGLFRRLSKADKAKVDEALERVGL-SELADR--QIGE-LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYF 268
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
54-267 |
2.94e-34 |
|
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: 124.32 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 54 SAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNI--YDPNlDVVll 131
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDItgLPPH-RIA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPK-SIFDN---VAYGPKlhGLARDKYDLEEIVEnslrkagLWEEVKDRLNQPGTGLSGGQQQRLCI 207
Cdd:COG0410 77 RLGIGYVPEGRRIFPSlTVEENlllGAYARR--DRAEVRADLERVYE-------LFPRLKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRtAY 267
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR-AY 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
54-274 |
1.08e-33 |
|
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: 121.39 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 54 SAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNKNIYDPNldvvllra 133
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDLASLS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 qvgmvfqkpnpfPKSIFDNVAYgpklhglardkydleeiVENSLRKAGLwEEVKDR-LNQpgtgLSGGQQQRLCIARTIA 212
Cdd:cd03214 68 ------------PKELARKIAY-----------------VPQALELLGL-AHLADRpFNE----LSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
53-258 |
1.09e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 123.82 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDF----EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLrtlNRMNDTIDgcRVTGKITLDNKNIYDPNldv 128
Cdd:COG4525 4 LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGFLA--PSSGEITLDGVPVTGPG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vllrAQVGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCI 207
Cdd:COG4525 76 ----ADRGVVFQKDALLPwLNVLDNVAFGLRLRGVPKA--ERRARAEELLALVGLADFARRRIWQ----LSGGMRQRVGI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQA 258
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
40-265 |
1.14e-33 |
|
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: 128.94 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 40 PHASKKP----NSTEIKISAQDaHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKIT 115
Cdd:TIGR02857 307 PLAGKAPvtaaPASSLEFSGVS-VAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 116 LdnkniydPNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAygpklhgLARDKYDLEEIVEnSLRKAGLWEEVKDR---LNQ 192
Cdd:TIGR02857 386 L-------ADADADSWRDQIAWVPQHPFLFAGTIAENIR-------LARPDASDAEIRE-ALERAGLDEFVAALpqgLDT 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 193 P----GTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVsDRT 265
Cdd:TIGR02857 451 PigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA-DRI 526
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
59-272 |
3.32e-33 |
|
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: 121.20 E-value: 3.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 59 HVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrMNDTIDgcrvTGKITLDNKNIYD-PNLDVVLLRAQVGM 137
Cdd:TIGR02673 9 KAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLY-GALTPS----RGQVRIAGEDVNRlRGRQLPLLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 138 VFQKPNPFP-KSIFDNVAYgpKLHGLARDKYDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPE 216
Cdd:TIGR02673 84 VFQDFRLLPdRTVYENVAL--PLEVRGKKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 217 VILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTayFHLGD 272
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRgTTVIVATHDLSLVDRVAHRV--IILDD 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
54-294 |
5.19e-33 |
|
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: 121.68 E-value: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 54 SAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNI--YDPNLdvvll 131
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF-YRPTS----GRILFDGRDItgLPPHR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMV--FQKPNPFPK-SIFDNVAYGPKLH-------------GLARDKYDLEEIVENSLRKAGLweevKDRLNQPGT 195
Cdd:COG0411 76 IARLGIArtFQNPRLFPElTVLENVLVAAHARlgrgllaallrlpRARREEREARERAEELLERVGL----ADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 196 GLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDL 273
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
250 260
....*....|....*....|.
gi 447014717 274 IEVNSTEKVFTQPDHQltEAY 294
Cdd:COG0411 232 IAEGTPAEVRADPRVI--EAY 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
53-285 |
6.85e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 122.26 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD-FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVVLL 131
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-----SSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRlnqPGTGLSGGQQQRLCIAR 209
Cdd:PRK13636 81 RESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPED--EVRKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
84-295 |
3.59e-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: 121.45 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 84 IGPSGCGKSTFLRTLNRMnDTIDgcrvTGKITLDNKNIydpnLDVVLLRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGL 162
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGF-EQPD----SGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHmTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 163 ARdkydlEEI---VENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELI 239
Cdd:TIGR01187 73 PR-----AEIkprVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 240 SELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:TIGR01187 144 KTIQEQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
40-271 |
3.61e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.36 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 40 PHASKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDgcrvTGKITLDNK 119
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-ETPD----SGRIMLDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 120 NIydpnLDVVLLRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRlnQPgTGLS 198
Cdd:PRK09452 77 DI----THVPAENRHVNTVFQSYALFPHmTVFENVAFGLRMQKTPAA--EITPRVMEALRMVQL-EEFAQR--KP-HQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 199 GGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
59-253 |
4.14e-32 |
|
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: 118.87 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 59 HVYYG---DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCrvtgkITLDNKNIYDPNLDVvlLRAQV 135
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGS-----ILIDGQDIREVTLDS--LRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 136 GMVFQKPNPFPKSIFDNVAYGpklhglaRDKYDLEEIVEnSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIA 208
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG-------RPDATDEEVIE-AAKAAQIHDKIMRfpdgydtIVGERGLKLSGGEKQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
65-287 |
5.04e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FE--AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM-NDTidgcrvTGKITLDNKNIYD--PNLDVVLLRAQVGMVF 139
Cdd:PRK13634 18 FErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPT------SGTVTIGERVITAgkKNKKLKPLRKKVGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRlnQPgTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:PRK13634 92 QFPEHqlFEETVEKDICFGPMNFGVSEE--DAKQKAREMIELVGLPEELLAR--SP-FELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 218 ILMDEPCSALDPIATAKVEELISEL--SDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
67-285 |
2.71e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKITLDNKNIYDpnldvvlLRAQVGMVFQKP-NP 144
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkVYVDGLDTSDEENLWD-------IRNKAGMVFQNPdNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 145 FPKSIFD-NVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKdrlnQPGTGLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:PRK13633 98 IVATIVEeDVAFGPENLGIPPE--EIRERVDESLKKVGMYEYRR----HAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 224 CSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
59-274 |
3.43e-31 |
|
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: 116.07 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 59 HVY-YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLN---RMNdtidgcrvTGKITLDNKNIydpNLDVVLLRAQ 134
Cdd:cd03263 8 KTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgelRPT--------SGTAYINGYSI---RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 135 VGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDLEeiVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAV 213
Cdd:cd03263 77 LGYCPQFDALFDElTVREHLRFYARLKGLPKSEIKEE--VELLLRVLGL-TDKANKR--ART-LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
71-287 |
7.53e-31 |
|
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: 118.28 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQNEVIAFIGPSGCGKSTFLRT---LNRMNDtidgcrvtGKITLDNKNIYDPNLDVVLL--RAQVGMVFQKPNPF 145
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLERPDS--------GRIRLGGEVLQDSARGIFLPphRRRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 P-KSIFDNVAYGPKLHGLARDKYDLEEIVENsLRKAGLweevkdrLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:COG4148 90 PhLSVRGNLLYGRKRAPRAERRISFDEVVEL-LGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 225 SALDpiATAKVE--ELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:COG4148 162 AALD--LARKAEilPYLERLRDELDIpiLYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
67-253 |
8.77e-31 |
|
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: 115.40 E-value: 8.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDpnLDVVLLRAQVGMVFQKPNPFP 146
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG-----QILIDGIDIRD--ISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYGpklHGLARDkydleEIVENSLRKAGLWEEVKDR-------LNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:cd03254 91 GTIMENIRLG---RPNATD-----EEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190
....*....|....*....|....*....|....
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
71-274 |
1.08e-30 |
|
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: 114.70 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQnEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVVL--LRAQVGMVFQKPNPFPK- 147
Cdd:cd03297 17 IDFDLNE-EVTGIFGASGAGKSTLLRCIAGL-EKPDG----GTIVLNGTVLFDSRKKINLppQQRKIGLVFQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 SIFDNVAYGPKLHGLARDKYDLEEIVEnSLRKAGLweevkdrLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSAL 227
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLD-LLGLDHL-------LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447014717 228 DPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
52-285 |
1.62e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.11 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 52 KISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNlDVVLL 131
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-----QSGTVFLGDKPISMLS-SRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPKSIFDNVAYG--PKLHGLARDKYDLEEIVENSLRKAGLwEEVKDRlnqPGTGLSGGQQQRLCIAR 209
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVAYGrsPWLSLWGRLSAEDNARVNQAMEQTRI-NHLADR---RLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
53-287 |
1.83e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.67 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQD-AHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVVll 131
Cdd:PRK13652 4 IETRDlCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP-----TSGSVLIRGEPITKENIREV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNP--FPKSIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLwEEVKDRLNQpgtGLSGGQQQRLCIAR 209
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL--DEETVAHRVSSALHMLGL-EELRDRVPH---HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
65-287 |
3.03e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 115.23 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FE--AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdtidgCRVTGKITLDNKNI--YDPNLDVVLLRAQVGMVFQ 140
Cdd:PRK13649 18 FEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLItsTSKNKDIKQIRKKVGLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNP--FPKSIFDNVAYGPKLHGLArdKYDLEEIVENSLRKAGLWEEVKDRlnQPGTgLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PRK13649 93 FPESqlFEETVLKDVAFGPQNFGVS--QEEAEALAREKLALVGISESLFEK--NPFE-LSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 219 LMDEPCSALDPIATAKVEELISEL-SDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVD 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
68-290 |
6.63e-30 |
|
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: 112.94 E-value: 6.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDVVLlraqvgmVFQKPNPFP- 146
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG-----GVILEGKQITEPGPDRMV-------VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVILMDEPCSA 226
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 227 LDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYF------HLGDLIEVNstekvFTQPDHQL 290
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVP-----FPRPRDRL 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
62-264 |
1.36e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.51 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIydpNlDVVLLRAQVGMVFQK 141
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGDLFIGEKRM---N-DVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPK-SIFDNVAYGPKLHGLarDKYDLEEIVENS---LRKAGLWEEvkdrlnQPgTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:PRK11000 84 YALYPHlSVAENMSFGLKLAGA--KKEEINQRVNQVaevLQLAHLLDR------KP-KALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADK 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
62-286 |
1.62e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM-NDT-----IDGCRVTgKITLDNKNIYdpnldvvllraqv 135
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTegqifIDGEDVT-HRSIQQRDIC------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 136 gMVFQKPNPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDR-LNQpgtgLSGGQQQRLCIARTIAV 213
Cdd:PRK11432 82 -MVFQSYALFPHmSLGENVGYGLKMLGVPKE--ERKQRVKEALELVDL-AGFEDRyVDQ----ISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
63-291 |
1.95e-29 |
|
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: 117.09 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKS-TFLRTLNRMNDTidGCRVTGKITLDNKNIYDpnLDVVLLRA----QVGM 137
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDP--AAHPSGSILFDGQDLLG--LSERELRRirgnRIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 138 VFQKP----NPFpKSIFDNVAYGPKLHGLARDKYDLEEIVEnSLRKAGLwEEVKDRLN----QpgtgLSGGQQQRLCIAR 209
Cdd:COG4172 97 IFQEPmtslNPL-HTIGKQIAEVLRLHRGLSGAAARARALE-LLERVGI-PDPERRLDayphQ----LSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
....
gi 447014717 288 HQLT 291
Cdd:COG4172 250 HPYT 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
61-253 |
2.45e-29 |
|
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: 111.55 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAI-KGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVvlLRAQVGMVF 139
Cdd:cd03251 10 YPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-----DSGRILIDGHDVRDYTLAS--LRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFPKSIFDNVAYGpklhglaRDKYDLEEIVEnSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIARTIA 212
Cdd:cd03251 83 QDVFLFNDTVAENIAYG-------RPGATREEVEE-AARAANAHEFIMElpegydtVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
48-254 |
4.03e-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: 115.92 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 48 STEIKISAQDAHVYY-GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDpnL 126
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG-----EVTLDGVPVSS--L 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 127 DVVLLRAQVGMVFQKPNPFPKSIFDNVAygpklhgLARDKYDLEEIVEnSLRKAGL--W-EEVKDRLNQP----GTGLSG 199
Cdd:TIGR02868 403 DQDEVRRRVSVCAQDAHLFDTTVRENLR-------LARPDATDEELWA-ALERVGLadWlRALPDGLDTVlgegGARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 200 GQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHS 254
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
60-265 |
8.05e-29 |
|
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: 109.80 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYD-PNLDVVLLRAQVGMV 138
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP-----TSGTIRVNGQDVSDlRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 FQKPNPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:cd03292 84 FQDFRLLPDrNVYENVAFALEVTGVPPR--EIRKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRT 265
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHAKELVDTTRHRV 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
72-271 |
1.02e-28 |
|
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: 109.50 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 72 DLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDGCRV--TGKITLDNkniydpnLDVVLL---RAQVGMVFQKPNPFP 146
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLL-------NLIAGFETpqSGRVLING-------VDVTAAppaDRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYG--PKLHGLARDKydleEIVENSLRKAGLWEEVKDRlnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:cd03298 84 HlTVEQNVGLGlsPGLKLTAEDR----QAIEVALARVGLAGLEKRL---PGE-LSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447014717 224 CSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
67-297 |
1.62e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.82 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKItlDNKNIYDPNLDVVLlRAQVGMVFQKPNPFP 146
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV--DIAKISDAELREVR-RKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:PRK10070 120 HmTVLDNTAFGMELAGINAE--ERREKALDALRQVGLENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 226 ALDP-IATAKVEELIS-ELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYITG 297
Cdd:PRK10070 194 ALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
67-293 |
1.98e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 111.34 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcRVT--GKITLDNKNiyDPNLDVvllRAQVGMVFQKP-- 142
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG-EVAwlGKDLLGMKD--DEWRAV---RSDIQMIFQDPla 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 --NPfPKSIFDNVA-----YGPKLHglardKYDLEEIVENSLRKAGLWEEVKDRLNQPgtgLSGGQQQRLCIARTIAVSP 215
Cdd:PRK15079 110 slNP-RMTIGEIIAeplrtYHPKLS-----RQEVKDRVKAMMLKVGLLPNLINRYPHE---FSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEA 293
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKA 260
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
53-274 |
2.44e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 108.61 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNkniYDPNLDV 128
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG-----FATVDG---FDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLLRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARD--KYDLEEIVENSlrkaglweEVKDRLNQPGTGLSGGQQQRL 205
Cdd:cd03266 74 AEARRRLGFVSDSTGLYDRlTARENLEYFAGLYGLKGDelTARLEELADRL--------GMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
69-253 |
4.63e-28 |
|
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: 113.51 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 69 KGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTidgcRVTGKITLDNKNIYDpnLDVVLLRAQVGMVFQKPNPFPKS 148
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-ET----PESGSVFYDGQDLAG--LDVQAVRRQLGVVLQNGRLMSGS 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 149 IFDNVAYGPKLhglardkyDLEEIVEnSLRKAGLWEEVKDR-------LNQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:TIGR03797 543 IFENIAGGAPL--------TLDEAWE-AARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQRQRLLIARALVRKPRILLFD 613
|
170 180 190
....*....|....*....|....*....|..
gi 447014717 222 EPCSALDPIATAKVEELISELsdQYTIVIVTH 253
Cdd:TIGR03797 614 EATSALDNRTQAIVSESLERL--KVTRIVIAH 643
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
67-287 |
6.40e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNiydPNLDVVLLRAQVGMVFQKPNP-- 144
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS---KQKEIKPVRKKVGVVFQFPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 145 FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRlnQPGTgLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKE--KAEKIAAEKLEMVGLADEFWEK--SPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 225 SALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
64-295 |
7.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 7.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVVL--LRAQVGMVFQK 141
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP-----TTGTVTVDDITITHKTKDKYIrpVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNP--FPKSIFDNVAYGPKLHGLardkyDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:PRK13646 94 PESqlFEDTVEREIIFGPKNFKM-----NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 220 MDEPCSALDPIATAKVEELISELS--DQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQpDHQLTEAYI 295
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD-KKKLADWHI 245
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
62-265 |
8.09e-28 |
|
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: 106.93 E-value: 8.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrMNDTIDGcrvtGKITLDNKNIYDPN--LDVVLLRAQVGMVF 139
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIG-LLEKFDS----GQVYLNGQETPPLNskKASKFRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKpnpFP----KSIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLWEevkdRLNQPGTGLSGGQQQRLCIARTIAVSP 215
Cdd:TIGR03608 83 QN---FAlienETVEENLDLGLKYKKL--SKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARvSDRT 265
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPEVAKQ-ADRV 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
62-264 |
8.94e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.23 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNkniydpnldvvlLRAQVGMVFQK 141
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------------AREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFP-KSIFDNVAYGpkLHGLARDKydleeiVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:PRK11247 90 ARLLPwKKVIDNVGLG--LKGQWRDA------ALQALAAVGL----ADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADR 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
53-252 |
1.23e-27 |
|
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: 106.41 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgC----RVTGKITLDNKNIYDPNLDV 128
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---------AgllpPSAGEVLWNGEPIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vllRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDLEEIvensLRKAGLweevKDRLNQPGTGLSGGQQQRLCI 207
Cdd:COG4133 74 ---RRRLAYLGHADGLKPElTVRENLRFWAALYGLRADREAIDEA----LEAVGL----AGLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVT 252
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
67-284 |
1.74e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.77 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDvvLLRAQVGMVFQKP-NPF 145
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG-----EIKIDGITISKENLK--EIRKKIGIIFQNPdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 -PKSIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK13632 97 iGATVEDDIAFGLENKKVPPKK--MKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 225 SALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
48-286 |
1.79e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.40 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 48 STEI-KISAqdahvYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTlnrmndtIDGC--RVTGKITLDNKniydp 124
Cdd:PRK10851 2 SIEIaNIKK-----SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRI-------IAGLehQTSGHIRFHGT----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 125 nlDVVLLRA---QVGMVFQKPNPFPK-SIFDNVAYGpkLHGLARDKYDLEEIVENSLRKagLWEEVK-DRL-NQPGTGLS 198
Cdd:PRK10851 65 --DVSRLHArdrKVGFVFQHYALFRHmTVFDNIAFG--LTVLPRRERPNAAAIKAKVTQ--LLEMVQlAHLaDRYPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 199 GGQQQRLCIARTIAVSPEVILMDEPCSALDpiATAKVE------ELISELsdQYTIVIVTHSMQQAARVSDRTAYFHLGD 272
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEEL--KFTSVFVTHDQEEAMEVADRVVVMSQGN 214
|
250
....*....|....
gi 447014717 273 LIEVNSTEKVFTQP 286
Cdd:PRK10851 215 IEQAGTPDQVWREP 228
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
67-264 |
1.92e-27 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 105.96 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrMNDTIDgcrvTGKITLDNKNIYdpNLD----VVLLRAQVGMVFQKP 142
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEVT--NLSysqkIILRRELIGYIFQSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 NPFPK-SIFDNVAYGPKLHGLArdKYDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:NF038007 93 NLIPHlSIFDNVALPLKYRGVA--KKERIERVNQVLNLFGI----DNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447014717 222 EPCSALDPIATAKVEELISELSDQ-YTIVIVTHSmQQAARVSDR 264
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYINQKgTTIIMVTHS-DEASTYGNR 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
62-275 |
2.34e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 105.76 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIYDPNLDVvllrAQVGMVFQK 141
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL-IKPDS----GEITFDGKSYQKNIEAL----RRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPK-SIFDNVAYGPKLHGLardkydLEEIVENSLRKAGLWEEVKDRLNqpgtGLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:cd03268 81 PGFYPNlTARENLRLLARLLGI------RKKRIDEVLDVVGLKDSAKKKVK----GFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
71-299 |
2.63e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.61 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM----NDTIDgcrVTGK-ITLD--NKNIYDpnldvvlLRAQVGMVFQKPN 143
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALlkpsSGTIT---IAGYhITPEtgNKNLKK-------LRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 P--FPKSIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLWEEVkdrLNQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:PRK13641 96 AqlFENTVLKDVEFGPKNFGFSEDE--AKEKALKWLKKVGLSEDL---ISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 222 EPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD----HQLTEAyIT 296
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkHYLDEP-AT 249
|
...
gi 447014717 297 GRF 299
Cdd:PRK13641 250 SRF 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
67-295 |
3.74e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.77 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDpnldVVLLRAQVGMVFQKPNPFP 146
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP-----TAGQIMLDGVDLSH----VPPYQRPINMMFQSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:PRK11607 105 HmTVEQNIAFGLKQDKLPKA--EIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 226 ALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
64-284 |
5.73e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.63 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTG--KITLDNKNIYDpnldVVLLRAQVGMVFQK 141
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKIKE----VKRLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 P--NPFPKSIFDNVAYGPkLHgLARDKYDLEEIVENSLRKAGLWEEVKDRlnQPGTgLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:PRK13645 99 PeyQLFQETIEKDIAFGP-VN-LGENKQEAYKKVPELLKLVQLPEDYVKR--SPFE-LSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYT--IVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
68-269 |
8.75e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 8.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmNDTIDGCRVTGKITLDNKNIYD-PnldvVLLRaQVGMVFQKPNPFP 146
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLTAlP----AEQR-RIGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYG--PKLHGLARDkydleEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:COG4136 90 HlSVGENLAFAlpPTIGRAQRR-----ARVEQALEEAGL-AGFADRD--PAT-LSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447014717 224 CSALDPIATAKVEELISELSDQYTI--VIVTHSMQ---QAARVSDRTAYFH 269
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEdapAAGRVLDLGNWQH 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
56-258 |
1.27e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 56 QDAHVY--YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDGCRV--TGKITLDNKNIYDPNldvvll 131
Cdd:PRK11248 3 QISHLYadYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL-------NLIAGFVPyqHGSITLDGKPVEGPG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 rAQVGMVFQKPNPFP-KSIFDNVAYGPKLHGLARDKYdlEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIART 210
Cdd:PRK11248 70 -AERGVVFQNEGLLPwRNVQDNVAFGLQLAGVEKMQR--LEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISEL--SDQYTIVIVTHSMQQA 258
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEA 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
66-255 |
1.31e-26 |
|
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: 103.82 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYdpNLDVVLLRAQVGMVFQKPNPF 145
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSG-----SVLLDGTDIR--QLDPADLRRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PKSIFDNVAYGpklHGLARDkydlEEIVEnSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:cd03245 91 YGTLRDNITLG---APLADD----ERILR-AAELAGVTDFVNKhpngldlQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSM 255
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
65-274 |
1.32e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.94 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM-------------NDTIDGCRVTGKITLDNKNIYDPNL----D 127
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLVIQKTRFkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 VVLLRAQVGMVFQ--KPNPFPKSIFDNVAYGPKLHGLarDKYDLEEIVENSLRKAGLWEEVKDRlnQPgTGLSGGQQQRL 205
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGV--SKEEAKKRAAKYIELVGLDESYLQR--SP-FELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
64-283 |
1.67e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYDpnldvvlLRAQVGMVFQKP- 142
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-------LRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 NPF-PKSIFDNVAYGPKLHGLARdkydlEEIVENsLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:PRK13642 92 NQFvGATVEDDVAFGMENQGIPR-----EEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 222 EPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVF 283
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
53-264 |
1.77e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 101.74 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndtidGCRV--TGKITLDNK--NIYDPNLDv 128
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-------GLYKpdSGEILVDGKevSFASPRDA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vlLRAQVGMVFQkpnpfpksifdnvaygpklhglardkydleeivenslrkaglweevkdrlnqpgtgLSGGQQQRLCIA 208
Cdd:cd03216 73 --RRAGIAMVYQ--------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
66-282 |
1.83e-26 |
|
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: 104.11 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIydPNLDVVLLRAQVGMVFQKPNPF 145
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG-----RVLVDGHDL--ALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PKSIFDNVAygpklhgLARDKYDLEEIVENSlRKAG-------LWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:cd03252 89 NRSIRDNIA-------LADPGMSMERVIEAA-KLAGahdfiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMqQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
70-284 |
8.32e-26 |
|
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: 102.96 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 70 GIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYdpNLDVVLLRA---QVGMVFQK-PNPF 145
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP-----AQGTVSFRGQDLY--QLDRKQRRAfrrDVQLVFQDsPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 -PKSIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPgtgLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:TIGR02769 102 nPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 225 SALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
53-264 |
1.18e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 101.20 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM--NDTidgcrvtGKITLDNKNI-YDPNLDVV 129
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIilPDS-------GEVLFDGKPLdIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQVGMvfqkpnpFPK-SIFDNVAYGPKLHGLARdkydlEEIVENSLR---KAGLWEEVKDRLNQpgtgLSGGQQQRL 205
Cdd:cd03269 74 YLPEERGL-------YPKmKVIDQLVYLAQLKGLKK-----EEARRRIDEwleRLELSEYANKRVEE----LSKGNQQKV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDR 197
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
64-261 |
1.26e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 106.34 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtIDGcrvtGKITLDNKNIYDPNLDVvlLRAQVGMVFQKPN 143
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE-PDS----GQILLDGHDLADYTLAS--LRRQVALVSQDVV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 PFPKSIFDNVAYGpklhglARDKYDLEEIvENSLRKAGLWEEVkDRL--------NQPGTGLSGGQQQRLCIARTIAVSP 215
Cdd:TIGR02203 417 LFNDTIANNIAYG------RTEQADRAEI-ERALAAAYAQDFV-DKLplgldtpiGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH---SMQQAARV 261
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTLVIAHrlsTIEKADRI 537
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
46-265 |
2.37e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 100.97 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 46 PNSTEIKISAQDAHVYYGDFEA----IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNI 121
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTS----GTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 122 YdpNLD---VVLLRAQ-VGMVFQK----PNpfpKSIFDNVAYgPKLhgLARDKyDLEEIVENSLRKAGLweevKDRLN-Q 192
Cdd:COG4181 77 F--ALDedaRARLRARhVGFVFQSfqllPT---LTALENVML-PLE--LAGRR-DARARARALLERVGL----GHRLDhY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 193 PGtGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARvSDRT 265
Cdd:COG4181 144 PA-QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRV 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
43-287 |
3.58e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.62 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 43 SKKPNSTEIKISAQDAHVYYGD-----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLD 117
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 118 NKNIYDPNLDVVL---------LRAQVGMVFQKP--NPFPKSIFDNVAYGPKlhGLARDKYDLEEIVENSLRKAGLWEEV 186
Cdd:PRK13631 92 DKKNNHELITNPYskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPV--ALGVKKSEAKKLAKFYLNKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 187 KDRlnQPgTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISEL-SDQYTIVIVTHSMQQAARVSDRT 265
Cdd:PRK13631 170 LER--SP-FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVADEV 246
|
250 260
....*....|....*....|..
gi 447014717 266 AYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
53-274 |
4.73e-25 |
|
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: 99.57 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIyQNEVIAFIGPSGCGKSTFLR---TLNRMndtidgcrVTGKITLDNkniYDPNLDVV 129
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRilaTLTPP--------SSGTIRIDG---QDVLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLArdKYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIA 208
Cdd:cd03264 69 KLRRRIGYLPQEFGVYPNfTVREFLDYIAWLKGIP--SKEVKARVDEVLELVNLGDRAKKKIGS----LSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
61-228 |
6.18e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.23 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLrtlnRMndtIDGC-RVT-GKITLDNKNIYD--P-NLDvvllraqV 135
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLL----RM---VAGLeRITsGEIWIGGRVVNElePaDRD-------I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 136 GMVFQKPNPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRlnQPgTGLSGGQQQRLCIARTIAVS 214
Cdd:PRK11650 79 AMVFQNYALYPHmSVRENMAYGLKIRGMPKA--EIEERVAEAARILEL-EPLLDR--KP-RELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 447014717 215 PEVILMDEPCSALD 228
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
67-291 |
6.24e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.55 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYD-PNLDVVLLRAQVGMVFQKP--- 142
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES-----QGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDPyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 -NPfPKSIFDNVAYGPKLHGLARDKYDLEEIVEnSLRKAGLWEEVKDRLNQPgtgLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:PRK10261 414 lDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAW-LLERVGLLPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 222 EPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLT 291
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
67-281 |
9.78e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.16 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRmNDTIDgcrvTGKITLDNKNI-----YDpnldvvllRAQ-VGMVFQ 140
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG-SLPPD----SGSILIDGKDVtklpeYK--------RAKyIGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 kpNPF----PK-SIFDN--VAYG-PKLHGLAR--DKYDLEEIVEnSLRKAGLWEEvkDRLNQPgTG-LSGGQQQRLCIAR 209
Cdd:COG1101 88 --DPMmgtaPSmTIEENlaLAYRrGKRRGLRRglTKKRRELFRE-LLATLGLGLE--NRLDTK-VGlLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKV----EELISElsDQYTIVIVTHSMQQAARVSDRTAYFHLGDLI-EVNSTEK 281
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEE--NNLTTLMVTHNMEQALDYGNRLIMMHEGRIIlDVSGEEK 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
53-294 |
1.06e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndTIDGCRVTGKITLDNKNI--YDPNldvvL 130
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-----SGELSPDSGEVRLNGRPLadWSPA----E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMVFQKPN-PFPKSIFDNVAYGpkLHGLARDKYDLEEIVENSLRKAGLWeEVKDRLNQpgtGLSGGQQQRLCIAR 209
Cdd:PRK13548 74 LARRRAVLPQHSSlSFPFTVEEVVAMG--RAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYP---QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 210 TIA------VSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEK 281
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
250
....*....|...
gi 447014717 282 VFTqpDHQLTEAY 294
Cdd:PRK13548 228 VLT--PETLRRVY 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
67-286 |
1.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.26 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLN---------RMNDTIDGcrvtgkITLDNKNIYDpnldvvlLRAQVGM 137
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINglllpddnpNSKITVDG------ITLTAKTVWD-------IREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 138 VFQKP-NPF-PKSIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLWEEVKdrlNQPGTgLSGGQQQRLCIARTIAVSP 215
Cdd:PRK13640 89 VFQNPdNQFvGATVGDDVAFGLENRAVPRPE--MIKIVRDVLADVGMLDYID---SEPAN-LSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISEL--SDQYTIVIVTHSMQQAArVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
67-264 |
1.14e-24 |
|
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: 103.79 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYdpNLDVVLLRAQVGMVFQKPNPFP 146
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEG-----SVLLDGVDIR--QIDPADLRRNIGYVPQDPRLFY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYGpklHGLARDkydlEEIVEnSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:TIGR03375 553 GTLRDNIALG---APYADD----EEILR-AAELAGVTEFVRRhpdgldmQIGERGRSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447014717 220 MDEPCSALDPIATAKV-EELISELSDQyTIVIVTHSMQQAARVsDR 264
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFkDRLKRWLAGK-TLVLVTHRTSLLDLV-DR 668
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
64-260 |
1.77e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 98.31 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIydPNLDVVLLRAQVGMVFQKPN 143
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG-----QVLLDGKPI--SQYEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 PFPKSIFDNVAYGpkLHGLArdkydLEEIVEN----------SLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAV 213
Cdd:cd03248 99 LFARSLQDNIAYG--LQSCS-----FECVKEAaqkahahsfiSELASGYDTEVGEKGSQ----LSGGQKQRVAIARALIR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAAR 260
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
38-287 |
1.78e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 38 FEPHASKKPNSTEIKISAQDAHVYY---GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM-NDTidgcrvTGK 113
Cdd:TIGR00958 464 IPLTGTLAPLNLEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPT------GGQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 114 ITLDNKNIydPNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAYGpklhglaRDKYDLEEIVeNSLRKAGLWEEVKDRLN-- 191
Cdd:TIGR00958 538 VLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG-------LTDTPDEEIM-AAAKAANAHDFIMEFPNgy 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 192 -----QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpiatAKVEELISELSDQY--TIVIVTHSMQQAARvSDR 264
Cdd:TIGR00958 608 dtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRAsrTVLLIAHRLSTVER-ADQ 682
|
250 260
....*....|....*....|...
gi 447014717 265 TAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
68-275 |
2.95e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG---CRVTGKITLDNKNIYDpnldvvlLRAQVGMVFQKP-- 142
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGnvsWRGEPLAKLNRAQRKA-------FRRDIQMVFQDSis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 --NPfPKSIFDNVAYgPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:PRK10419 101 avNP-RKTVREIIRE-PLRHLLSLDKAERLARASEMLRAVDLDDSVLDKR--PPQ-LSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
53-253 |
4.13e-24 |
|
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: 97.85 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVT--GKiTLDNKNIYDpnldvvl 130
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGE-RRGGEDVWE------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMV---FQKPNPFPKSIFDNVAYGpkLH---GLARdKYDLEEIvenslRKAGLWEE---VKDRLNQPGTGLSGGQ 201
Cdd:COG1119 76 LRKRIGLVspaLQLRFPRDETVLDVVLSG--FFdsiGLYR-EPTDEQR-----ERARELLEllgLAHLADRPFGTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447014717 202 QQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTH 253
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTH 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
63-274 |
5.12e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGC-RVTGK--ITLDNKNIydpnldVVLLRAQVGMVF 139
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyRVAGQdvATLDADAL------AQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFPK-SIFDNVAYGPKLHGLARDKYdlEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PRK10535 93 QRYHLLSHlTAAQNVEVPAVYAGLERKQR--LLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARvSDRTAYFHLGDLI 274
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
53-271 |
5.65e-24 |
|
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: 95.75 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEA--IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTL--NRMNdtidgcrVTGKITLDNKNI--YDPNL 126
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLIlgLLRP-------TSGRVRLDGADIsqWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 127 dvvlLRAQVGMVFQKPNPFPKSIFDNVaygpklhglardkydleeivenslrkaglweevkdrlnqpgtgLSGGQQQRLC 206
Cdd:cd03246 74 ----LGDHVGYLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 207 IARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVsDRTAYFHLG 271
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPETLASA-DRILVLEDG 171
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
72-265 |
6.98e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.96 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 72 DLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDGCRV--TGKITLDNKNiydpNLDVVLLRAQVGMVFQKPNPFPK-S 148
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL-------NLIAGFLTpaSGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 149 IFDNVAYGpkLH-GL---ARDKYDLEEIVenslRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK10771 88 VAQNIGLG--LNpGLklnAAQREKLHAIA----RQMGI-EDLLARL--PGQ-LSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447014717 225 SALDPIATAKVEELISELSD--QYTIVIVTHSMQQAARVSDRT 265
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQerQLTLLMVSHSLEDAARIAPRS 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
57-287 |
1.13e-23 |
|
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: 99.03 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 57 DAHVYYGDFEAikGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdTIDGcrvtGKITLDNKNIYDPNLDVVLL--RAQ 134
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT-RPDE----GEIVLNGRTLFDSRKGIFLPpeKRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 135 VGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDLEEIVEnslrKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAV 213
Cdd:TIGR02142 77 IGYVFQEARLFPHlSVRGNLRYGMKRARPSERRISFERVIE----LLGI-GHLLGRL--PGR-LSGGEKQRVAIGRALLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
72-279 |
1.60e-23 |
|
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: 95.70 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 72 DLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIydpnLDVVLLRAQVGMVFQKPNPFPK-SIF 150
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP-----ASGSIKVNDQSH----TGLAPYQRPVSMLFQENNLFAHlTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 151 DNVAYG--PKLHGLARDKydleEIVENSLRKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEPCSALD 228
Cdd:TIGR01277 89 QNIGLGlhPGLKLNAEQQ----EKVVDAAQQVGI-ADYLDRL--PEQ-LSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447014717 229 PIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNST 279
Cdd:TIGR01277 161 PLLREEMLALVKQLCSErqRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
61-264 |
3.33e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRT-LNRMNDTidgcrvTGKITLDNKNIydpNLDVvllRAQVG-Mv 138
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIiLGILAPD------SGEVLWDGEPL---DPED---RRRIGyL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 fqkpnP-----FPK-SIFDNVAYGPKLHGLARDKydleeivenSLRKAGLW-E--EVKDRLNQPGTGLSGGQQQRLCIAR 209
Cdd:COG4152 77 -----PeerglYPKmKVGEQLVYLARLKGLSKAE---------AKRRADEWlErlGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIV-THSMQQAARVSDR 264
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDR 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
53-275 |
3.70e-23 |
|
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: 93.53 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFE--AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRmndtiDGCRVTGKITLDNKNIYDPNldvVL 130
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-----DLKPQQGEITLDGVPVSDLE---KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMVFQKPNPFPKSIFDNVaygpklhglardkydleeivenslrkaglweevkdrlnqpGTGLSGGQQQRLCIART 210
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVsDRTAYFHLGDLIE 275
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
67-253 |
6.51e-23 |
|
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: 94.10 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtIDGCRvtGKITLDNKNIYDpnLDVVLLRAQVGMVFQKPNPFP 146
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL---VELSS--GSILIDGVDISK--IGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAygpklhglARDKYDLEEIvENSLRKAGLWEEVK-------DRLNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:cd03244 92 GTIRSNLD--------PFGEYSDEEL-WQALERVGLKEFVEslpggldTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190
....*....|....*....|....*....|....
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
68-287 |
7.89e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.18 E-value: 7.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTlnrmndtIDGCRV--TGKITLDNKNIYDPNldVVLLRAQVGMVFQKP-NP 144
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRL-------IDGLLEaeSGQIIIDGDLLTEEN--VWDIRHKIGMVFQNPdNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 145 F-PKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRlnQPGTgLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:PRK13650 94 FvGATVEDDVAFGLENKGIPHE--EMKERVNEALELVGM-QDFKER--EPAR-LSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 224 CSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAArVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
61-275 |
7.89e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.11 E-value: 7.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVvlLRAQVGMVFQ 140
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP-----QSGRILIDGTDIRTVTRAS--LRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPKSIFDNVAYGpklhglaRDKYDLEEIVEnSLRKAGLWEEVKDRLN-------QPGTGLSGGQQQRLCIARTIAV 213
Cdd:PRK13657 417 DAGLFNRSIEDNIRVG-------RPDATDEEMRA-AAERAQAHDFIERKPDgydtvvgERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMqQAARVSDRTAYFHLGDLIE 275
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVE 549
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
53-294 |
8.05e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.80 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndTIDGCRVTGKITLDNKNIYD-PNLDVVLL 131
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLL-----TGELTPSSGEVRLNGRPLAAwSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RA----QVGMVFqkpnPFpkSIFDNVAYGpkLHGLARDKYDLEEIVENSLRKAGLWEeVKDRLNQpgtGLSGGQQQRLCI 207
Cdd:COG4559 77 RAvlpqHSSLAF----PF--TVEEVVALG--RAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQ---TLSGGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 208 ARTIA-------VSPEVILMDEPCSALDP---IATAkveELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEV 276
Cdd:COG4559 145 ARVLAqlwepvdGGPRWLFLDEPTSALDLahqHAVL---RLARQLARRgGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
250
....*....|....*...
gi 447014717 277 NSTEKVFTqpDHQLTEAY 294
Cdd:COG4559 222 GTPEEVLT--DELLERVY 237
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
66-256 |
2.00e-22 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 92.48 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNKNIydPNLDVVLLRAQVGMVFQKPNPF 145
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDI--STIPLEDLRSSLTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PKSIFDNVAygpklhglARDKYDLEEIVEnSLRkaglweevkdrLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:cd03369 95 SGTIRSNLD--------PFDEYSDEEIYG-ALR-----------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190
....*....|....*....|....*....|.
gi 447014717 226 ALDPIATAKVEELISELSDQYTIVIVTHSMQ 256
Cdd:cd03369 155 SIDYATDALIQKTIREEFTNSTILTIAHRLR 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
53-293 |
2.14e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.03 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYY----GDF------EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndTIDGCRVTGKITLDNKNIY 122
Cdd:PRK11308 6 LQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLL-----TMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 123 DPNLDVV-LLRAQVGMVFQKP----NPFPK--SIFDNvaygPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLnqPGT 195
Cdd:PRK11308 81 KADPEAQkLLRQKIQIVFQNPygslNPRKKvgQILEE----PLLINTSLSAAERREKALAMMAKVGLRPEHYDRY--PHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 196 gLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDL 273
Cdd:PRK11308 155 -FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGRC 233
|
250 260
....*....|....*....|
gi 447014717 274 IEVNSTEKVFTQPDHQLTEA 293
Cdd:PRK11308 234 VEKGTKEQIFNNPRHPYTQA 253
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
67-253 |
2.64e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.63 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtIDgcrvTGKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFP 146
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD-ID----EGEILLDGHDLRDYTLAS--LRNQVALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYGpklhglARDKYDLEEIvENSLRKA---GLWEEVKDRLN----QPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:PRK11176 431 DTIANNIAYA------RTEQYSREQI-EEAARMAyamDFINKMDNGLDtvigENGVLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190
....*....|....*....|....*....|....
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
68-254 |
3.76e-22 |
|
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: 91.46 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTL-NRmndtIDGCRVTGKITLDNKNIYDPNLdvvllRAQVGMVFQkpnpfp 146
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGR----RTGLGVSGEVLINGRPLDKRSF-----RKIIGYVPQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 ksifDNVAYGpklhglardkydleeivENSLRKAgLWEEVKDRlnqpgtGLSGGQQQRLCIARTIAVSPEVILMDEPCSA 226
Cdd:cd03213 90 ----DDILHP-----------------TLTVRET-LMFAAKLR------GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180
....*....|....*....|....*....
gi 447014717 227 LDPIATAKVEELISELSDQ-YTIVIVTHS 254
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTgRTIICSIHQ 170
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
56-264 |
3.95e-22 |
|
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: 92.20 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 56 QDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNI--YDPNLDVvllRA 133
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPV-----KSGSIRLDGEDItkLPPHERA---RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 QVGMVFQKPNPFPK-SIFDNVAYGPKLHGlARDKYDLEEIVEnslrkagLWEEVKDRLNQPGTGLSGGQQQRLCIARTIA 212
Cdd:TIGR03410 76 GIAYVPQGREIFPRlTVEENLLTGLAALP-RRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDR 264
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADR 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
41-275 |
4.54e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 91.83 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 41 HASKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDgcrvTGKITLDNKn 120
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI-YPPD----SGTVTVRGR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 121 iydpnlDVVLLRAQVGMvfqkpNPfPKSIFDNVAYGPKLHGLARDKYD--LEEIVENSlrkaglweEVKDRLNQPGTGLS 198
Cdd:cd03220 85 ------VSSLLGLGGGF-----NP-ELTGRENIYLNGRLLGLSRKEIDekIDEIIEFS--------ELGDFIDLPVKTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 199 GGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVI-VTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
62-292 |
5.84e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 92.20 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTL-NRMndTIDgcrvTGKITLDNKNIYDPNLDVV-------LLRA 133
Cdd:TIGR02323 13 YGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLaGRL--APD----HGTATYIMRSGAELELYQLseaerrrLMRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 134 QVGMVFQKPNPFPK---SIFDNVayGPKLHGLARDKY-DLEEIVENSLRKAglwEEVKDRLNQPGTGLSGGQQQRLCIAR 209
Cdd:TIGR02323 87 EWGFVHQNPRDGLRmrvSAGANI--GERLMAIGARHYgNIRATAQDWLEEV---EIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
....*
gi 447014717 288 HQLTE 292
Cdd:TIGR02323 242 HPYTQ 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
50-267 |
6.83e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 50 EIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKST-FlrtlnRMndtIDG-CRVT-GKITLDNKNI----- 121
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtF-----YM---IVGlVKPDsGRIFLDGEDIthlpm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 122 YdpnldvvlLRAQVGMVF--QKPnpfpkSIF------DNVAYGPKLHGLarDKYDLEEIVENSLRKAGLwEEVKDrlnQP 193
Cdd:COG1137 73 H--------KRARLGIGYlpQEA-----SIFrkltveDNILAVLELRKL--SKKEREERLEELLEEFGI-THLRK---SK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 194 GTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRtAY 267
Cdd:COG1137 134 AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDR-AY 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
53-264 |
1.02e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgC---RVT-GKITLDNKNIYDPNlDV 128
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL---------CgdpRATsGRIVFDGKDITDWQ-TA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLLRAQVGMVFQKPNPFPK-SIFDNVAYGpklhGLARDKYDLEEIVEnslRKAGLWEEVKDRLNQPGTGLSGGQQQRLCI 207
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRmTVEENLAMG----GFFAERDQFQERIK---WVYELFPRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADR 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
62-284 |
1.41e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDgcrvtGKITLDNKNIYDPNLDVVLLRaqVGMVFQK 141
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH-----GHVWLDGEHIQHYASKEVARR--IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 P-NPFPKSIFDNVAYGPKLHG--LARDKYDLEEIVENSLRKAGlweeVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PRK10253 90 AtTPGDITVQELVARGRYPHQplFTRWRKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
62-287 |
1.47e-21 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 90.80 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKST-FLRTLNRMNDTidgcrvTGKITLDNKNIYDPNLDvvlLRAQVGMVF- 139
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsFYMIVGLVRPD------AGKILIDGQDITHLPMH---ERARLGIGYl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 -QKPNPFPK-SIFDNVAYGPKLhglaRDKYDLEEIVEnslRKAGLWEE--VKDRLNQPGTGLSGGQQQRLCIARTIAVSP 215
Cdd:TIGR04406 82 pQEASIFRKlTVEENIMAVLEI----RKDLDRAEREE---RLEALLEEfqISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISELSDQYTIVIVT-HSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPD 287
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
56-273 |
1.60e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 56 QDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgCRV----TGKITLDNKNIYD-PNLDVVL 130
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLI---------CGIerpsAGKIWFSGHDITRlKNREVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMVFQKPNPF-PKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIAR 209
Cdd:PRK10908 77 LRRQIGMIFQDHHLLmDRTVYDNVAIPLIIAGASGD--DIRRRVSAALDKVGLLDKAKNFPIQ----LSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSD-QYTIVIVTHSMQQAARVSDRTAYFHLGDL 273
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
49-264 |
1.88e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 49 TEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdTIDGcrvtGKITLDNK--NIYDPnL 126
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVY-QPDS----GEILLDGEpvRFRSP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 127 DVvlLRAQVGMVFQKPNPFPK-SIFDNVAYG--PKLHGLARDKyDLEEIVENSLRKAGL----WEEVKDrlnqpgtgLSG 199
Cdd:COG1129 75 DA--QAAGIAIIHQELNLVPNlSVAENIFLGrePRRGGLIDWR-AMRRRARELLARLGLdidpDTPVGD--------LSV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 200 GQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADR 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-253 |
3.58e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 42 ASKKPNSTEIKISAQDAHVYYGD--FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIdgcrvTGKITLDNK 119
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-----QGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 120 NIYDPNLDVvlLRAQVGMVFQKPNPFPKSIFDNVAygpklhgLARDKYDLEEIVEnSLRKAGLWE--EVKDRLNQ-PGTG 196
Cdd:PRK11160 403 PIADYSEAA--LRQAISVVSQRVHLFSATLRDNLL-------LAAPNASDEALIE-VLQQVGLEKllEDDKGLNAwLGEG 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 197 ---LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:PRK11160 473 grqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
66-271 |
5.33e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM--NDTIDGCRVTgkiTLDNKNIYDPNL--DVVLLRAQVGMVFQK 141
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIE---LLGRTVQREGRLarDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPK-SIFDNVAYGPK---------LHGLARDKydlEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTI 211
Cdd:PRK09984 95 FNLVNRlSVLENVLIGALgstpfwrtcFSWFTREQ---KQRALQALTRVGMVHFAHQRVST----LSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 212 AVSPEVILMDEPCSALDPIATAKVEELISEL--SDQYTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
62-267 |
6.52e-21 |
|
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: 89.14 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTflrTLNRMNDTIdgcRVT-GKITLDNKNIYDPNLDVvllRAQVGMVF- 139
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLV---KPDsGKILLDGQDITKLPMHK---RARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 -QKPNPFPK-SIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLwEEVKdrlNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:cd03218 81 pQEASIFRKlTVEENILAVLEIRGLSKKE--REEKLEELLEEFHI-THLR---KSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRtAY 267
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVRETLSITDR-AY 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
62-265 |
9.18e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 9.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLR----TLNRMNDTidgCRVTGKitldnkniydpnldvvllrAQVGM 137
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKvlagVLRPTSGT---VRRAGG-------------------ARVAY 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 138 VFQK---PNPFPKSIFDNVAYG--PKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIA 212
Cdd:NF040873 60 VPQRsevPDSLPLTVRDLVAMGrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELS-DQYTIVIVTHSMQQAARVSDRT 265
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCV 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
36-264 |
1.57e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 36 SHFEPHASKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdtidgCRVTGKIT 115
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-----SPDAGKIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 116 LDNKNIYDpnlDVVLLRAQVGMVFQKPNPFPK-SIFDN-VAYGPKLHGLARDkydLEEIVENSLRKAGLWEEVKDRLNQp 193
Cdd:PRK13536 100 VLGVPVPA---RARLARARIGVVPQFDNLDLEfTVRENlLVFGRYFGMSTRE---IEAVIPSLLEFARLESKADARVSD- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 194 gtgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKV-EELISELSDQYTIVIVTHSMQQAARVSDR 264
Cdd:PRK13536 173 ---LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
68-264 |
1.71e-20 |
|
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: 91.35 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrV------TGKITLDNKNIYdpNLDVVLLRAQVGMVFQK 141
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLL-----------VgvwpptAGSVRLDGADLS--QWDREELGRHIGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPKSIFDNVAygpklhglaR-DKYDLEEIVEnSLRKAGlweeVKD-----------RLNQPGTGLSGGQQQRLCIAR 209
Cdd:COG4618 415 VELFDGTIAENIA---------RfGDADPEKVVA-AAKLAG----VHEmilrlpdgydtRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMqQAARVSDR 264
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDK 535
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
53-285 |
1.89e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 91.34 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYG-DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIydPNLDVVLL 131
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQA-----RSGEILLNGFSL--KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPKSIFDNVAYGpklhglARDKYDLEEIVEnSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQR 204
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENLLLG------AKENVSQDEIWA-ACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQyTIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
.
gi 447014717 285 Q 285
Cdd:TIGR01193 698 R 698
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
63-292 |
2.19e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.40 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrMNDTIDGCRVTGKITLDNKNIYD-PNLDVVLLRA-QVGMVFQ 140
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILNlPEKELNKLRAeQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KP----NPFPKsIFDNVAYGPKLHglarDKYDLEEIVENSLR--KAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVS 214
Cdd:PRK09473 105 DPmtslNPYMR-VGEQLMEVLMLH----KGMSKAEAFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 215 PEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTE 292
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSI 259
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
50-253 |
3.06e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 50 EIKisaqDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrMNdtIDGCRVT-GKITLDNKNIYDpnLDV 128
Cdd:COG0396 2 EIK----NLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MG--HPKYEVTsGSILLDGEDILE--LSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLlRAQVG--MVFQKPNPFP---KSIFDNVAYGpKLHGLARDKYDLEEIVENSLRKAGLWEEVKDR-LNqpgTGLSGGQQ 202
Cdd:COG0396 72 DE-RARAGifLAFQYPVEIPgvsVSNFLRTALN-ARRGEELSAREFLKLLKEKMKELGLDEDFLDRyVN---EGFSGGEK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447014717 203 QRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISEL-SDQYTIVIVTH 253
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrSPDRGILIITH 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
67-259 |
3.31e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDVvlLRAQVGMVFQKP-NPF 145
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG-----EIFYNNQAITDDNFEK--LRKHIGIVFQNPdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PKSI--FDnVAYGPKLHGLARDKydLEEIVENSLRKAGLWeevkDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:PRK13648 97 VGSIvkYD-VAFGLENHAVPYDE--MHRRVSEALKQVDML----ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 447014717 224 CSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAA 259
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAM 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
54-292 |
3.56e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.67 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 54 SAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNI-YDPN----LDV 128
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL------------SARLAPDAGEVhYRMRdgqlRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 V---------LLRAQVGMVFQKPNpfpksifD----------NVayGPKLHGLARDKYdleeiveNSLR-KAGLW-EEVK 187
Cdd:PRK11701 76 YalseaerrrLLRTEWGFVHQHPR-------DglrmqvsaggNI--GERLMAVGARHY-------GDIRaTAGDWlERVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 188 ---DRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAK----VEELISELsdQYTIVIVTHSMQQAAR 260
Cdd:PRK11701 140 idaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARlldlLRGLVREL--GLAVVIVTHDLAVARL 217
|
250 260 270
....*....|....*....|....*....|..
gi 447014717 261 VSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTE 292
Cdd:PRK11701 218 LAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQ 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
53-264 |
7.47e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdTIDgcrvTGKITLDNKNIYDPNLDVV--- 129
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLL-PPD----SGEVLVDGLDVATTPSRELakr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 --LLRaqvgmvfQKPNPFPK-SIFDNVAYG--PKLHG--LARDkydlEEIVENSLRKAGLwEEVKDR-LNQpgtgLSGGQ 201
Cdd:COG4604 77 laILR-------QENHINSRlTVRELVAFGrfPYSKGrlTAED----REIIDEAIAYLDL-EDLADRyLDE----LSGGQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 202 QQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADH 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
62-264 |
9.83e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 9.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDG--CRVTGKITLDNKNIYD-PNLDVvllrAQVGMV 138
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVF-------NCLTGfyKPTGGTILLRGQHIEGlPGHQI----ARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 --FQKPNPFPK-SIFDN--VAYGPK-----LHGLARDK-YDLEEivENSLRKAGLWEEV---KDRLNQPGTGLSGGQQQR 204
Cdd:PRK11300 84 rtFQHVRLFREmTVIENllVAQHQQlktglFSGLLKTPaFRRAE--SEALDRAATWLERvglLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
65-293 |
1.30e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.76 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNiydpnLDVVLLR------------ 132
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS-----RQVIELSeqsaaqmrhvrg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKP----NP-FPksIFDNVAYGPKLH-GLARDKYDLEeiVENSLRKAGLwEEVKDRLNQPGTGLSGGQQQRLC 206
Cdd:PRK10261 104 ADMAMIFQEPmtslNPvFT--VGEQIAESIRLHqGASREEAMVE--AKRMLDQVRI-PEAQTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 207 IARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYT--IVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
....*....
gi 447014717 285 QPDHQLTEA 293
Cdd:PRK10261 259 APQHPYTRA 267
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
53-286 |
1.39e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTlnrMNDTIDgcRVTGKITLDNKNIYdpNLDVVLLR 132
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRA---INGTLT--PTAGTVLVAGDDVE--ALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPN-PFPKSIFDNVAYG--PKLHGLARDKYDLEEIVENSLRKAGlweeVKDRLNQPGTGLSGGQQQRLCIAR 209
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGrtPHRSRFDTWTETDRAAVERAMERTG----VAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQP 286
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
53-256 |
1.74e-19 |
|
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: 84.44 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGD-----FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrMNDTIdgcRVTGKITLDNKniydpnld 127
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELE---KLSGSVSVPGS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 vvllraqVGMVFQKPNPFPKSIFDNVaygpkLHGLARDKYDLEEIVEN-SLRK------AGLWEEVKDRlnqpGTGLSGG 200
Cdd:cd03250 68 -------IAYVSQEPWIQNGTIRENI-----LFGKPFDEERYEKVIKAcALEPdleilpDGDLTEIGEK----GINLSGG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 201 QQQRLCIARTIAVSPEVILMDEPCSALDPiATAK--VEELI-SELSDQYTIVIVTHSMQ 256
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDA-HVGRhiFENCIlGLLLNNKTRILVTHQLQ 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
67-289 |
1.75e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNlDVVLLRAQVGMVFQKPNP-- 144
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP-----QKGKVLVSGIDTGDFS-KLQGIRKLVGIVFQNPETqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 145 FPKSIFDNVAYGPKlhGLARDKYDLEEIVENSLRKAGLweeVKDRLNQPGTgLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK13644 91 VGRTVEEDLAFGPE--NLCLPPIEIRKRVDRALAEIGL---EKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 225 SALDPIATAKVEELISELSDQ-YTIVIVTHSMQQaARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQ 289
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
68-293 |
2.09e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.52 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKStfLRTLNRMNDTIDGCRVT-GKITLDNKniydPNLDVVLLRAQVGMVFQKPnpfp 146
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTaGRVLLDGK----PVAPCALRGRKIATIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFD---NVAYGPKLHGLARDKYDLEEIVENSLRKAGLwEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:PRK10418 89 RSAFNplhTMHTHARETCLALGKPADDATLTAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 224 CSALDPIATAKVEELISELSDQYT--IVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEA 293
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRS 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
56-253 |
2.19e-19 |
|
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: 84.12 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 56 QDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRtlnrmndTIDGC---RVT-GKITLDNKNIYDPNLDVvll 131
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK-------TIMGHpkyEVTeGEILFKGEDITDLPPEE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVG--MVFQKPnpfpksifdnvaygPKLHGLArdkydleeiVENSLRKaglweevkdrLNQpgtGLSGGQQQRLCIAR 209
Cdd:cd03217 74 RARLGifLAFQYP--------------PEIPGVK---------NADFLRY----------VNE---GFSGGEKKRNEILQ 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTH 253
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEgKSVLIITH 162
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
68-264 |
3.45e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.06 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDV-VLLRAQ-VGMVFQKPNPF 145
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDG-----SSGEVSLVGQPLHQMDEEArAKLRAKhVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PK-SIFDNVAYGPKLHGlARDKYDLEEIVEnSLRKAGLWEevkdRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK10584 101 PTlNALENVELPALLRG-ESSRQSRNGAKA-LLEQLGLGK----RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447014717 225 SALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRR 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-257 |
4.67e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.21 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 39 EPHASKKPNSTE--IKISAQDAHVYYGDFEAIKG-IDLDIYQNEVIAFIGPSGCGKSTFLRTL-----NRMNDTIDGCRV 110
Cdd:PRK11174 334 HPQQGEKELASNdpVTIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQGSLKINGIEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 111 TgkitldnkniydpNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAygpklhgLARDKYDlEEIVENSLRKAGLWE------ 184
Cdd:PRK11174 414 R-------------ELDPESWRKHLSWVGQNPQLPHGTLRDNVL-------LGNPDAS-DEQLQQALENAWVSEflpllp 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 185 -----EVKDRlnqpGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQ 257
Cdd:PRK11174 473 qgldtPIGDQ----AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
66-300 |
6.24e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDvvlLRAQ-VGMVFQKP-- 142
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP-----TSGELLIDDHPLHFGDYS---YRSQrIRMIFQDPst 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 --NPFPK--SIFD-NVAYGPKLHGLARdkydlEEIVENSLRKAGLweeVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:PRK15112 99 slNPRQRisQILDfPLRLNTDLEPEQR-----EKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
....*
gi 447014717 296 TGRFG 300
Cdd:PRK15112 251 AGHFG 255
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
59-250 |
8.80e-19 |
|
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: 86.41 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 59 HV---YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtIDGcrvtGKITLDNKNIYDPNLDVvlLRAQV 135
Cdd:COG5265 362 NVsfgYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD-VTS----GRILIDGQDIRDVTQAS--LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 136 GMVFQKPNPFPKSIFDNVAYGpklhglaRDKYDLEEIVE-----------NSLRKaGLWEEVKDRlnqpGTGLSGGQQQR 204
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYG-------RPDASEEEVEAaaraaqihdfiESLPD-GYDTRVGER----GLKLSGGEKQR 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELS-DQYTIVI 250
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVArGRTTLVI 549
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
85-277 |
8.84e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.84 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 85 GPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNI--YDPNLdvvlLRAQVGMVFQKPNPFPKSIFDNVAYGPKLHGL 162
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISP-----TSGTLLFEGEDIstLKPEI----YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 163 ARDkydlEEIVENSLRKAGLWEEVkdrLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISEL 242
Cdd:PRK10247 111 QPD----PAIFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRY 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447014717 243 SDQYTIVI--VTHS---MQQAARVSDRTAyfHLGDLIEVN 277
Cdd:PRK10247 184 VREQNIAVlwVTHDkdeINHADKVITLQP--HAGEMQEAR 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
62-299 |
9.63e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.40 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTflrTLNRMNDTIDgcRVTGKITLDNKNIYDPNLDVVLLRAqVGMVFQK 141
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDISLLPLHARARRG-IGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPFPK-SIFDNvaygpkLHGLARDKYDLEEiVENSLRKAGLWEE--VKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PRK10895 87 ASIFRRlSVYDN------LMAVLQIRDDLSA-EQREDRANELMEEfhIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQYTIVIVT-HSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTqpDHQLTEAYITG 297
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ--DEHVKRVYLGE 237
|
..
gi 447014717 298 RF 299
Cdd:PRK10895 238 DF 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
62-274 |
1.11e-18 |
|
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: 83.15 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKITLDNKNIYdpnldvvllRAQVGMVFQ 140
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGeVRVAGLVPWKRRKKF---------LRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFpksIFDNvaygPKLHGLA--RDKYDLEEiVENSLRKAGLWE--EVKDRLNQPGTGLSGGQQQRLCIARTIAVSPE 216
Cdd:cd03267 102 QKTQL---WWDL----PVIDSFYllAAIYDLPP-ARFKKRLDELSEllDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 217 VILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
63-263 |
1.44e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidGCRV---TGKITLDNKNIydPNLDVVLL---RAQVG 136
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI--------GGQIapdHGEILFDGENI--PAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 137 MVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYdLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSP 215
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHTQLPAPL-LHSTVMMKLEAVGL----RGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447014717 216 EVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSD 263
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIAD 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
67-265 |
1.67e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.48 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRmNDTIDGcrvtGKITLDNKniyDPNLDVV---------LLRAQVGM 137
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPDS----GSILVRHD---GGWVDLAqaspreilaLRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 138 VFQkpnpFPKSIfdnvaygPKLHGLardkydleEIVENSLRKAGLWEEVK--------DRLN--------QPGTgLSGGQ 201
Cdd:COG4778 98 VSQ----FLRVI-------PRVSAL--------DVVAEPLLERGVDREEArararellARLNlperlwdlPPAT-FSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 202 QQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYT-IVIVTHSMQQAARVSDRT 265
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVADRV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
67-291 |
3.89e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtidgCRVTGKITLDNKNIYDPNLDVVL-LRAQVGMVFQKPNPF 145
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNLNRRQLLpVRHRIQVVFQDPNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 --PK-SIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLnqPgTGLSGGQQQRLCIARTIAVSPEVILMDE 222
Cdd:PRK15134 375 lnPRlNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRY--P-AEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 223 PCSALDPIATAKVEELISELSDQYTI--VIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLT 291
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
67-273 |
5.41e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 84.29 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGkitldNKNIyDPNLDVVllRAQVGMVFQKPNPFP 146
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-----GKDI-ETNLDAV--RQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYGPKLHGLARDKYDLEeiVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:TIGR01257 1017 HlTVAEHILFYAQLKGRSWEEAQLE--MEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447014717 226 ALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDL 273
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
68-253 |
1.77e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndtidG--CRVTGKITLdnkniydPNLDVVLlraqvgmvF--QKPN 143
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA-------GlwPYGSGRIAR-------PAGARVL--------FlpQRPY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 PFPKSIFDNVAYgPKlhglARDKYDLEEIVEnSLRKAGLwEEVKDRLNQP---GTGLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:COG4178 437 LPLGTLREALLY-PA----TAEAFSDAELRE-ALEAVGL-GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|...
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
46-264 |
1.82e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 46 PNSTEIkISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNdTIDgcrvTGKITLDNKNIydPN 125
Cdd:PRK13537 2 PMSVAP-IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT-HPD----AGSISLCGEPV--PS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 126 lDVVLLRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKydLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQR 204
Cdd:PRK13537 74 -RARHARQRVGVVPQFDNLDPDfTVRENLLVFGRYFGLSAAA--ARALVPPLLEFAKL----ENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKV-EELISELSDQYTIVIVTHSMQQAARVSDR 264
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
62-283 |
3.56e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVVLLRAQVGMVFQK 141
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-----QKGAVLWQGKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNP--FPKSIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAglweEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:PRK13638 86 PEQqiFYTDIDSDIAFSLRNLGVPEA--EITRRVDEALTLV----DAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYT-IVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVF 283
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
68-252 |
5.09e-17 |
|
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: 78.08 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtiDGCRVTGKITLDNKNiydpnLDVVLLRAQVGMVFQKPNPFPK 147
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGQP-----RKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 -SIFDNVAYGP--KLHGLARDKYDLEEIVENSLRKAGLwEEVKDRLNQpgtGLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:cd03234 96 lTVRETLTYTAilRLPRKSSDAIRKKRVEDVLLRDLAL-TRIGGNLVK---GISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|....*...
gi 447014717 225 SALDPIATAKVEELISELSDQYTIVIVT 252
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
68-253 |
5.19e-17 |
|
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: 81.14 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFPK 147
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSG-----EILFDGIPREEIPREV--LANSVAMVDQDIFLFEG 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 SIFDNVAY------GPKLHGLARDKYDLEEIVEnslRKAGLWEEvkdrLNQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:TIGR03796 568 TVRDNLTLwdptipDADLVRACKDAAIHDVITS---RPGGYDAE----LAEGGANLSGGQRQRLEIARALVRNPSILILD 640
|
170 180 190
....*....|....*....|....*....|..
gi 447014717 222 EPCSALDPIATAKVEELISELSdqYTIVIVTH 253
Cdd:TIGR03796 641 EATSALDPETEKIIDDNLRRRG--CTCIIVAH 670
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
62-264 |
7.81e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.46 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFlrtlnrMN--------DtidgcrvTGKITLDNK--NIYDPNldvVLL 131
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKilyglyqpD-------SGEILIDGKpvRIRSPR---DAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 RAQVGMVFQKPNPFPK-SIFDNVAYG-PKLHGLARDKYDLEEIVENSLRKAGL----WEEVKDrlnqpgtgLSGGQQQRL 205
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGlEPTKGGRLDRKAARARIRELSERYGLdvdpDAKVED--------LSVGEQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADR 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
60-293 |
1.00e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.02 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGD----FEAIKGIDLDIYQNEVIAFIGPSGCGKStfLRTLNRMNdTIDgcrVTGKITLDNKNIYDPNLDVV------ 129
Cdd:PRK11022 11 VHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMG-LID---YPGRVMAEKLEFNGQDLQRIsekerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 -LLRAQVGMVFQKP----NPFPKSIFdNVAYGPKLHGLARDKYDLEEIVEnSLRKAGLwEEVKDRLNQPGTGLSGGQQQR 204
Cdd:PRK11022 85 nLVGAEVAMIFQDPmtslNPCYTVGF-QIMEAIKVHQGGNKKTRRQRAID-LLNQVGI-PDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|.
gi 447014717 283 FTQPDHQLTEA 293
Cdd:PRK11022 242 FRAPRHPYTQA 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
63-285 |
1.40e-16 |
|
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: 79.85 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcRVTGKITLDNKNIYDPNLDvvlLRAQV----GMV 138
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG-EVNVRVGDEWVDMTKPGPD---GRGRAkryiGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 FQKPNPFP-KSIFDNV--AYGPKL-HGLARDKydleeiVENSLRKAGLWEE-VKDRLNQPGTGLSGGQQQRLCIARTIAV 213
Cdd:TIGR03269 371 HQEYDLYPhRTVLDNLteAIGLELpDELARMK------AVITLKMVGFDEEkAEEILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELI----SELSDqyTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQ--TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
53-282 |
5.00e-16 |
|
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: 77.92 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMND------------------------TIDG- 107
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverpSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 108 -CRVTG-KITLDNKNIYDPNLDVVL-LRAQVGMVFQKPNPF--PKSIFDNVaygpkLHGLARDKYDLEEIVEnslRKAGL 182
Cdd:TIGR03269 81 pCPVCGgTLEPEEVDFWNLSDKLRRrIRKRIAIMLQRTFALygDDTVLDNV-----LEALEEIGYEGKEAVG---RAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 183 WEEVK--DRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQA 258
Cdd:TIGR03269 153 IEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVI 232
|
250 260
....*....|....*....|....
gi 447014717 259 ARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-255 |
5.36e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.53 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 52 KISAQDAHVYYG---DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtGKITLDNKNIYDPNLDv 128
Cdd:PTZ00265 382 KIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG----DIIINDSHNLKDINLK- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vLLRAQVGMVFQKPNPFPKSIFDNVAYgpKLHGL----------------------------ARDKYDLEEIVeNSLRKA 180
Cdd:PTZ00265 457 -WWRSKIGVVSQDPLLFSNSIKNNIKY--SLYSLkdlealsnyynedgndsqenknkrnscrAKCAGDLNDMS-NTTDSN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 181 GL------WEEVKDR-------------------------LNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDP 229
Cdd:PTZ00265 533 ELiemrknYQTIKDSevvdvskkvlihdfvsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260
....*....|....*....|....*...
gi 447014717 230 IATAKVEELISEL--SDQYTIVIVTHSM 255
Cdd:PTZ00265 613 KSEYLVQKTINNLkgNENRITIIIAHRL 640
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
55-268 |
7.65e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 55 AQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNIYDPNldvvllRAQ 134
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL------------AGELEPDSGEVSIPK------GLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 135 VGMVFQKPNPFP-KSIFDNVAYGpkLHGLARDKYDLEEI----------------VENSLRKAGLWE---EVK------- 187
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDG--DAELRALEAELEELeaklaepdedlerlaeLQEEFEALGGWEaeaRAEeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 188 ---DRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpIATakVEELISELSD-QYTIVIVTHsmqqaarvsD 263
Cdd:COG0488 141 fpeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES--IEWLEEFLKNyPGTVLVVSH---------D 208
|
....*
gi 447014717 264 RtaYF 268
Cdd:COG0488 209 R--YF 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
64-256 |
1.04e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.29 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFL-RTLNRMNdtidgcRVTGKITLDNKNIYDPNLDVVLLRAQ--VGMVFQ 140
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ------TLEGKVHWSNKNESEPSFEATRSRNRysVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPKSIFDNVAYGPKL----HGLARDKYDLEEIVEnsLRKAGLWEEVKDRlnqpGTGLSGGQQQRLCIARTIAVSPE 216
Cdd:cd03290 87 KPWLLNATVEENITFGSPFnkqrYKAVTDACSLQPDID--LLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447014717 217 VILMDEPCSALD-PIATAKVEELISEL--SDQYTIVIVTHSMQ 256
Cdd:cd03290 161 IVFLDDPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQ 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
111-272 |
1.06e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 111 TGKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFPKSIFDNVAYGpklhglaRDKYDLEEiVENSLRKAGLWEEVKDRL 190
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKD--LRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATRED-VKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 191 NQ------P-GTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARv 261
Cdd:PTZ00265 1346 NKydtnvgPyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKR- 1424
|
170
....*....|.
gi 447014717 262 SDRTAYFHLGD 272
Cdd:PTZ00265 1425 SDKIVVFNNPD 1435
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
66-292 |
1.62e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLDNKNIYdpNLDVVLLRA----QVGMVFQK 141
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLL--HASEQTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 P----NPFpKSIFDNVAYGPKLHGLARDKYDLEEIVeNSLRKAGLwEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:PRK15134 101 PmvslNPL-HTLEKQLYEVLSLHRGMRREAARGEIL-NCLDRVGI-RQAAKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTE 292
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
53-269 |
1.92e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 71.71 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNkniydpnldvvllr 132
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------AGELEPDE-------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 aqvGMVFQKPNPfpksifdNVAYgpklhglardkydleeivenslrkaglweevkdrLNQpgtgLSGGQQQRLCIARTIA 212
Cdd:cd03221 55 ---GIVTWGSTV-------KIGY----------------------------------FEQ----LSGGEKMRLALAKLLL 86
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISELSDqyTIVIVTHSMQQAARVSDRTAYFH 269
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSHDRYFLDQVATKIIELE 141
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
70-294 |
3.80e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 70 GIDLDIYQNEVIAFIGPSGCGKSTFLrtlNRMNDTIDGcrvTGKITLDNKNIYD-PNLDVVLLRA---QvgmvfQKPNPF 145
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLL---ARMAGLLPG---QGEILLNGRPLSDwSAAELARHRAylsQ-----QQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PKSIFDNVA-YGPKLHGLARDKYDLEEIVEnslrKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIA-VSPEV------ 217
Cdd:COG4138 83 AMPVFQYLAlHQPAGASSEAVEQLLAQLAE----ALGL----EDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegql 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTqpDHQLTEAY 294
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT--PENLSEVF 230
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
68-253 |
3.93e-15 |
|
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: 75.46 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYdpNLDVVLLRAQVGMVFQKPNPFPK 147
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP-----TSGSVRLDGADLK--QWDRETFGKHIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 SIFDNVAYgpklhglARDKYDLEEIVEnSLRKAGLWEEVkdrLNQP----------GTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:TIGR01842 407 TVAENIAR-------FGENADPEKIIE-AAKLAGVHELI---LRLPdgydtvigpgGATLSGGQRQRIALARALYGDPKL 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 447014717 218 ILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTH 253
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKARgITVVVITH 512
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
62-285 |
6.10e-15 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 72.43 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM-NDTidgcrvTGKITLDNKNIYDPNLDvvllraQVGMVFQ 140
Cdd:TIGR03740 10 FGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIlRPT------SGEIIFDGHPWTRKDLH------KIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPK-SIFDNVAYGPKLHGLarDKYDLEEIvensLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:TIGR03740 78 SPPLYENlTARENLKVHTTLLGL--PDSRIDEV----LNIVDLTNTGKKKAKQ----FSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLI---EVNST---EKVFTQ 285
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGyqgKINKSenlEKLFVE 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
65-253 |
1.22e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTL-NRMNDTIDGCRVtgkitldnkniydpnlDVvllraqvgmvfqKPN 143
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLaGALKGTPVAGCV----------------DV------------PDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 PFP--KSIFDNVaygpklhGLARDKYDLEEIvensLRKAGLWEEVKDRlnQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:COG2401 95 QFGreASLIDAI-------GRKGDFKDAVEL----LNAVGLSDAVLWL--RRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 447014717 222 EPCSALDPiATAK-VEELISELSDQY--TIVIVTH 253
Cdd:COG2401 162 EFCSHLDR-QTAKrVARNLQKLARRAgiTLVVATH 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
71-282 |
1.72e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQNEVIAFIGPSGCGKSTFLrtlnrmnDTIDGCRV--TGKITLDNKNIYDPNLDVVLLRAQ--VGMVFQKPNPFP 146
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLI-------NAISGLTRpqKGRIVLNGRVLFDAEKGICLPPEKrrIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYGPKlhglARDKYDLEEIVEnslrKAGLwEEVKDRLnqPGTgLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:PRK11144 90 HyKVRGNLRYGMA----KSMVAQFDKIVA----LLGI-EPLLDRY--PGS-LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 226 ALD-PiatAKVEEL--ISELSDQYTIVI--VTHSMQQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:PRK11144 158 SLDlP---RKRELLpyLERLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
61-264 |
1.81e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNK--NIYDPNLDVVLlraQVGMV 138
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-----TKGTITINNInyNKLDHKLAAQL---GIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 FQKPNPFPK-SIFDNVAYG----PKLHGL-ARDKYDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIA 212
Cdd:PRK09700 86 YQELSVIDElTVLENLYIGrhltKKVCGVnIIDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447014717 213 VSPEVILMDEPCSALDPIATAKVEELISEL-SDQYTIVIVTHSMQQAARVSDR 264
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDR 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
75-294 |
1.84e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 75 IYQNEVIAFIGPSGCGKSTFlrtLNRMNDTIDGcrvTGKITLDNKNIYD-PNLDVVLLRA---QvgmvfQKPNPFPKSIF 150
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPLEAwSAAELARHRAylsQ-----QQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 151 DNVA-YGPKLHGLARDKYDLEEIVEnSLRkaglweeVKDRLNQPGTGLSGGQQQR-------LCIARTIAVSPEVILMDE 222
Cdd:PRK03695 88 QYLTlHQPDKTRTEAVASALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 223 PCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPdhQLTEAY 294
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE--NLAQVF 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
67-253 |
4.18e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.44 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFP 146
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-----DIRFHDIPLTKLQLDS--WRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYG------PKLHGLARdkydLEEIVENSLR-KAGLWEEVKDRlnqpGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:PRK10789 403 DTVANNIALGrpdatqQEIEHVAR----LASVHDDILRlPQGYDTEVGER----GVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190
....*....|....*....|....*....|....
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
47-253 |
4.79e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 47 NSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMND-TIdgcrVTGKITLDNKNIYDPN 125
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAyKI----LEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 126 LDvvlLRAQVG--MVFQKPNPFP---KSIFDNVAYGPKLHGLARDKYD-LE--EIVENSLRKAGLWEEVKDR-LNQpgtG 196
Cdd:CHL00131 78 PE---ERAHLGifLAFQYPIEIPgvsNADFLRLAYNSKRKFQGLPELDpLEflEIINEKLKLVGMDPSFLSRnVNE---G 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 197 LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYT-IVIVTH 253
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENsIILITH 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
67-273 |
7.08e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.61 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIydpnldvvllraqvgmvfqKPNPFP 146
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL-RPPAS----GEITLDGKPV-------------------TRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYGP---KLHGLARDkydlEEIVENslrkAGLweevkdrlnqpGTGLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:cd03215 71 DAIRAGIAYVPedrKREGLVLD----LSVAEN----IAL-----------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447014717 224 CSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDL 273
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
53-275 |
8.96e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNI-YDPNLDVVLL 131
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL------------AGELEPDSGTVkLGETVKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 rAQVGMVFqKPNpfpKSIFDNVAYGpklhglARDKYDLEeiVENSLRK---AGlweevkDRLNQPGTGLSGGQQQRLCIA 208
Cdd:COG0488 384 -DQHQEEL-DPD---KTVLDELRDG------APGGTEQE--VRGYLGRflfSG------DDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 209 RTIAVSPEVILMDEPCSALDpIATakVEELISELSDqY--TIVIVTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLD-IET--LEALEEALDD-FpgTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-264 |
9.57e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 38 FEPHASKKPNSTEIKISAQDAHVYYGDF--EAIKGidlDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKIT 115
Cdd:PRK13409 326 FEERPPRDESERETLVEYPDLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLL------------AGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 116 LDNKNIyDPNLDvvllraqvgmvfqkpnpfpksifdnVAYGPKlhglaRDKYDLEEIVENSLRKAG-------LWEEVKD 188
Cdd:PRK13409 391 PDEGEV-DPELK-------------------------ISYKPQ-----YIKPDYDGTVEDLLRSITddlgssyYKSEIIK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 189 RLN------QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALD---PIATAKVEELISELSDQyTIVIVTHSMQQAA 259
Cdd:PRK13409 440 PLQlerlldKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRIAEEREA-TALVVDHDIYMID 518
|
....*
gi 447014717 260 RVSDR 264
Cdd:PRK13409 519 YISDR 523
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
66-262 |
1.29e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGCRVTGKITLdnkNIYDPNLDVVLLRAQVGMVFQKPNPF 145
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM---SKLSSAAKAELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PK-SIFDNVAYgPKLHGLARDKYDLEEIVEnSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVILMDEPC 224
Cdd:PRK11629 100 PDfTALENVAM-PLLIGKKKPAEINSRALE-MLAAVGLEHRANHRPSE----LSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447014717 225 SALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVS 262
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMS 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
50-271 |
1.41e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 50 EIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKiTLDNKNIydpnldv 128
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeAWLFGQ-PVDAGDI------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vLLRAQVG-M-----------VFQkpnpfpksifdNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGtG 196
Cdd:NF033858 336 -ATRRRVGyMsqafslygeltVRQ-----------NLELHARLFHLPAA--EIAARVAEMLERFDL-ADVADAL--PD-S 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 197 LSGGQQQRLCIArtIAV--SPEVILMDEPCSALDPIATAKVEELISELS--DQYTIVIVTHSMQQAARVsDRTAYFHLG 271
Cdd:NF033858 398 LPLGIRQRLSLA--VAVihKPELLILDEPTSGVDPVARDMFWRLLIELSreDGVTIFISTHFMNEAERC-DRISLMHAG 473
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
66-264 |
1.45e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTlnrmndtIDGCR--VTGKITLDNK--NIYDP----NLDVVLL---RAQ 134
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARA-------LFGADpaDSGEIRLDGKpvRIRSPrdaiRAGIAYVpedRKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 135 VGMVFqkpnpfPKSIFDNVAYgPKLHGLAR----DKYDLEEIVENSLRKAGlweeVK-DRLNQPGTGLSGGQQQRLCIAR 209
Cdd:COG1129 339 EGLVL------DLSIRENITL-ASLDRLSRggllDRRRERALAEEYIKRLR----IKtPSPEQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 210 TIAVSPEVILMDEPcsaldpiaT------AKVE--ELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:COG1129 408 WLATDPKVLILDEP--------TrgidvgAKAEiyRLIRELAAEgKAVIVISSELPELLGLSDR 463
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
61-253 |
1.63e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTfLRTLNRMNDTIDgcrvTGKITLDNKNIydPNLDVVLLRAQVGMVFQ 140
Cdd:PRK10790 350 YRDDNLVLQNINLSVPSRGFVALVGHTGSGKST-LASLLMGYYPLT----EGEIRLDGRPL--SSLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPKSIFDNVAygpklhgLARDKYdlEEIVENSLRKAGLWEEVKD-------RLNQPGTGLSGGQQQRLCIARTIAV 213
Cdd:PRK10790 423 DPVVLADTFLANVT-------LGRDIS--EEQVWQALETVQLAELARSlpdglytPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
53-254 |
2.55e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNL--DVVL 130
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-----AAGTIKLDGGDIDDPDVaeACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 LRAQVGMvfqKPNpfpKSIFDNVAYGPKLHGlardkyDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIART 210
Cdd:PRK13539 78 LGHRNAM---KPA---LTVAENLEFWAAFLG------GEELDIAAALEAVGL----APLAHLPFGYLSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447014717 211 IAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIV-THS 254
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAaTHI 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
53-253 |
5.57e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.12 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTL-NRMNDTIDGcrvtGKITLDNKNI--YDPNldvv 129
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLaGREDYEVTG----GTVEFKGKDLleLSPE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 lLRAQVG--MVFQKPNPFP---KSIFDNVAYGP--KLHGL-ARDKYDLEEIVENSLRKAGLWEEVKDRlnQPGTGLSGGQ 201
Cdd:PRK09580 74 -DRAGEGifMAFQYPVEIPgvsNQFFLQTALNAvrSYRGQePLDRFDFQDLMEEKIALLKMPEDLLTR--SVNVGFSGGE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447014717 202 QQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSD-QYTIVIVTH 253
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTH 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
53-288 |
8.14e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLN---RMNDTIDGCRVTGKITLDNKNIYD-PNLDV 128
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 VLLRAqvgMVFQKPNP-FPKSIFDNVAYGPKLHGLARDKYDLE--EIVENSLRKAGlweeVKDRLNQPGTGLSGGQQQRL 205
Cdd:PRK13547 82 ARLRA---VLPQAAQPaFAFSAREIVLLGRYPHARRAGALTHRdgEIAWQALALAG----ATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIA---------VSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVT--HSMQQAARVSDRTAYFHLGDLI 274
Cdd:PRK13547 155 QFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHADRIAMLADGAIV 234
|
250
....*....|....
gi 447014717 275 EVNSTEKVFTqPDH 288
Cdd:PRK13547 235 AHGAPADVLT-PAH 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
66-264 |
9.34e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNI----YDPNLDVVLLRAQVGMVF-Q 140
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML------------TGILVPTSGEVrvlgYVPFKRRKEFARRIGVVFgQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 K-------PnpfPKSIFDNVAygpKLHGLARDKYD--LEEIVEnslrkaGLweEVKDRLNQPGTGLSGGQQQRLCIArti 211
Cdd:COG4586 104 RsqlwwdlP---AIDSFRLLK---AIYRIPDAEYKkrLDELVE------LL--DLGELLDTPVRQLSLGQRMRCELA--- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 212 AV---SPEVILMDEPCSALDPIATAKVEELISELSDQY--TIVIVTHSMQQAARVSDR 264
Cdd:COG4586 167 AAllhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDR 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
79-274 |
1.10e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 79 EVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDpnLDVVLLRAQVGMVFQK-PNPFPKSIFDNVAYG- 156
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPP-----SEGEILLDAQPLES--WSSKAFARKVAYLPQQlPAAEGMTVRELVAIGr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 157 -PkLHG-LARDKYDLEEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAK 234
Cdd:PRK10575 111 yP-WHGaLGRFGAADREKVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447014717 235 VEELISELSDQ--YTIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:PRK10575 186 VLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-264 |
8.17e-12 |
|
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: 65.58 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 38 FEPHASKKPNSTEIKISAQDAHVYYGDF--EAIKGidlDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKIT 115
Cdd:COG1245 327 FEVHAPRREKEEETLVEYPDLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKIL------------AGVLK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 116 LDNKNIyDPNLDvvllraqvgmvfqkpnpfpksifdnVAYGPklhglardKY---DLEEIVENSLRKAG--------LWE 184
Cdd:COG1245 392 PDEGEV-DEDLK-------------------------ISYKP--------QYispDYDGTVEEFLRSANtddfgssyYKT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 185 EVKDRLN------QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALD---PIATAKVEELISELSDQYTIViVTHSM 255
Cdd:COG1245 438 EIIKPLGleklldKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRFAENRGKTAMV-VDHDI 516
|
....*....
gi 447014717 256 QQAARVSDR 264
Cdd:COG1245 517 YLIDYISDR 525
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
66-273 |
1.60e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndtidGCR--VTGKITLDNKNIydpNLDVVLLRAQVGMVFqkpn 143
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLY-------GLRpaRGGRIMLNGKEI---NALSTAQRLARGLVY---- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 pFPKsifDNVAYGpkLHGLARDKYDLEEIVENSLrkaGLW-EEVKDR----------------LNQPGTGLSGGQQQRLC 206
Cdd:PRK15439 343 -LPE---DRQSSG--LYLDAPLAWNVCALTHNRR---GFWiKPARENavleryrralnikfnhAEQAARTLSGGNQQKVL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 207 IARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHS-MQQAARVSDRTAYFHLGDL 273
Cdd:PRK15439 414 IAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSdLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
80-284 |
1.74e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 80 VIAFIGPSGCGKSTFLRTLnrmndtIDGCRVT-GKITldnknIYDPNLDVVLLRAQVGMVFQKPN---PFPKSIFDNVAY 155
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKAL------MGFVRLAsGKIS-----ILGQPTRQALQKNLVAYVPQSEEvdwSFPVLVEDVVMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 156 GPKLHG--LARDKYDLEEIVENSLRKAGLWEEvkdRLNQPGTgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATA 233
Cdd:PRK15056 104 GRYGHMgwLRRAKKRDRQIVTAALARVDMVEF---RHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447014717 234 KVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHlGDLIEVNSTEKVFT 284
Cdd:PRK15056 180 RIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFT 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
64-285 |
2.16e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIyDPN--LDVVllraQVGMVFQK 141
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDI-SPRspLDAV----KKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNP-----FPK-SIFDNVAYGPKLHgLARDKYDLEEIVENSLRKAGlwEEVKDRL-------NQPGTGLSGGQQQRLCIA 208
Cdd:PRK09700 345 ESRrdngfFPNfSIAQNMAISRSLK-DGGYKGAMGLFHEVDEQRTA--ENQRELLalkchsvNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 209 RTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
53-253 |
2.47e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNR---MNDtidgcrvtGKITLDNkniydpnlDVV 129
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD--------GRIIYEQ--------DLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 LLRAQvgmvfQKPnpfPK----SIFDNVAYGPK------------LHGLARDKYD--LEEI--VENSLRKAGLWE---EV 186
Cdd:PRK11147 68 VARLQ-----QDP---PRnvegTVYDFVAEGIEeqaeylkryhdiSHLVETDPSEknLNELakLQEQLDHHNLWQlenRI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 187 KDRLNQPG-------TGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELIseLSDQYTIVIVTH 253
Cdd:PRK11147 140 NEVLAQLGldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQGSIIFISH 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
63-295 |
3.21e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgCRVTG---KITLDNKNIYDPNLDVVLLRAQ----- 134
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAI---------CGVTKdnwRVTADRMRFDDIDLLRLSPRERrklvg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 135 --VGMVFQKP----NP---FPKSIFDNV-AYGPKLHGLARDKYDLEEIVEnSLRKAGLwEEVKDRLNQPGTGLSGGQQQR 204
Cdd:PRK15093 89 hnVSMIFQEPqsclDPserVGRQLMQNIpGWTYKGRWWQRFGWRKRRAIE-LLHRVGI-KDHKDAMRSFPYELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 205 LCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELS--DQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKV 282
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
250
....*....|...
gi 447014717 283 FTQPDHQLTEAYI 295
Cdd:PRK15093 247 VTTPHHPYTQALI 259
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
63-255 |
9.95e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 63 GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIYDPN---LDVVLLRAQVgmVF 139
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD-----KVEGHVHMKGSVAYVPQqawIQNDSLRENI--LF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKP--NPFPKSIFDNVAYGPKLHGLARDkyDLEEIVENslrkaglweevkdrlnqpGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:TIGR00957 722 GKAlnEKYYQQVLEACALLPDLEILPSG--DRTEIGEK------------------GVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447014717 218 ILMDEPCSALDP-IATAKVEELISE--LSDQYTIVIVTHSM 255
Cdd:TIGR00957 782 YLFDDPLSAVDAhVGKHIFEHVIGPegVLKNKTRILVTHGI 822
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
79-261 |
2.19e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 79 EVIAFIGPSGCGKSTFLrtlNRMNDTIDGCRVTGKITLDNKNIYDPNLDVVLLRAQVGMVFQKPNPFPKSIFDNVAYGPK 158
Cdd:PLN03211 95 EILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 159 lhGLARDKYDLeeIVENSLRKAGLWE-EVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEE 237
Cdd:PLN03211 172 --SLTKQEKIL--VAESVISELGLTKcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180
....*....|....*....|....
gi 447014717 238 LISELSdQYTIVIVTHSMQQAARV 261
Cdd:PLN03211 248 TLGSLA-QKGKTIVTSMHQPSSRV 270
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
53-253 |
3.60e-10 |
|
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: 58.52 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGkitldnkniydpnldvvLLR 132
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRIL------------AG-----------------LLR 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 133 AQVGMVFQKPNPFPK---SIFDNVAY-----GPK--------LHGLARDKYDLEEIVENSLRKAGLweevKDRLNQPGTG 196
Cdd:TIGR01189 52 PDSGEVRWNGTPLAEqrdEPHENILYlghlpGLKpelsalenLHFWAAIHGGAQRTIEDALAAVGL----TGFEDLPAAQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 197 LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISE-LSDQYTIVIVTH 253
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
68-252 |
4.32e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidGCRVTGKITLDNKNIydpnlDVVLLRAQVGMVFQKPNPFPK 147
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPI-----DAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 -SIFDNVAYGPKLHgLARDKYDLE--EIVENSLRKAGLWEEVKDRLNQPGT--GLSGGQQQRLCIARTIAVSPEVILMDE 222
Cdd:TIGR00955 114 lTVREHLMFQAHLR-MPRRVTKKEkrERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|
gi 447014717 223 PCSALDPIATAKVEELISELSDQYTIVIVT 252
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
68-254 |
4.36e-10 |
|
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: 57.55 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmndtidGC--RVTGKITLdnkniydpnldvvLLRAQVGMVFQKPnpf 145
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-------GLwpWGSGRIGM-------------PEGEDLLFLPQRP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 pksifdnvaYGPklhglardkydleeivENSLRKAGL--WEEVkdrlnqpgtgLSGGQQQRLCIARTIAVSPEVILMDEP 223
Cdd:cd03223 74 ---------YLP----------------LGTLREQLIypWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|.
gi 447014717 224 CSALDPIATAKVEELISELSdqYTIVIVTHS 254
Cdd:cd03223 119 TSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
84-269 |
1.05e-09 |
|
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: 58.99 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 84 IGPSGCGKSTFLRTLNRMNDTIDGCRVtgkITLDNKNIYDPN---LDVVLLRAQVgmvfqkpnPFPKSIFDNvaygpKLH 160
Cdd:TIGR00954 484 CGPNGCGKSSLFRILGELWPVYGGRLT---KPAKGKLFYVPQrpyMTLGTLRDQI--------IYPDSSEDM-----KRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 161 GLaRDKyDLEEIVENS-----LRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPiataKV 235
Cdd:TIGR00954 548 GL-SDK-DLEQILDNVqlthiLEREGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DV 617
|
170 180 190
....*....|....*....|....*....|....
gi 447014717 236 EELISELSDQYTIVIVThsmqqaarVSDRTAYFH 269
Cdd:TIGR00954 618 EGYMYRLCREFGITLFS--------VSHRKSLWK 643
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
60-268 |
1.05e-09 |
|
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: 59.18 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 60 VYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgkitldnKNIYDPNldvvllrAQVGMVF 139
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-----------EARPQPG-------IKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFP-KSIFDNV--AYGPKLHGLAR------------DKYD--------LEEIVENslrkAGLW------EEVKDRL 190
Cdd:TIGR03719 75 QEPQLDPtKTVRENVeeGVAEIKDALDRfneisakyaepdADFDklaaeqaeLQEIIDA----ADAWdldsqlEIAMDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 191 N-----QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDqyTIVIVTHsmqqaarvsDRt 265
Cdd:TIGR03719 151 RcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH---------DR- 218
|
...
gi 447014717 266 aYF 268
Cdd:TIGR03719 219 -YF 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
67-275 |
1.52e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLdVVLLRAQVGMVFQKPNPFP 146
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP-----DAGSILIDGQEMRFAST-TAALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 K-SIFDNVAYG--PKLHGLardkydleeivensLRKAGLWEEVKDRL---------NQPGTGLSGGQQQRLCIARTIAVS 214
Cdd:PRK11288 93 EmTVAENLYLGqlPHKGGI--------------VNRRLLNYEAREQLehlgvdidpDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 215 PEVILMDEPCSALDPIATAKVEELISELSDQYTIVI-VTHSMQQAARVSDRTAYFHLGDLIE 275
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-271 |
1.53e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 45 KPNSTEIKISAQDAHVYYGDFE-----AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrMNDTIDGcrvTGKITLDNK 119
Cdd:TIGR01271 414 KQNNKARKQPNGDDGLFFSNFSlyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSGR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 120 NIYDPnldvvllraqvgmvfQKPNPFPKSIFDNVaygpkLHGLARDKYDLEEIV-----ENSLRKagLWEEVKDRLNQPG 194
Cdd:TIGR01271 489 ISFSP---------------QTSWIMPGTIKDNI-----IFGLSYDEYRYTSVIkacqlEEDIAL--FPEKDKTVLGEGG 546
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 195 TGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpIATAK--VEELISELSDQYTIVIVTHSMQQAARvSDRTAYFHLG 271
Cdd:TIGR01271 547 ITLSGGQRARISLARAVYKDADLYLLDSPFTHLD-VVTEKeiFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
68-293 |
1.67e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMndtIDGCrvTGKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFPK 147
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM---VEVC--GGEIRVNGREIGAYGLRE--LRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 SIFDNVayGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIART-IAVSPEVILMDEPCSA 226
Cdd:PTZ00243 1399 TVRQNV--DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATAN 1476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 227 LDPIATAKVEELISELSDQYTIVIVTHSMQQAAR-----VSDRTAYFHLGDLIE-VNSTEKVFtqpdHQLTEA 293
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQydkiiVMDHGAVAEMGSPRElVMNRQSIF----HSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
50-287 |
1.77e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 57.23 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 50 EIKIsaQDAHVYYGDF--EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIydPNLD 127
Cdd:cd03288 19 EIKI--HDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDG-----KIVIDGIDI--SKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 128 VVLLRAQVGMVFQKPNPFPKSIFDNVayGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCI 207
Cdd:cd03288 90 LHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 208 ARTIAVSPEVILMDEPCSALDpIATAKVEE--LISELSDQyTIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:cd03288 168 ARAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
..
gi 447014717 286 PD 287
Cdd:cd03288 245 ED 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
67-274 |
2.89e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNIYDPNLDVVL------LRAQVGMVFQ 140
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVL------------TGIYTRDAGSILYLGKEVTFngpkssQEAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNPFPK-SIFDNVAYG------------PKLHGLArDKYdleeivensLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCI 207
Cdd:PRK10762 87 ELNLIPQlTIAENIFLGrefvnrfgridwKKMYAEA-DKL---------LARLNLRFSSDKLVGE----LSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLI 274
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
61-268 |
7.48e-09 |
|
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: 55.11 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 61 YYGDF--EAIKGidlDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKniyDPNLDVvllraqvgmv 138
Cdd:cd03237 9 TLGEFtlEVEGG---SISESEVIGILGPNGIGKTTFIKML------------AGVLKPDEG---DIEIEL---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 139 fqkpnpfpksifDNVAYGP-----KLHGLARDKydLEEIVENSLRKAGLWEEVKDRL------NQPGTGLSGGQQQRLCI 207
Cdd:cd03237 61 ------------DTVSYKPqyikaDYEGTVRDL--LSSITKDFYTHPYFKTEIAKPLqieqilDREVPELSGGELQRVAI 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 208 ARTIAVSPEVILMDEPCSALDP----IATAKVEELIseLSDQYTIVIVTHSMQQAARVSDRTAYF 268
Cdd:cd03237 127 AACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFA--ENNEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-285 |
1.06e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 46 PNSTEIKIsaQDAHVYY--GDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMND------TIDGCRVTgKITLD 117
Cdd:PLN03232 1230 PSRGSIKF--EDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElekgriMIDDCDVA-KFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 118 NkniydpnldvvlLRAQVGMVFQKPNPFPKSIfdnvaygpklhglardKYDLEEIVENSlrKAGLWE-----EVKDRLNQ 192
Cdd:PLN03232 1307 D------------LRRVLSIIPQSPVLFSGTV----------------RFNIDPFSEHN--DADLWEaleraHIKDVIDR 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 193 PGTGL-----------SGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARV 261
Cdd:PLN03232 1357 NPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC 1436
|
250 260
....*....|....*....|....
gi 447014717 262 sDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:PLN03232 1437 -DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
45-271 |
1.13e-08 |
|
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: 55.25 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 45 KPNSTEIKISAQDAHVYYGDFE-----AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrMNDTIDGcrvTGKITLDNK 119
Cdd:cd03291 25 KQENNDRKHSSDDNNLFFSNLClvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 120 NIYDPNLDVVLlraqvgmvfqkpnpfPKSIFDNVAYGpklhgLARDKYDLEEIV-----ENSLRKagLWEEVKDRLNQPG 194
Cdd:cd03291 100 ISFSSQFSWIM---------------PGTIKENIIFG-----VSYDEYRYKSVVkacqlEEDITK--FPEKDNTVLGEGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 195 TGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpIATAK--VEELISELSDQYTIVIVTHSMQQaARVSDRTAYFHLG 271
Cdd:cd03291 158 ITLSGGQRARISLARAVYKDADLYLLDSPFGYLD-VFTEKeiFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
62-263 |
2.08e-08 |
|
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: 54.83 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRM--NDTIDGCRVTGKITLDNKNIYDPNldvvllRAQVGMVF 139
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTE------RAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNPFPK-SIFDNVAYGPKL-HGLARDKYDleeivENSLRKAGLWEEVK---DRLNQPGTGLSGGQQQRLCIARTIAVS 214
Cdd:TIGR02633 85 QELTLVPElSVAENIFLGNEItLPGGRMAYN-----AMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447014717 215 PEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSD 263
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAVCD 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
70-258 |
2.68e-08 |
|
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: 52.88 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 70 GIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNiydpnLDVVLLRAQVGMVFQKPNPFPK-- 147
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-----PLAGRVLLNGGP-----LDFQRDSIARGLLYLGHAPGIKtt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 -SIFDNvaygpkLHGLARDKYDleEIVENSLRKAGLwEEVKDRlnqPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSA 226
Cdd:cd03231 88 lSVLEN------LRFWHADHSD--EQVEEALARVGL-NGFEDR---PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....
gi 447014717 227 LDPIATAKVEELISELSDQYTIVIVT--HSMQQA 258
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTthQDLGLS 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
193-273 |
4.18e-08 |
|
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: 54.06 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 193 PGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLG 271
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
..
gi 447014717 272 DL 273
Cdd:TIGR02633 480 KL 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
53-264 |
5.15e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRtlnrmndTIDGCRV--TGKITLDNKNIY--DPNldv 128
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMK-------IIAGIVPpdSGTLEIGGNPCArlTPA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 129 vlLRAQVG--MVFQKPNPFPK-SIFDNVaygpkLHGLARdKYDLEEIVENSLRKAGlweeVKDRLNQPGTGLSGGQQQRL 205
Cdd:PRK15439 82 --KAHQLGiyLVPQEPLLFPNlSVKENI-----LFGLPK-RQASMQKMKQLLAALG----CQLDLDSSAGSLEVADRQIV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 206 CIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQgVGIVFISHKLPEIRQLADR 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
68-255 |
5.17e-08 |
|
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: 54.18 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDGcrvtgKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFPK 147
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGLNIAKIGLHD--LRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 SIFDNV-AYGpklhglardKYDLEEiVENSLRKAGLWEEVK---DRLN----QPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:TIGR00957 1375 SLRMNLdPFS---------QYSDEE-VWWALELAHLKTFVSalpDKLDhecaEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190
....*....|....*....|....*....|....*.
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYTIVIVTHSM 255
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-256 |
6.50e-08 |
|
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: 53.76 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 40 PHASKK-PNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrvTGKITLDN 118
Cdd:TIGR01271 1206 PHAQKCwPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQIDG 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 119 KNiydpnLDVVLL---RAQVGMVFQKPNPFPKSIFDNVAygpklhglARDKYDLEEI--VENSLRKAGLWEEVKDRLN-- 191
Cdd:TIGR01271 1280 VS-----WNSVTLqtwRKAFGVIPQKVFIFSGTFRKNLD--------PYEQWSDEEIwkVAEEVGLKSVIEQFPDKLDfv 1346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 192 --QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQ 256
Cdd:TIGR01271 1347 lvDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
81-256 |
8.17e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 81 IAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNIY-DPNLDVVLL---RAQVgmvfqkpNPfPKSIFDNVAYG 156
Cdd:PRK11147 348 IALIGPNGCGKTTLLKLM------------LGQLQADSGRIHcGTKLEVAYFdqhRAEL-------DP-EKTVMDNLAEG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 157 PKlhglardkydleEIVENSlRKAGLWEEVKD------RLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpi 230
Cdd:PRK11147 408 KQ------------EVMVNG-RPRHVLGYLQDflfhpkRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD-- 472
|
170 180 190
....*....|....*....|....*....|
gi 447014717 231 atakVE--ELISELSDQY--TIVIVTHSMQ 256
Cdd:PRK11147 473 ----VEtlELLEELLDSYqgTVLLVSHDRQ 498
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
67-292 |
9.65e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 67 AIKGIDLDIYQNEVIAFIGPSGCGKSTflrtlnrMNDTIDGcrvtgkITLDNKNIYDPNLDVVLLRAQVGMVFQKpnpfp 146
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKST-------LSNLIAG------VTMPNKGTVDIKGSAALIAISSGLNGQL----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 kSIFDNVAYGPKLHGLARDKydLEEIVENSLRKAglweEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSA 226
Cdd:PRK13545 101 -TGIENIELKGLMMGLTKEK--IKEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 227 LDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQPDHQLTE 292
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKK 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
80-253 |
1.01e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 80 VIAFIGPSGCGKSTFLRTLNrmndtidG------CRVTGKITLDN--------------KNIYDPNLDVVllraqvgmvf 139
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILS-------GelipnlGDYEEEPSWDEvlkrfrgtelqnyfKKLYNGEIKVV---------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 140 QKPNpfpksifdNVAYGPK-LHGLARD---KYDleeivenslrKAGLWEEVKDRLN------QPGTGLSGGQQQRLCIAR 209
Cdd:PRK13409 164 HKPQ--------YVDLIPKvFKGKVREllkKVD----------ERGKLDEVVERLGlenildRDISELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447014717 210 TIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTH 253
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
82-252 |
1.11e-07 |
|
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: 51.09 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 82 AFIGPSGCGKSTFLRTL-NRMNDTIdgcrVTGKITLDNKniydpnldvvllraqvgmvfQKPNPFPKSIfdnvAYGPKLh 160
Cdd:cd03232 37 ALMGESGAGKTTLLDVLaGRKTAGV----ITGEILINGR--------------------PLDKNFQRST----GYVEQQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 161 glarDKYDLEEIVENSLR-KAGLweevkdrlnqpgTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELI 239
Cdd:cd03232 88 ----DVHSPNLTVREALRfSALL------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170
....*....|...
gi 447014717 240 SELSDQYTIVIVT 252
Cdd:cd03232 152 KKLADSGQAILCT 164
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
70-259 |
1.12e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 70 GIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIY----DPNLDVVLLRAQVGMvfqKPNPF 145
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR-----PDAGEVLWQGEPIRrqrdEYHQDLLYLGHQPGI---KTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 PksiFDNVAYGPKLHGLARDkydleEIVENSLRKAGLweevKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCS 225
Cdd:PRK13538 91 A---LENLRFYQRLHGPGDD-----EALWEALAQVGL----AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 447014717 226 ALDPIATAKVEELISELSDQYTIVIVT--HSMQQAA 259
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTthQDLPVAS 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
62-260 |
2.19e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLrTLnrmndtIDGCRV--TGKITLDNKNIYDPNldvvlLRAQVG--- 136
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SL------IAGARKiqQGRVEVLGGDMADAR-----HRRAVCpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 137 --MvfqkP-----NPFPK-SIFDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRlnqPGTGLSGGQQQR--LC 206
Cdd:NF033858 79 ayM----PqglgkNLYPTlSVFENLDFFGRLFGQDAA--ERRRRIDELLRATGL-APFADR---PAGKLSGGMKQKlgLC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 207 IArtIAVSPEVILMDEPCSALDPIATAKVEELISEL---SDQYTIVIVTHSMQQAAR 260
Cdd:NF033858 149 CA--LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraeRPGMSVLVATAYMEEAER 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
66-245 |
2.32e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 66 EAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMnDTIDGcrvtGKITLDNKNIydPNLDVVLLRAQvgmvfqkpnpf 145
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL-RPPAS----GSIRLDGEDI--TGLSPRERRRL----------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 146 pksifdNVAYGP---KLHGLARDkYDLEE------IVENSLRKAGL--WEEVKDR--------------LNQPGTGLSGG 200
Cdd:COG3845 334 ------GVAYIPedrLGRGLVPD-MSVAEnlilgrYRRPPFSRGGFldRKAIRAFaeelieefdvrtpgPDTPARSLSGG 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447014717 201 QQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ 245
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA 451
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
189-263 |
3.08e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 189 RLNQPGTGLSGGQQQRLCIARTIAVSPE--VILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHS---MQQAARVS 262
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLgNTVILIEHNldvLSSADWII 159
|
.
gi 447014717 263 D 263
Cdd:cd03238 160 D 160
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
71-280 |
3.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQNEVIAFIGPSGCGK----STFLRTLNRMNDTIdgcrvtgkitldnkniydpnldvVLLRAQVGMVFQKPNPFP 146
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKtsliSAMLGELPPRSDAS-----------------------VVIRGTVAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 147 KSIFDNVAYG----PKLHGLARD----KYDLEeivensLRKAGLWEEVKDRlnqpGTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PLN03130 693 ATVRDNILFGspfdPERYERAIDvtalQHDLD------LLPGGDLTEIGER----GVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 219 LMDEPCSALDPIATAKV-EELISELSDQYTIVIVTHSMQQAARVsDRTAYFHLGDLIEVNSTE 280
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYE 824
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
68-256 |
3.67e-07 |
|
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: 50.62 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrvTGKITLDNKNIYDPNLDVvlLRAQVGMVFQKPNPFPK 147
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT------EGDIQIDGVSWNSVPLQK--WRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 SIFDNV-AYGpklhglardKYDLEEI--VENSLRKAGLWEEVKDRLN----QPGTGLSGGQQQRLCIARTIAVSPEVILM 220
Cdd:cd03289 92 TFRKNLdPYG---------KWSDEEIwkVAEEVGLKSVIEQFPGQLDfvlvDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 447014717 221 DEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQ 256
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
64-285 |
4.72e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 64 DFEAIKGIDLDIYQNEVIAFIGPSGCGKSTflrtLNRMndtidgcrVTGKITLDNKNIyDPNLDVVLLRAQVGMVFQKPN 143
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKST----LSNI--------IGGSLSPTVGKV-DRNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 pfpksiFDNVAYGPKLHGLARD--KYDLEEIVENSlrkaglweEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:PRK13546 103 ------IENIEFKMLCMGFKRKeiKAMTPKIIEFS--------ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 222 EPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDRTAYFHLGDLIEVNSTEKVFTQ 285
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQnKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
71-256 |
4.81e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQNEVIAFIGPSGCGKSTFLRT-LNRMNDTIDGCrvtgkitldnkniydpnldvVLLRAQVGMVFQKPNPFPKSI 149
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSS--------------------VVIRGSVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 150 FDNVAYG----PKLHGLARD----KYDLEEIVENSLRKAGlweevkdrlnQPGTGLSGGQQQRLCIARTIAVSPEVILMD 221
Cdd:PLN03232 696 RENILFGsdfeSERYWRAIDvtalQHDLDLLPGRDLTEIG----------ERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190
....*....|....*....|....*....|....*.
gi 447014717 222 EPCSALDP-IATAKVEELISELSDQYTIVIVTHSMQ 256
Cdd:PLN03232 766 DPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLH 801
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
79-273 |
6.32e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 79 EVIAFIGPSGCGKSTFLRTLNRmndtidgcRVT-GKITLDNKNIYDPNLDVVLLRAqVGMVFQKPNPFPKS------IFD 151
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLAE--------RVTtGVITGGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTStvreslRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 152 NVAYGPKlhglARDKYDLEEIVENSLRKAGLwEEVKDRL-NQPGTGLSGGQQQRLCIARTIAVSPEVIL-MDEPCSALDP 229
Cdd:TIGR00956 861 AYLRQPK----SVSKSEKMEYVEEVIKLLEM-ESYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 230 IATAKVEELISELSDQ-YTIVIVTHS-----MQQAARV-----SDRTAYFhlGDL 273
Cdd:TIGR00956 936 QTAWSICKLMRKLADHgQAILCTIHQpsailFEEFDRLlllqkGGQTVYF--GDL 988
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
197-264 |
1.72e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447014717 197 LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMPELLGITDR 460
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
190-273 |
2.16e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 190 LNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISEL-SDQYTIVIVTHSMQQAARVSDRTAYF 268
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkAEGLSIILVSSEMPEVLGMSDRILVM 468
|
....*
gi 447014717 269 HLGDL 273
Cdd:PRK10762 469 HEGRI 473
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
171-252 |
3.44e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 171 EIVE-NSLRKA--GLweevkdrlnqPG-TGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQY 246
Cdd:PLN03140 1000 ELVElDNLKDAivGL----------PGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTG 1069
|
....*.
gi 447014717 247 TIVIVT 252
Cdd:PLN03140 1070 RTVVCT 1075
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
52-229 |
3.93e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 52 KISAQDAHVYYGD--FeAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYDPNLDVv 129
Cdd:PRK10522 322 TLELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP-----QSGEILLDGKPVTAEQPED- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 130 lLRAQVGMVFQKPNPFPKSIfdnvayGPKlhGLARDkydlEEIVENSLRKAGLWEEVKDRLNQ-PGTGLSGGQQQRLCIA 208
Cdd:PRK10522 395 -YRKLFSAVFTDFHLFDQLL------GPE--GKPAN----PALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALL 461
|
170 180
....*....|....*....|.
gi 447014717 209 RTIAVSPEVILMDEPCSALDP 229
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDP 482
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
68-276 |
5.07e-06 |
|
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: 46.49 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNrmNDTIDGCRVTGKITLDNKNiYDPNLDVvlLRAQVGMVFQKPNPFPK 147
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIP-YKEFAEK--YPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 148 sifdnvaygpklhglardkYDLEEIVENSLRKAGlweevkdrlNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSAL 227
Cdd:cd03233 98 -------------------LTVRETLDFALRCKG---------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447014717 228 DPIATAKVEELISELSDQYTIVIVThSMQQAarvSDRTayFHLGDLIEV 276
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFV-SLYQA---SDEI--YDLFDKVLV 192
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
47-266 |
5.68e-06 |
|
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: 47.70 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 47 NSTEIKISAQDAHVYYGDFE-AIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTIDG-CRVTGKITLDN-----K 119
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGKSILTNisdvhQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 120 NI-YDPNLDVV--LLRAQvgmvfqkpnpfpksifDNVAYGPKLHGLARDkyDLEEIVENSLRKAGLwEEVKDRLnqPGTg 196
Cdd:TIGR01257 2013 NMgYCPQFDAIddLLTGR----------------EHLYLYARLRGVPAE--EIEKVANWSIQSLGL-SLYADRL--AGT- 2070
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 197 LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKV-EELISELSDQYTIVIVTHSMQQAARVSDRTA 266
Cdd:TIGR01257 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLA 2141
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
192-284 |
7.07e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 192 QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHS-MQQAARVSDRTAYFHL 270
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSeLPEVLGLSDRVLVMHE 480
|
90
....*....|....*....
gi 447014717 271 G----DLIEVNST-EKVFT 284
Cdd:PRK13549 481 GklkgDLINHNLTqEQVME 499
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
77-251 |
8.16e-06 |
|
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: 47.09 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 77 QNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITlDNKNIYD--PNLDVVLLRAQvGMVFQkpNPFpKSIFDN-- 152
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIL------------SGELK-PNLGDYDeePSWDEVLKRFR-GTELQ--DYF-KKLANGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 153 -VAYGPKLHGLARDKYDLEeiVENSLRKA---GLWEEVKDRLN------QPGTGLSGGQQQRLCIARTIAVSPEVILMDE 222
Cdd:COG1245 161 kVAHKPQYVDLIPKVFKGT--VRELLEKVderGKLDELAEKLGlenildRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180
....*....|....*....|....*....
gi 447014717 223 PCSALDPIATAKVEELISELSDQYTIVIV 251
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLV 267
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
53-255 |
8.20e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 53 ISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTlnrmndtidgcrVTGKITLDNKNI-YDPNLdvvll 131
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRV------------VLGLVAPDEGVIkRNGKL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 132 raQVGMVFQKPN-----PFPKSIFDNVAYGPKlhglardKYDLEEIVENsLRKAGLweevkdrLNQPGTGLSGGQQQRLC 206
Cdd:PRK09544 68 --RIGYVPQKLYldttlPLTVNRFLRLRPGTK-------KEDILPALKR-VQAGHL-------IDAPMQKLSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447014717 207 IARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ--YTIVIVTHSM 255
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDL 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
62-263 |
1.17e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgCRV------TGKITLDN-----KNIYDPNldvvl 130
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL---------SGVyphgtyEGEIIFEGeelqaSNIRDTE----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 131 lRAQVGMVFQKPNPFPK-SIFDNVAYGPKLHGLARDKYDleeivENSLRKAGLWEEVKDRLN--QPGTGLSGGQQQRLCI 207
Cdd:PRK13549 81 -RAGIAIIHQELALVKElSVLENIFLGNEITPGGIMDYD-----AMYLRAQKLLAQLKLDINpaTPVGNLGLGQQQLVEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447014717 208 ARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSD 263
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISD 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
192-264 |
1.39e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 1.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 192 QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSDR 264
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADR 465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
198-285 |
1.57e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 198 SGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKV-EELISELSDQYTIVIVTHSMQQAARVSDRTAYFHLGDLIEV 276
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
....*....
gi 447014717 277 NSTEKVFTQ 285
Cdd:NF000106 226 GKVDELKTK 234
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
71-253 |
1.79e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDiyqNEVIAFIGPSGCGKSTFLRTL----------------NRMNDTIDGCRVTGKITLDNKNIydpnldvVLLRAQ 134
Cdd:COG0419 19 IDFD---DGLNLIVGPNGAGKSTILEAIryalygkarsrsklrsDLINVGSEEASVELEFEHGGKRY-------RIERRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 135 vGMVFQKPNPFP---KSIFDNVAYGPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTG------LSGGQQQRL 205
Cdd:COG0419 89 -GEFAEFLEAKPserKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGldpietLSGGERLRL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447014717 206 CIARTIAvspevILMDEpcSALDPIATAKVEELISELSdqytivIVTH 253
Cdd:COG0419 168 ALADLLS-----LILDF--GSLDEERLERLLDALEELA------IITH 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
70-284 |
2.56e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 70 GIDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIydPNLDVVLLRAQVGMVFQKPNPFPKSI 149
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 150 fdnvaygpklhglardKYDLEEIVENSlrKAGLWE-----EVKD--RLN---------QPGTGLSGGQQQRLCIARTIAV 213
Cdd:PLN03130 1330 ----------------RFNLDPFNEHN--DADLWEsleraHLKDviRRNslgldaevsEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 214 SPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARvSDRTAYFHLGDLIEVNSTEKVFT 284
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
62-228 |
5.08e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 62 YGDFEAIKGIDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITLDNKNI-YDPNldvvllrAQVGMVFQ 140
Cdd:PRK15064 329 FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL------------VGELEPDSGTVkWSEN-------ANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 141 KPNP-FPK--SIFDNVAYgpklhglARDKYDLEEIVENSLRKAgLWEEvkDRLNQPGTGLSGGQQQRLCIARTIAVSPEV 217
Cdd:PRK15064 390 DHAYdFENdlTLFDWMSQ-------WRQEGDDEQAVRGTLGRL-LFSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170
....*....|.
gi 447014717 218 ILMDEPCSALD 228
Cdd:PRK15064 460 LVMDEPTNHMD 470
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
197-295 |
6.54e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 197 LSGGQQQRLCIARTIA--VSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQ---AARVSD---RTAY 267
Cdd:PRK00635 477 LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIIDigpGAGI 556
|
90 100
....*....|....*....|....*...
gi 447014717 268 FhlGDLIEVNSTEKVFTQPDHQLTEAYI 295
Cdd:PRK00635 557 F--GGEVLFNGSPREFLAKSDSLTAKYL 582
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
68-263 |
8.08e-05 |
|
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: 43.02 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 68 IKGIDLDIYQNEVIAFIGPSGCGKST--------------------FLRT-LNRMN----DTIDGCRVTgkITLDNKNI- 121
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveslsaYARQfLGQMDkpdvDSIEGLSPA--IAIDQKTTs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 122 YDPnldvvllRAQVGMVfqkpnpfpksifdnvaygPKLHGLARDKYDLEEIVE--NSLRKAGLweevkD--RLNQPGTGL 197
Cdd:cd03270 89 RNP-------RSTVGTV------------------TEIYDYLRLLFARVGIRErlGFLVDVGL-----GylTLSRSAPTL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 198 SGGQQQRLCIARTIAVSPEVIL--MDEPCSALDPIATAKVEELISELSDQ-YTIVIVTH---SMQQAARVSD 263
Cdd:cd03270 139 SGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHdedTIRAADHVID 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
79-251 |
1.03e-04 |
|
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: 42.74 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 79 EVIAFIGPSGCGKSTFLRTLnrmndtidgcrvTGKITlDNKNIYD--PNLDVVL--------------LRAQVGMVFQKP 142
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKIL------------AGKLK-PNLGKFDdpPDWDEILdefrgselqnyftkLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 143 ---NPFPKSIFDNVAygpKLHGLARDKYDLEEIVENSlrkaglweEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVIL 219
Cdd:cd03236 94 qyvDLIPKAVKGKVG---ELLKKKDERGKLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190
....*....|....*....|....*....|..
gi 447014717 220 MDEPCSALDPIATAKVEELISELSDQYTIVIV 251
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEDDNYVLV 194
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
45-271 |
1.23e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 45 KPNSTEIKISAQDAHVYYGDFEAIKG-IDLDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDTidgcrVTGKITLDNKNIYD 123
Cdd:PRK13543 3 EPLHTAPPLLAAHALAFSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHV-----ESGQIQIDGKTATR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 124 PNldvvllRAQVgMVFQKPNPFPK---SIFDNVAYGPKLHGlardkYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGG 200
Cdd:PRK13543 78 GD------RSRF-MAYLGHLPGLKadlSTLENLHFLCGLHG-----RRAKQMPGSALAIVGLAGYEDTLVRQ----LSAG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014717 201 QQQRLCIARtIAVSPEVI-LMDEPCSALDPIATAKVEELIS-ELSDQYTIVIVTHSMQQAARVsdRTAYFHLG 271
Cdd:PRK13543 142 QKKRLALAR-LWLSPAPLwLLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTHGAYAAPPV--RTRMLTLE 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
180-241 |
1.49e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447014717 180 AGLWEEVKDRlnqpGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpiatAKVEELISE 241
Cdd:PTZ00243 770 GGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD----AHVGERVVE 823
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
156-254 |
2.07e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 156 GPKLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIA---RTIAVSPEVILMDEPCSALDPIAT 232
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLL 275
|
90 100
....*....|....*....|...
gi 447014717 233 AKVEELISELSDQYT-IVIVTHS 254
Cdd:pfam13304 276 RRLLELLKELSRNGAqLILTTHS 298
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
196-253 |
2.48e-04 |
|
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: 40.81 E-value: 2.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014717 196 GLSGGQQQRLCIA-----RTIAVSPEVILmDEPCSALDPIATAKVEELISELSDQYTIVIV-TH 253
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIViTH 139
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-258 |
3.96e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 10 LEKDKLVnteqSQLTDTQLHHGTSYVSHFEPHASKKPNSTEIKISAQDAHVYYGDFEAIKGIDLDIYQNEVIAFIGPSGC 89
Cdd:PRK10938 222 ILQQALV----AQLAHSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 90 GKSTFLRTlnrmndtidgcrvtgkITLDNKNIYdpNLDVVLLRAQVGMvfqkpnpfPKSIFD---NVAY-GPKLHglard 165
Cdd:PRK10938 298 GKSTLLSL----------------ITGDHPQGY--SNDLTLFGRRRGS--------GETIWDikkHIGYvSSSLH----- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 166 kydLEEIVENSLRKA---------GLWEEVKDRLNQ------------------PGTGLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PRK10938 347 ---LDYRVSTSVRNVilsgffdsiGIYQAVSDRQQKlaqqwldilgidkrtadaPFHSLSWGQQRLALIVRALVKHPTLL 423
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447014717 219 LMDEPCSALDPIATAKV----EELISELSDQytIVIVTHSMQQA 258
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVrrfvDVLISEGETQ--LLFVSHHAEDA 465
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
70-269 |
4.36e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 70 GIDLDiyqnEVIAFIGPSGCGKSTFLRTlnrmndtidgcrVTGKItldnkniyDPNLDVVLLRAQVGMVFqkpnpFPKSI 149
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKL------------ISGEL--------QPSSGTVFRSAKVRMAV-----FSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 150 FD--NVAYGPKLHGLARDKYDLEEIVENSLRKAGLweeVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSAL 227
Cdd:PLN03073 582 VDglDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGV---TGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447014717 228 DPIAtakVEELISELS-DQYTIVIVTH-------SMQQAARVSD-RTAYFH 269
Cdd:PLN03073 659 DLDA---VEALIQGLVlFQGGVLMVSHdehlisgSVDELWVVSEgKVTPFH 706
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
197-269 |
5.49e-04 |
|
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: 39.86 E-value: 5.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447014717 197 LSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSD--QYTIVIVTHSMQQAARVSDRTAYFH 269
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
71-272 |
1.09e-03 |
|
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: 40.55 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 71 IDLDIYQNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvT-------GKITLDNKNIYDPNLDvvLLRAQVGMVFqkpn 143
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLL------------TglyrpesGEILLDGQPVTADNRE--AYRQLFSAVF---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 144 pfpkS---IFDNVaYGPklhglarDKYDLEEIVENSLRKAGLWEEVK---DRLNQpgTGLSGGQQQRLciARTIAV---S 214
Cdd:COG4615 413 ----SdfhLFDRL-LGL-------DGEADPARARELLERLELDHKVSvedGRFST--TDLSQGQRKRL--ALLVALledR 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 215 PeVILMDEPCSALDPIATAKV-EELISELSDQ-YTIVIVTHsmqqaarvSDRtaYFHLGD 272
Cdd:COG4615 477 P-ILVFDEWAADQDPEFRRVFyTELLPELKARgKTVIAISH--------DDR--YFDLAD 525
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
65-263 |
1.13e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 65 FEAIKGID---LDIYQNEVIAFIGPSGCGKSTFLRTLNRMNDtidgcRVTGKITLDNKNIyDPNLDVVLLRAQVGMVFQK 141
Cdd:PRK10982 8 FPGVKALDnvnLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEI-DFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 142 PNPF-PKSIFDNVAYG--PKlHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQpgtgLSGGQQQRLCIARTIAVSPEVI 218
Cdd:PRK10982 82 LNLVlQRSVMDNMWLGryPT-KGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447014717 219 LMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSMQQAARVSD 263
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCD 202
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
189-255 |
1.37e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 189 RLNQPGTGLSGGQQQRLCIARTI---AVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSM 255
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNL 892
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
77-253 |
2.09e-03 |
|
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: 38.12 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 77 QNEVIAFIGPSGCGKSTFLRTLnrmndtidgcrvtgkitldnkniydpnldvvllraqvgmvfqkpnpfpksifdnvayg 156
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL---------------------------------------------------------- 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 157 pkLHGLARDKYDLEEIVENSLRKAGLWEEVKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVE 236
Cdd:smart00382 23 --ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....
gi 447014717 237 ELISELSDQY-------TIVIVTH 253
Cdd:smart00382 101 LLEELRLLLLlkseknlTVILTTN 124
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
177-265 |
4.62e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 177 LRKAGLWEEVKDRLNQPGTGlsggQQQRLCIARtiAVSPEV---ILmDEPCSALDPIATAKVEELISELSDQ-YTIVIVT 252
Cdd:NF040905 124 LAKVGLDESPDTLVTDIGVG----KQQLVEIAK--ALSKDVkllIL-DEPTAALNEEDSAALLDLLLELKAQgITSIIIS 196
|
90
....*....|...
gi 447014717 253 HSMQQAARVSDRT 265
Cdd:NF040905 197 HKLNEIRRVADSI 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
184-254 |
4.88e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 184 EEVKDRLN-------QPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDpiATAKVE--ELISELSDQYTIVIVTHS 254
Cdd:NF040905 385 EEYRKKMNiktpsvfQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGAKYEiyTIINELAAEGKGVIVISS 462
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
171-251 |
8.33e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 171 EIVENSLRKAGLWEE------VKDRLNQPGTGLSGGQQQRLCIARTIAVSPEVILMDEPCSALDPIATAKVEELISELSD 244
Cdd:PRK10938 104 EIIQDEVKDPARCEQlaqqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ 183
|
....*...
gi 447014717 245 Q-YTIVIV 251
Cdd:PRK10938 184 SgITLVLV 191
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
189-255 |
8.33e-03 |
|
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: 37.21 E-value: 8.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447014717 189 RLNQPGTGLSGGQQQRLCIARTI---AVSPEVILMDEPCSALDPIATAKVEELISELSDQ-YTIVIVTHSM 255
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNL 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
190-299 |
8.45e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 190 LNQPGTGLSGGQQQRLCIARTI--AVSPEVILMDEPCSALDPIATAKVEELISELSDQYTIVIVTHSMQQAARVSDRT-- 265
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVid 561
|
90 100 110
....*....|....*....|....*....|....*...
gi 447014717 266 ----AYFHLGDLIEVNSTEKVFTQPDhQLTEAYITGRF 299
Cdd:TIGR00630 562 igpgAGEHGGEVVASGTPEEILANPD-SLTGQYLSGRK 598
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
79-165 |
8.79e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.96 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014717 79 EVIAFIGPSGCGKSTFLRTLNRMNDTI--DGCRvtgKITLDNKNIYDPNLDVV-LLRAQVGMVFQKPNPFpksIFDNVAY 155
Cdd:COG4639 3 SLVVLIGLPGSGKSTFARRLFAPTEVVssDDIR---ALLGGDENDQSAWGDVFqLAHEIARARLRAGRLT---VVDATNL 76
|
90
....*....|....
gi 447014717 156 GP----KLHGLARD 165
Cdd:COG4639 77 QRearrRLLALARA 90
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
81-122 |
9.04e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.29 E-value: 9.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 447014717 81 IAFIGPSGCGKSTFLRTL--------NRMNDTIDgcRVTGKITLDNKNIY 122
Cdd:pfam01926 2 VALVGRPNVGKSTLINALtgakaivsDYPGTTRD--PNEGRLELKGKQII 49
|
|
|