|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-251 |
1.22e-175 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 483.05 E-value: 1.22e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGRFPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 161 EPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIV 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|.
gi 1899776741 241 DGPDGPLACYF 251
Cdd:COG4604 241 EIDGKRICVYF 251
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
2.07e-100 |
|
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: 292.72 E-value: 2.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGRFPYSH--GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQ 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
....*..
gi 1899776741 239 IVDGPDG 245
Cdd:COG1120 241 VIEDPVT 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-243 |
1.85e-74 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 226.82 E-value: 1.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGRFPY-SH-GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWlSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQ 238
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
....*
gi 1899776741 239 IVDGP 243
Cdd:PRK11231 241 IHPEP 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
6.19e-66 |
|
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: 202.28 E-value: 6.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 3 TLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 83 enhfitkltvrqlvgfgrfpyshgrltkkdeeiistYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEP 162
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 163 LNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-245 |
1.43e-65 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 204.64 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 3 TLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 83 ENHFITKLTVRQLVGFGRFPY--SHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLD 160
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 161 EPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIV 240
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGIL 252
|
....*
gi 1899776741 241 DGPDG 245
Cdd:PRK10575 253 PHPAG 257
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-245 |
3.70e-63 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 198.07 E-value: 3.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLtmvgRLL----DIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQLV 96
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLL----RALsgelSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFGRFPysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ------ETDYVLLDEPLNNLDIAH 170
Cdd:PRK13548 98 AMGRAP--HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAH 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 171 SVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIVDGPDG 245
Cdd:PRK13548 176 QHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADVLVQPHPET 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-246 |
1.13e-62 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 196.88 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVkkdyndEVRIG------PANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLA 74
Cdd:COG4559 1 MLEAENL------SVRLGgrtlldDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 KILSILRQENH--FitKLTVRQLVGFGRFPysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ 152
Cdd:COG4559 75 RRRAVLPQHSSlaF--PFTVEEVVALGRAP--HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 153 --ETD-----YVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:COG4559 151 lwEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
250 260
....*....|....*....|.
gi 1899776741 226 AETLSEIFNTPVQIVDGPDGP 246
Cdd:COG4559 230 DELLERVYGADLRVLAHPEGG 250
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
2.57e-61 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 193.00 E-value: 2.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVsstkSKDLAKI--- 76
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkAILG-LLPPTSGTVRLFGKPP----RRARRRIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 ---LSILRQenhfiTKLTVRQLVGFGRFPYS--HGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLC 151
Cdd:COG1121 81 pqrAEVDWD-----FPITVRDVVLMGRYGRRglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 152 QETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICaFGPAEEIMHAETLSE 231
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPENLSR 233
|
250
....*....|
gi 1899776741 232 IFNTPVQIVD 241
Cdd:COG1121 234 AYGGPVALLA 243
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-233 |
4.11e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.88 E-value: 4.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRI-GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKilsi 79
Cdd:COG3638 2 MLELRNLSKRYPGGTPAlDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LR-------QENHFITKLTVRQLVGFGRFPYSH------GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYV 146
Cdd:COG3638 78 LRrrigmifQQFNLVPRLSVLTNVLAGRLGRTStwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQIcAF-GPAEEImH 225
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV-VFdGPPAEL-T 235
|
....*...
gi 1899776741 226 AETLSEIF 233
Cdd:COG3638 236 DAVLREIY 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-243 |
7.46e-57 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 182.49 E-value: 7.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQLVGFGR 100
Cdd:PRK10253 27 TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FPYS--HGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHL 178
Cdd:PRK10253 107 YPHQplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 179 QRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIVDGP 243
Cdd:PRK10253 187 SELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDP 251
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-233 |
3.22e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.48 E-value: 3.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVsSTKSKDLAKILSILR 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGF-GRFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLD 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 161 EPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMhAETLSEIF 233
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-233 |
4.23e-54 |
|
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: 174.29 E-value: 4.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDY-NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILS-- 78
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 79 -ILRQENHFITKLTVRQLVGFGRFPYSH------GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLC 151
Cdd:cd03256 81 gMIFQQFNLIERLSVLENVLSGRLGRRStwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 152 QETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEImHAETLSE 231
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDE 239
|
..
gi 1899776741 232 IF 233
Cdd:cd03256 240 IY 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-218 |
1.62e-53 |
|
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: 171.95 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 4 LNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKD--LAKILSIL 80
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLkAILG-LLKPTSGSIRVFGKPLEKERKRIgyVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENhfitkLTVRQLVGFGRFPYS--HGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:cd03235 81 RDFP-----ISVRDVVLMGLYGHKglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNIcAVKDGQICAFG 218
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-232 |
2.09e-52 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 170.04 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIlSIL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVG-FGRFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:COG4555 80 PDERGLYDRLTVRENIRyFAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEI 232
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-233 |
3.68e-52 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 169.40 E-value: 3.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDY-NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI--- 76
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFITKLTVRQLVGFGRFPYSH------GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVL 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEImHAETLS 230
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVLR 239
|
...
gi 1899776741 231 EIF 233
Cdd:TIGR02315 240 HIY 242
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-224 |
4.45e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 166.47 E-value: 4.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDE-VRigpANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSI 79
Cdd:COG3840 1 MLRLDDLTYRYGDFpLR---FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKLTVRQLVGFGRFPysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-231 |
1.70e-49 |
|
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: 162.12 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRI-GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:COG1122 1 IELENLSFSYPGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQ--ENHFITKlTVRQLVGFGrfPYSHGrLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFG--PENLG-LPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM-HAETLSE 231
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFsDYELLEE 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-233 |
2.26e-48 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 164.24 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGRFPYSH--GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 159 LDEPLNNLDIAHSVQMMQhLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIF 233
Cdd:PRK09536 163 LDEPTASLDINHQVRTLE-LVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
7.28e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.90 E-value: 7.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKi 76
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTAlrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lsiLRQEN--------HFITKLTVRQLVgfgRFPYS-HGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVA 147
Cdd:COG1136 83 ---LRRRHigfvfqffNLLPELTALENV---ALPLLlAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 148 MVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASkYADNICAVKDGQI 214
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
5.72e-47 |
|
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: 155.34 E-value: 5.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI- 76
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAlkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 ---LSILRQENHFITKLTVRQLVgfgRFP-YSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ 152
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENV---ELPlLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 153 ETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASkYADNICAVKDGQI 214
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-213 |
8.85e-46 |
|
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: 152.24 E-value: 8.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 4 LNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSI 79
Cdd:cd03225 2 LKNLSFSYPDGAR--PAlddiSLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQE-NHFITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:cd03225 80 VFQNpDDQFFGPTVEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
5.65e-45 |
|
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: 157.76 E-value: 5.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA-----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAK 75
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRavddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 ilsiLRQE--------NH-FITKLTVRQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGL-RELENRFLDQLSGGQRQRA 144
Cdd:COG1123 340 ----LRRRvqmvfqdpYSsLNPRMTVGDIIAEP--LRLHGLLSRAErRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 145 YVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
..
gi 1899776741 225 HA 226
Cdd:COG1123 494 AN 495
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
4.54e-44 |
|
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: 147.67 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-200 |
4.90e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 144.30 E-value: 4.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstkskdlAKILSILRQENHFITKL--TVRQLVGF 98
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSLplTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 GRFPY--SHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHSVQMMQ 176
Cdd:NF040873 81 GRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD-AESRERII 159
|
170 180
....*....|....*....|....
gi 1899776741 177 HLQRAAAEFGRTIIVVLHDINFAS 200
Cdd:NF040873 160 ALLAEEHARGATVVVVTHDLELVR 183
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-225 |
1.74e-42 |
|
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: 144.18 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKDLAKI---L 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLrLIVG-LLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVGFgrFPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAF--PLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 157 VLLDEPLNNLD-IAHSV--QMMQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:cd03261 158 LLYDEPTAGLDpIASGVidDLIRSLKK---ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
16-241 |
1.67e-40 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 139.59 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 16 RIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDiDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQL 95
Cdd:COG4138 11 RLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGrfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ-------ETDYVLLDEPLNNLDI 168
Cdd:COG4138 90 LALH---QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 169 AHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIVD 241
Cdd:COG4138 167 AQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE 238
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
2.56e-40 |
|
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: 138.96 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI---L 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVGFG-RFpysHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPlRE---HTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 156 YVLLDEPLNNLDIAHS---VQMMQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAE 227
Cdd:COG1127 162 ILLYDEPTAGLDPITSaviDELIRELRD---ELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
2.92e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 131.54 E-value: 2.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSST--KSKDLAKILSI 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKLTVRQLVGFGrfpyshgrltkkdeeiistyidffglrelenrfldqLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
3.54e-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: 131.37 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVsSTKSKDLAKILSILR 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVgfgrfpyshgrltkkdeeiistyidffglrelenrfldQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:cd03230 80 EEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
4.19e-38 |
|
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: 130.44 E-value: 4.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 3 TLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLakilsilrq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 83 enhfitkltvRQLVGFgrfpyshgrltkkdeeiistyidffglrelenrfLDQLSGGQRQRAYVAMVLCQETDYVLLDEP 162
Cdd:cd00267 72 ----------RRRIGY----------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 163 LNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-214 |
4.28e-38 |
|
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: 132.63 E-value: 4.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKskdlAKI 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS----RRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFI---------TKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGL---RELENRFLDQLSGGQRQRA 144
Cdd:cd03257 77 RKIRRKEIQMVfqdpmsslnPRMTIGEQIAEP--LRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 145 YVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNIcAV-KDGQI 214
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRV-AVmYAGKI 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-218 |
1.19e-37 |
|
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: 131.08 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILRQENHFITKLTVRQLVGFGRF 101
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 PYSHgrLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRA 181
Cdd:cd03298 97 PGLK--LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1899776741 182 AAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-224 |
1.64e-37 |
|
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: 131.65 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYND-EVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFgrFPYSHGRLTKKDEEIISTYIDFFGL--RELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL--VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-196 |
1.94e-37 |
|
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: 130.67 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTkSKDLAKIL 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-GPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 silrQENHFITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:cd03293 80 ----QQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDI 196
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
16-241 |
4.12e-37 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 130.82 E-value: 4.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 16 RIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDiDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQL 95
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGRfpySHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ-------ETDYVLLDEPLNNLDI 168
Cdd:PRK03695 90 LTLHQ---PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 169 AHSVQMMQhLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIVD 241
Cdd:PRK03695 167 AQQAALDR-LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
5.05e-37 |
|
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: 129.52 E-value: 5.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSkDLAKILSI 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLrILAG-LLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKLTVRQLVGFgrfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1899776741 160 DEPLNNLDiAHSVQMMQHLQRAAAEFGRTIIVVLHD 195
Cdd:COG4133 156 DEPFTALD-AAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-245 |
1.76e-36 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 129.95 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGRLLDIDE-------GTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTV 92
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAFSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 93 RQLVGFGRFPYSH--GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ---------ETDYVLLDE 161
Cdd:PRK13547 101 REIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTPVQIVD 241
Cdd:PRK13547 181 PTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGFAVRLVD 260
|
....
gi 1899776741 242 GPDG 245
Cdd:PRK13547 261 AGDG 264
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
2.12e-36 |
|
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: 129.15 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI 76
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVlkdvSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQE-----NhfiTKLTVRQLVgfgRFPYSHGRLTKKDEEIIStYIDFFGL-RELENRFLDQLSGGQRQRAYVAMVL 150
Cdd:COG1124 81 VQMVFQDpyaslH---PRHTVDRIL---AEPLRIHGLPDREERIAE-LLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
3.00e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 3.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlakilsil 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQ-----EN-----HfitkLTVRQLVGFGRfpyshgRLTKKDEEIISTYI----DFFGLRELENRFLDQLSGGQRQRayV 146
Cdd:COG3839 75 RNiamvfQSyalypH----MTVYENIAFPL------KLRKVPKAEIDRRVreaaELLGLEDLLDRKPKQLSGGQRQR--V 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 147 AM--VLCQETDYVLLDEPLNNLDiAHS-VQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:COG3839 143 ALgrALVREPKVFLLDEPLSNLD-AKLrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
4.91e-36 |
|
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: 127.10 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSStKSKDLAKILSILR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQ-LVGFGR-FPYSHGRLTKKDEEIIstyiDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHARlYGVPGAERRERIDELL----DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
6.68e-36 |
|
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: 133.73 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRI-GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:COG4988 337 IELEDVSFSYPGGRPAlDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFItKLTVRQLVGFGRFPYShgrltkkDEEII----STYIDFFgLRELENRfLD--------QLSGGQRQRAYVAM 148
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLGRPDAS-------DEELEaaleAAGLDEF-VAALPDG-LDtplgeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 149 VLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFAsKYADNICAVKDGQICAFGPAEEIMHAE 227
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-225 |
7.84e-36 |
|
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: 127.85 E-value: 7.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKiLSILR--QENHFITKLTVRQ---- 94
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR-LGIARtfQNPRLFPELTVLEnvlv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 95 -------------LVGFGRFPYSHGRLTKKDEEIistyIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:COG0411 103 aaharlgrgllaaLLRLPRARREEREARERAEEL----LERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
2.29e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkdlakilsiLR 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP---------PR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QEN------------HfitkLTVRQLVGFGrfpYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRayVAM 148
Cdd:COG1118 74 ERRvgfvfqhyalfpH----MTVAENIAFG---LRVRPPSKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQR--VAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 149 --VLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:COG1118 145 arALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.45e-35 |
|
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: 131.56 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVR--IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID---EGTIEVAGYDVSSTKSKDLAK 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDVpaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 ILSILRQE-NHFITKLTVRQLVgfgRFPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQE 153
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQI---AEALENLGLSRAEaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 154 TDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
9.29e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 124.34 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYND-EV--RIgpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKsKDLAKIl 77
Cdd:COG1126 1 MIEIENLHKSFGDlEVlkGI---SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK-KDINKL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 silRQE-----------NHfitkLTVRQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRay 145
Cdd:COG1126 76 ---RRKvgmvfqqfnlfPH----LTVLENVTLA--PIKVKKMSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQR-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 146 VAMV--LCQETDYVLLDEPLNNLD---IAHSVQMMQHLqraAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPA 220
Cdd:COG1126 145 VAIAraLAMEPKVMLFDEPTSALDpelVGEVLDVMRDL---AKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
...
gi 1899776741 221 EEI 223
Cdd:COG1126 221 EEF 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
1.38e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.43 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTkSKDLAKI 76
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTAlddvSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-GPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LsilrQENHFITKLTVRQLVGFG-RFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:COG1116 86 F----QEPALLPWLTVLDNVALGlEL---RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDI 196
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-225 |
4.31e-34 |
|
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: 122.55 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKiLSILR--QENHFITKLTVRQ--LV 96
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LGIGRtfQIPRLFPELTVLEnvMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 G----------FGRFPYSHGRLTKKDEEIistyIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNL 166
Cdd:cd03219 99 AaqartgsgllLARARREEREARERAEEL----LERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 167 DIAHSVQMMQHLqRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:cd03219 175 NPEETEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-223 |
5.27e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 124.05 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVrigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSStksKDLAKi 76
Cdd:COG1125 1 MIEFENVTKRYPDGT---VAvddlSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD---LDPVE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lsiLR-------QEN----HfitkLTVRQ---LVgfgrfPyshgRLTKKDEEIISTYID----FFGL--RELENRFLDQL 136
Cdd:COG1125 74 ---LRrrigyviQQIglfpH----MTVAEniaTV-----P----RLLGWDKERIRARVDelleLVGLdpEEYRDRYPHEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 137 SGGQRQRAYVAMVLCQETDYVLLDEPLNNLD--IAHSVQ-MMQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:COG1125 138 SGGQQQRVGVARALAADPPILLMDEPFGALDpiTREQLQdELLRLQR---ELGKTIVFVTHDIDEALKLGDRIAVMREGR 214
|
250
....*....|
gi 1899776741 214 ICAFGPAEEI 223
Cdd:COG1125 215 IVQYDTPEEI 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-225 |
5.84e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.21 E-value: 5.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlakilsil 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQEN----------HfitkLTVRQLVGFG-RFpyshgRLTKKDE--EIISTYIDFFGLRELENRFLDQLSGGQRQRayVA 147
Cdd:COG3842 77 RNVGmvfqdyalfpH----LTVAENVAFGlRM-----RGVPKAEirARVAELLELVGLEGLADRYPHQLSGGQQQR--VA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 148 M--VLCQETDYVLLDEPLNNLDiAHSVQMMQ----HLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAE 221
Cdd:COG3842 146 LarALAPEPRVLLLDEPLSALD-AKLREEMReelrRLQR---ELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
....
gi 1899776741 222 EIMH 225
Cdd:COG3842 222 EIYE 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-232 |
8.08e-34 |
|
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: 122.95 E-value: 8.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIlsilRQE--------NHFITKLTV 92
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL----RKKvglvfqfpEHQLFEETV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 93 RQLVGFGrfPYSHGrLTKKD-EEIISTYIDFFGLRElenRFLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD 167
Cdd:TIGR04521 101 YKDIAFG--PKNLG-LSEEEaEERVKEALELVGLDE---EYLERspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 168 IAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI-MHAETLSEI 232
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVfSDVDELEKI 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-236 |
1.02e-33 |
|
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: 124.45 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDV-SSTKSKDLA---KILSILRQENHFITKLTVRQL 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPpekRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGRfPYSHGRLTKKDEEIIstyIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:TIGR02142 96 LRYGM-KRARPSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 176 QHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIFNTP 236
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARED 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-214 |
1.24e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.93 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVrigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKi 76
Cdd:COG2884 1 MIRFENVSKRYPGGR---EAlsdvSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lsiLR-------QENHFITKLTVRQLVgfgRFPYshgRLTKKDEEIISTYI----DFFGLRELENRFLDQLSGGQRQRAY 145
Cdd:COG2884 77 ---LRrrigvvfQDFRLLPDRTVYENV---ALPL---RVTGKSRKEIRRRVrevlDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-214 |
1.48e-33 |
|
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: 120.48 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYD-VSSTKSKDLA----KIlSILRQENHFITKLTVRQLVGFGRF 101
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKKINLPpqqrKI-GLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 PYSHGRLTKKDEEIIstyiDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRA 181
Cdd:cd03297 102 RKRNREDRISVDELL----DLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|...
gi 1899776741 182 AAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
1.49e-33 |
|
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: 127.19 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVR--IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSI 79
Cdd:COG4987 334 LELEDVSFRYPGAGRpvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENH-FITklTVRQ--LVGfgrfpyshgRLTKKDEEIISTyIDFFGLRELENRF---LD--------QLSGGQRQRAY 145
Cdd:COG4987 414 VPQRPHlFDT--TLREnlRLA---------RPDATDEELWAA-LERVGLGDWLAALpdgLDtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMH 225
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLA 558
|
..
gi 1899776741 226 AE 227
Cdd:COG4987 559 QN 560
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-164 |
1.74e-33 |
|
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: 118.52 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 19 PANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQLVGF 98
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 GRfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLD----QLSGGQRQRAYVAMVLCQETDYVLLDEPLN 164
Cdd:pfam00005 83 GL--LLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
3.60e-33 |
|
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: 119.67 E-value: 3.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGRfpyshgRLTKKDEEIISTYI----DFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL------KLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
3.99e-33 |
|
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: 119.53 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKsKDLAKIL 77
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAvddlSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQ-LVGFGRFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:cd03263 78 GYCPQFDALFDELTVREhLRFYARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
8.16e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.38 E-value: 8.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILR 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKlTVRQLVgfgRFPYSHgRLTKKDEEIISTYIDFFGLRElenRFLDQ----LSGGQRQRAYVAMVLCQETDYV 157
Cdd:COG4619 81 QEPALWGG-TVRDNL---PFPFQL-RERKFDRERALELLERLGLPP---DILDKpverLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-214 |
1.49e-32 |
|
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: 118.04 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKkdYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgyDVSSTKSKDLAKILSILR 81
Cdd:TIGR01277 1 LALDKVR--YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVN--DQSHTGLAPYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGRFPYShgRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:TIGR01277 77 QENNLFAHLTVRQNIGLGLHPGL--KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
4.69e-32 |
|
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: 117.30 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDL--- 73
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 -AKILSILRQENHFITKlTVRQLVGFgrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLC 151
Cdd:cd03258 81 rRRIGMIFQHFNLLSSR-TVFENVAL---PLEIAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 152 QETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-225 |
9.37e-32 |
|
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: 118.26 E-value: 9.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 9 KDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKdLAKILSILRQENHFIT 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK-VRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 89 KLTVRQ-LVGFGRF-PYSHGRLTKKDEEIistyIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNL 166
Cdd:TIGR01188 80 DLTGREnLEMMGRLyGLPKDEAEERAEEL----LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 167 DiAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:TIGR01188 156 D-PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
1.13e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlakilSIL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-----RLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQEN-------HFITKLTVRQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ 152
Cdd:PRK09493 76 RQEAgmvfqqfYLFPHLTALENVMFG--PLRVRGASKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 153 ETDYVLLDEPLNNLD--IAHSV-QMMQHLqraaAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:PRK09493 154 KPKLMLFDEPTSALDpeLRHEVlKVMQDL----AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
1.18e-31 |
|
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: 116.18 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstksKDLAKILSILR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG--------KDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITK------LTVRQLVGFGRfpyshgRLTKKDEEII----STYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLC 151
Cdd:cd03300 73 PVNTVFQNyalfphLTVFENIAFGL------RLKKLPKAEIkervAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 152 QETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
1.20e-31 |
|
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: 116.28 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILR 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFG-RFPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGlRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
1.40e-31 |
|
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: 114.02 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVR--IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSI 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKpvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENhFITKLTVRqlvgfgrfpyshgrltkkdEEIistyidffglrelenrfldqLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:cd03228 81 VPQDP-FLFSGTIR-------------------ENI--------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINfASKYADNICAVKDGQ 213
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
3.47e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.06 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDY-NDEVRIgpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYD-VSSTKSKdlaKILS 78
Cdd:PRK10771 1 MLKLTDITWLYhHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSR---RPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 79 ILRQENHFITKLTVRQLVGFGRFPyshG-RLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGLNP---GlKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-225 |
3.93e-31 |
|
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: 114.45 E-value: 3.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKDLAKI-LSILRQENHFITKLTVRQLVGF 98
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLkTIMG-LLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 GRFPYSHGRLTKKDEEIISTyidFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPlnNLDIAHSV--QMMQ 176
Cdd:cd03224 99 GAYARRRAKRKARLERVYEL---FPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP--SEGLAPKIveEIFE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1899776741 177 HLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:cd03224 174 AIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-225 |
6.34e-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: 117.12 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYD-VSSTKSKDLA---KILSILRQE----NHfitkLT 91
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGIFLPphrRRIGYVFQEarlfPH----LS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 92 VRQLVGFGRFPYSHGRLTKKDEEIIstyiDFFGLRELENRFLDQLSGGQRQRayVAMV--LCQETDYVLLDEPLNNLDIA 169
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISFDEVV----ELLGIGHLLDRRPATLSGGERQR--VAIGraLLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 170 HSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
6.88e-31 |
|
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: 113.78 E-value: 6.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKdlakiLSILR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN-----INELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QE-----NHF--ITKLTVRQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQE 153
Cdd:cd03262 76 QKvgmvfQQFnlFPHLTVLENITLA--PIKVKGMSKAEaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 154 TDYVLLDEPLNNLD---IAHSVQMMQHLqraaAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03262 154 PKVMLFDEPTSALDpelVGEVLDVMKDL----AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
9.68e-31 |
|
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: 113.06 E-value: 9.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGgITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKdLAKILSILR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFgrFPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDY--IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEfgRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
4.47e-30 |
|
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: 111.60 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstKSKDLAKILSI-- 79
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG------KPLDIAARNRIgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKLTVR-QLVGFGRFpysHGrLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:cd03269 75 LPEERGLYPKMKVIdQLVYLAQL---KG-LKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 158 LLDEPLNNLDIAhSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03269 151 ILDEPFSGLDPV-NVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
5.12e-30 |
|
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: 111.89 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDI-----DEGTIEVAGYDVSSTKSKDLA-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 -KILSILRQENHFitKLTVRQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLD--QLSGGQRQRAYVAMVL 150
Cdd:cd03260 81 rRVGMVFQKPNPF--PGSIYDNVAYG--LRLHGIKLKEElDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFgrTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-224 |
2.22e-29 |
|
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: 111.20 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI----LSILRQENHFITKLTVRQL 95
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGRfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:cd03294 123 VAFGL--EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1899776741 176 QHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:cd03294 201 DELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-214 |
3.57e-29 |
|
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: 108.88 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVagyDVSSTKSKDLAKILSILRQE-NHFITKLTVRQLVGFG 99
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL---NGKPIKAKERRKSIGYVMQDvDYQLFTDSVREELLLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RfpyshgRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQ 179
Cdd:cd03226 97 L------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1899776741 180 RAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03226 171 ELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
3.23e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 106.68 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI 76
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAvdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lSILRQENHFITKLTVRQLVG-FGRFpysHG----RLTKKDEEIISTyidfFGLRELENRFLDQLSGGQRQRAYVAMVLC 151
Cdd:cd03266 81 -GFVSDSTGLYDRLTARENLEyFAGL---YGlkgdELTARLEELADR----LGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 152 QETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
5.03e-28 |
|
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: 111.85 E-value: 5.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:COG2274 474 IELENVSFRYPGDSP--PVldniSLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKlTVRQLVGFGRFPYShgrltkkDEEIISTyIDFFGLRELENRF---LD--------QLSGGQRQRAYV 146
Cdd:COG2274 552 GVVLQDVFLFSG-TIRENITLGDPDAT-------DEEIIEA-ARLAGLHDFIEALpmgYDtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFAsKYADNICAVKDGQICAFGPAEEIM 224
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-240 |
6.28e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 106.71 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVG-----------RLLDIDEGTIEVA------GY 63
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygndvRLFGERRGGEDVWelrkriGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 64 dVSStkskDLAkilsilrqeNHFITKLTVRQLV--GF----GRFPyshgRLTKKDEEIISTYIDFFGLRELENRFLDQLS 137
Cdd:COG1119 83 -VSP----ALQ---------LRFPRDETVLDVVlsGFfdsiGLYR----EPTDEQRERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 138 GGQRQRAYV--AMV-----LcqetdyvLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVK 210
Cdd:COG1119 145 QGEQRRVLIarALVkdpelL-------ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK 217
|
250 260 270
....*....|....*....|....*....|
gi 1899776741 211 DGQICAFGPAEEIMHAETLSEIFNTPVQIV 240
Cdd:COG1119 218 DGRVVAAGPKEEVLTSENLSEAFGLPVEVE 247
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
7.46e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVrigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:COG1132 340 IEFENVSFSYPGDR---PVlkdiSLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENhFITKLTVRQLVGFGRFPYShgrltkkDEEIIS----TYIDFFgLRELENRfLD--------QLSGGQRQRAY 145
Cdd:COG1132 417 GVVPQDT-FLFSGTIRENIRYGRPDAT-------DEEVEEaakaAQAHEF-IEALPDG-YDtvvgergvNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFAsKYADNICAVKDGQICAFGPAEEIM 224
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
8.76e-28 |
|
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: 105.57 E-value: 8.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDY-NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI---L 77
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVGFG-RFPYSHGRLTKKDeeiISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlEVTGVPPREIRKR---VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
4.95e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYN-----DEVrigpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSstkSKDLAK 75
Cdd:COG4152 1 MLELKGLTKRFGdktavDDV-----SFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 I--------LSilrqenhfiTKLTVR-QLVGFGRFpysHGrLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRA- 144
Cdd:COG4152 73 IgylpeergLY---------PKMKVGeQLVYLARL---KG-LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 145 YVAMVLCqETDYVLLDEPLNNLD-IAhsVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:COG4152 140 LIAALLH-DPELLILDEPFSGLDpVN--VELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-224 |
5.44e-27 |
|
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: 104.16 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENH-FITklTVRQLVGFG 99
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVlFDG--TIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RFPyshgrltKKDEEIIS----TYIDFFgLRELENRFlD--------QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD 167
Cdd:cd03249 101 KPD-------ATDEEVEEaakkANIHDF-IMSLPDGY-DtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 168 iAHSVQMMQH-LQRAAAefGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:cd03249 172 -AESEKLVQEaLDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-214 |
2.32e-26 |
|
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: 101.52 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkDLAKILSILr 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-ALRRIGALI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVgfgrfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:cd03268 79 EAPGFYPNLTARENL------RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 162 PLNNLDiAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03268 153 PTNGLD-PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
3.13e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.22 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDE-VRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQeNHFITKLTVRQLVGFGRfPYShgrltkKDEEIIS----TYIDFF--GLRELENRFLDQ----LSGGQRQRAYVAMVL 150
Cdd:TIGR02857 402 PQ-HPFLFAGTIAENIRLAR-PDA------SDAEIREalerAGLDEFvaALPQGLDTPIGEggagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSVQMMQHLqRAAAEfGRTIIVVLHDINFASKyADNICAV 209
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEAL-RALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-234 |
7.95e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 101.88 E-value: 7.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDY-NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSiL 80
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGRfpYSH----GRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMGR--YGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKdGQICAFGPAEEIMHAETLSEIFN 234
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAFS 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-227 |
1.25e-25 |
|
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: 100.38 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:cd03251 1 VEFKNVTFRYPGDGP--PVlrdiSLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKlTVRQLVGFGRFPYSH------GRLTKKDEEIIST---YIDFFGLRELenrfldQLSGGQRQRAYVAM 148
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAYGRPGATReeveeaARAANAHEFIMELpegYDTVIGERGV------KLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 149 VLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIMHAE 227
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-227 |
1.29e-25 |
|
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: 100.29 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKDLAKI-LSILRQENHFITKLTVRQ--LV 96
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTTLLkTLMG-LLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRLTVEEnlLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFGRFPyshGRLTKKDEEIistYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNldIAHSV--QM 174
Cdd:TIGR03410 99 GLAALP---RRSRKIPDEI---YELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG--IQPSIikDI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 175 MQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAE 227
Cdd:TIGR03410 171 GRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-214 |
1.41e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGRlLDIDEGTIEVA-----GY--------DVS 66
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLkLLAGE-LEPDSGTVKLGetvkiGYfdqhqeelDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 67 STkskdlakILSILRQENHFITKLTVRQLVgfGRFPYSHGRLTKKdeeiISTyidffglrelenrfldqLSGGQRQRAYV 146
Cdd:COG0488 394 KT-------VLDELRDGAPGGTEQEVRGYL--GRFLFSGDDAFKP----VGV-----------------LSGGEKARLAL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLDIahsvQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
2.01e-25 |
|
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: 97.52 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYdvsstkskdlakilsilr 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 qenhfitkltvrqlvgfGRFPYshgrltkkdeeiistyidffglrelenrfLDQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:cd03221 63 -----------------VKIGY-----------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 162 PLNNLDIAHSVQMMQHLQraaaEFGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:cd03221 97 PTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
3.12e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.20 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQE-NHFITKLTVRQLVGFGr 100
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVFSSTVWDDVAFG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 fPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQR 180
Cdd:PRK13647 105 -PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDR 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1899776741 181 AAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:PRK13647 184 LHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
3.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.48 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKS----KDLAKILSILRQ-ENHFITKLTVRQL 95
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQfPEHQLFEETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGrfPYSHGRLTKKDEEIISTYIDFFGLRE-LENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQM 174
Cdd:PRK13634 107 ICFG--PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 175 MQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM-HAETLSEI 232
Cdd:PRK13634 185 MEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFaDPDELEAI 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-225 |
3.92e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.64 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILR 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGRfpyshgRLTKKDEEIISTYI----DFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGL------KLAGAKKEEINQRVnqvaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
5.14e-25 |
|
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: 98.47 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRI-GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI--- 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAAlHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFITKLTVRQLVGFGRfpyshgRLTKKDEEII----STYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ 152
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPL------EVRGKKEREIqrrvGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 153 ETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
6.20e-25 |
|
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: 98.52 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVkkdyndEVRIGPA------NLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKDL 73
Cdd:COG0410 3 MLEVENL------HAGYGGIhvlhgvSLEVEEGEIVALLGRNGAGKTTLLkAISG-LLPPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 AKI-LSILRQENHFITKLTVR---QLVGFGRFPYSHGRLTKkdEEIistYiDFF-GLRELENRFLDQLSGGQRQRAYVAM 148
Cdd:COG0410 76 ARLgIGYVPEGRRIFPSLTVEenlLLGAYARRDRAEVRADL--ERV---Y-ELFpRLKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 149 VLCQETDYVLLDEPLnnLDIAHSV--QMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:COG0410 150 ALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
....*..
gi 1899776741 227 ETLSEIF 233
Cdd:COG0410 227 PEVREAY 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
9.53e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkdlakilsiL 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS---------L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLtvRQLVGF-----GRFPY-----------------SHGRLTKKDEEIISTyidfFGLRELENRFLDQLSG 138
Cdd:PRK11264 74 SQQKGLIRQL--RQHVGFvfqnfNLFPHrtvleniiegpvivkgePKEEATARARELLAK----VGLAGKETSYPRRLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 139 GQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALD-PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
....*
gi 1899776741 219 PAEEI 223
Cdd:PRK11264 227 PAKAL 231
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-214 |
1.34e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 97.42 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI----LSILRQENHFITKLTVRQLV 96
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLrnkkLGFIYQFHHLLPDFTALENV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFgrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:TIGR02211 105 AM---PLLIGKKSVKEaKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIF 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1899776741 176 QHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQI 214
Cdd:TIGR02211 182 DLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-237 |
1.38e-24 |
|
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: 97.79 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYND-EVRIgpANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVssTKSKDLAKILSIL 80
Cdd:cd03299 1 LKVENLSKDWKEfKLKN--VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGrfpYSHGRLTKK--DEEIISTyIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG---LKKRKVDKKeiERKVLEI-AEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGpaeeimhaeTLSEIFNTPV 237
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG---------KPEEVFKKPK 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-218 |
1.46e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIlSILR 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI-GVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQ-LVGFGRFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLD 160
Cdd:PRK13536 121 QFDNLDLEFTVREnLLVFGRY---FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 161 EPLNNLDiAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:PRK13536 198 EPTTGLD-PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-224 |
1.51e-24 |
|
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: 97.61 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI-LSIL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQ--LVGFGRFPYSHGRLTKKDEEIIstyiDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:cd03218 81 PQEASIFRKLTVEEniLAVLEIRGLSKKEREEKLEELL----EEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 159 LDEPLNNLD-IAhsVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:cd03218 157 LDEPFAGVDpIA--VQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-195 |
2.06e-24 |
|
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: 101.28 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENH-FITklTVRQLVGFG 99
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHlFDT--TVRENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RfpyshGRLTkkDEEiISTYIDFFGLRELENRFLD-----------QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDI 168
Cdd:TIGR02868 433 R-----PDAT--DEE-LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*..
gi 1899776741 169 AHSVQMMQHLqrAAAEFGRTIIVVLHD 195
Cdd:TIGR02868 505 ETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-231 |
2.50e-24 |
|
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: 96.92 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRI-GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:cd03253 1 IEFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQEnhfiTKL---TVRQLVGFGRfpyshgrLTKKDEEIIST----------------YIDFFGLRELenrfldQLSGGQR 141
Cdd:cd03253 81 PQD----TVLfndTIGYNIRYGR-------PDATDEEVIEAakaaqihdkimrfpdgYDTIVGERGL------KLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 142 QRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFASKyADNICAVKDGQIcafgpAE 221
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRI-----VE 215
|
250
....*....|
gi 1899776741 222 EIMHAETLSE 231
Cdd:cd03253 216 RGTHEELLAK 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-228 |
4.93e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGrLLDI-DEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLETpDSGQLNIAGHQFDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 R------QENHFITKLTVRQ-LVgfgRFPYSHGRLTKKD-----EEIISTyidfFGLRELENRFLDQLSGGQRQRAYVAM 148
Cdd:COG4161 82 QkvgmvfQQYNLWPHLTVMEnLI---EAPCKVLGLSKEQarekaMKLLAR----LRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 149 VLCQETDYVLLDEPLNNLD---IAHSVQMMQHLqraaAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDpeiTAQVVEIIREL----SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
...
gi 1899776741 226 AET 228
Cdd:COG4161 231 PQT 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-223 |
4.97e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKS----KDLAKILSILRQ--ENHFITKlTVRQ 94
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQfpEAQLFEN-TVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 95 LVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRE-LENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQ 173
Cdd:PRK13641 106 DVEFG--PKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 174 MMQ---HLQRAaaefGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK13641 184 MMQlfkDYQKA----GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-214 |
7.84e-24 |
|
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: 95.86 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 7 VKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHF 86
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 87 ITKLTVRQLVGFGRFPY--SHGRLTKKDEEIistyIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLN 164
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYdlPPARFKKRLDEL----SELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1899776741 165 NLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-223 |
1.28e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 4 LNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDV--SSTKSKDLAkilsILR 81
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDIC----MVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGRfpyshgRLTKKDEEIISTYID----FFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGL------KMLGVPKEERKQRVKealeLVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-225 |
3.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSST-KSKDL----AKILSILRQENHFITKLTVRQL 95
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIkpvrKKVGVVFQFPESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGrfPYSHGRLTKKDEEIISTYIDFFGL-RELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQM 174
Cdd:PRK13643 106 VAFG--PQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 175 MQhLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:PRK13643 184 MQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-225 |
3.90e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILR 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGR--FPyshgRLTKKDEEIISTYI----DFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLtvLP----RRERPNAAAIKAKVtqllEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-247 |
6.65e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.99 E-value: 6.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvssTKSKDLAKILSILRQENHFI--TKLTVRQLVGFG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG-----ASPGKGWRHIGYVPQRHEFAwdFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RF----PYShgRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:TIGR03771 76 RTghigWLR--RPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 176 QHLQRAAAEfGRTIIVVLHDINFASKYADNICAVkDGQICAFGPAEEIMHAETLSEIFNTpvqivdGPDGPL 247
Cdd:TIGR03771 154 ELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGV------SDSSPL 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
7.98e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.14 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKi 76
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTAlddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lsiLRQE-----NHF--ITKLTVRQLVGfgrFPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAM 148
Cdd:COG1135 80 ---ARRKigmifQHFnlLSSRTVAENVA---LPLEIAGVPKAEiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 149 VLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNIcAV-KDGQICAFGPAEEI 223
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRV-AVlENGRIVEQGPVLDV 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.00e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYND-EVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLA--KIL 77
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQE-NHFITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:PRK13639 81 GIVFQNpDDQLFAPTVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-226 |
1.09e-22 |
|
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: 94.35 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLD---IDEGTIEVAGYDVSSTKSKDL 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAvdgvSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 AKI----LSILRQE-----NHFitkLTVRQLVGfgRFPYSHGRLTKKD-EEIISTYIDFFGLRELEnRFLD----QLSGG 139
Cdd:COG0444 81 RKIrgreIQMIFQDpmtslNPV---MTVGDQIA--EPLRIHGGLSKAEaRERAIELLERVGLPDPE-RRLDryphELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 140 QRQRAYVAMVLCQETDYVLLDEPLNNLDIahSVQ-----MMQHLQRaaaEFGRTIIVVLHDINFASKYADNIC---Avkd 211
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDV--TIQaqilnLLKDLQR---ELGLAILFITHDLGVVAEIADRVAvmyA--- 226
|
250
....*....|....*
gi 1899776741 212 GQICAFGPAEEIMHA 226
Cdd:COG0444 227 GRIVEEGPVEELFEN 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-195 |
1.28e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.52 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVR-IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVS--STKSKDLAKIL 77
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 silrqEN-----HfitkLTVRQLVGFGRfpysHGRLTKKDEeiISTYI-DFFGLRELEnRFLD----QLSGGQRQRayVA 147
Cdd:PRK11650 83 -----QNyalypH----MSVRENMAYGL----KIRGMPKAE--IEERVaEAARILELE-PLLDrkprELSGGQRQR--VA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 148 M--VLCQETDYVLLDEPLNNLDIAHSVQM---MQHLQRaaaEFGRTIIVVLHD 195
Cdd:PRK11650 145 MgrAIVREPAVFLFDEPLSNLDAKLRVQMrleIQRLHR---RLKTTSLYVTHD 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-224 |
2.47e-22 |
|
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: 91.52 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENhFITKLTVRQLVGFgr 100
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT-FLFSGTIMENIRL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 fpyshGRLTKKDEEII----STYIDFFgLRELENRFLDQ-------LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDia 169
Cdd:cd03254 100 -----GRPNATDEEVIeaakEAGAHDF-IMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNID-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 170 hsVQMMQHLQRAAAEF--GRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:cd03254 172 --TETEKLIQEALEKLmkGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-232 |
2.74e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.39 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:PRK13635 6 IRVEHISFRYPDAAT--YAlkdvSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQ--ENHFITKlTVRQLVGFGRfpYSHGrlTKKDE--EIISTYIDFFGLRElenrFLDQ----LSGGQRQRAYVAMV 149
Cdd:PRK13635 84 GMVFQnpDNQFVGA-TVQDDVAFGL--ENIG--VPREEmvERVDQALRQVGMED----FLNRephrLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 150 LCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIM-HAET 228
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFkSGHM 233
|
....
gi 1899776741 229 LSEI 232
Cdd:PRK13635 234 LQEI 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-194 |
8.99e-22 |
|
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: 90.02 E-value: 8.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 7 VKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGRLLD--IDEGTIEVAGYDVSSTKSKdlaKILSILRQE 83
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdAISGRVEGggTTSGQILFNGQPRKPDQFQ---KCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 84 NHFITKLTVRQLVGFgrfpYSHGRLT-KKDEEIISTYIDFFGLRELE-----NRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:cd03234 90 DILLPGLTVRETLTY----TAILRLPrKSSDAIRKKRVEDVLLRDLAltrigGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1899776741 158 LLDEPLNNLD--IAHS-VQMMQHLqraaAEFGRTIIVVLH 194
Cdd:cd03234 166 ILDEPTSGLDsfTALNlVSTLSQL----ARRNRIVILTIH 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-222 |
1.35e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKilsiLRQEN--------HFITKLTV 92
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ----LRREHfgfifqryHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 93 RQLVgfgRFP--YShGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAH 170
Cdd:PRK10535 104 AQNV---EVPavYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 171 SVQMMQHLQRAAAEfGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEE 222
Cdd:PRK10535 180 GEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-228 |
1.49e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTmVGRLLDI-DEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMpRSGTLNIAGNHFDFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 R------QENHFITKLTVRQ--------LVGFgrfpySHGRLTKKDEEIISTyidfFGLRELENRFLDQLSGGQRQRAYV 146
Cdd:PRK11124 82 RnvgmvfQQYNLWPHLTVQQnlieapcrVLGL-----SKDQALARAEKLLER----LRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLD---IAHSVQMMQHLQraaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELA----ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF 228
|
....*
gi 1899776741 224 MHAET 228
Cdd:PRK11124 229 TQPQT 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-223 |
1.53e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.93 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlakilsilR 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QEN----------HfitkLTVRQLVGFGRfpyshgRLTKKDEEIISTYIdFFGLR-----ELENRFLDQLSGGQRQRAYV 146
Cdd:PRK09452 87 HVNtvfqsyalfpH----MTVFENVAFGL------RMQKTPAAEITPRV-MEALRmvqleEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLDIAHSVQM---MQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQR---KLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-237 |
1.73e-21 |
|
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: 90.25 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI---LSILRQENH--FITKLTVRQL 95
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQDSPsaVNPRMTVRQI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFgrfPYSHgrLTKKDE----EIISTYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAH 170
Cdd:TIGR02769 111 IGE---PLRH--LTSLDEseqkARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 171 SVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQIcafgpAEEIMHAETLSeiFNTPV 237
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI-----VEECDVAQLLS--FKHPA 245
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-223 |
1.80e-21 |
|
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: 91.02 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlaKILSILRQENHFITKLTVRQLVGFGRfpyshgRLTKK 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGL------KMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 112 D-EEIISTYIDFFGLRELEN---RFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGR 187
Cdd:TIGR01187 73 PrAEIKPRVLEALRLVQLEEfadRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1899776741 188 TIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-197 |
1.94e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.69 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID---EGTIEVAGYDVssTKSKDLAKIL 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL--TALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVGFGrFPYSHGRLTKKDEeiISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPPTIGRAQRRAR--VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDIN 197
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.54e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 89.66 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVR--IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILS 78
Cdd:PRK13632 7 MIKVENVSFSYPNSENnaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 79 ILRQ--ENHFItKLTVRQLVGFG----RFPyshgrlTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ 152
Cdd:PRK13632 87 IIFQnpDNQFI-GATVEDDIAFGlenkKVP------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 153 ETDYVLLDE------PLNNLDIahsVQMMQHLQRAAAefgRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMHA 226
Cdd:PRK13632 160 NPEIIIFDEstsmldPKGKREI---KKIMVDLRKTRK---KTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN 232
|
....*.
gi 1899776741 227 ETLSEI 232
Cdd:PRK13632 233 KEILEK 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-229 |
2.91e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 31 ALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQE-NHFITKLTVRQLVGFGrfPYSHGRLT 109
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNpDDQIFSPTVEQDIAFG--PINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 110 KKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTI 189
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTV 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1899776741 190 IVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:PRK13652 192 IFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
3.28e-21 |
|
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: 91.92 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgydvsstkskDLAKILSILR 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----------ETVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVGFGrfpYSHGRLTKKdeEIIS-TYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:TIGR03719 393 SRDALDPNKTVWEEISGG---LDIIKLGKR--EIPSrAYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1899776741 160 DEPLNNLDiahsVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICA 208
Cdd:TIGR03719 468 DEPTNDLD----VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILA 512
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
3.64e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYN----DEVRI--GpANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTK----S 70
Cdd:COG1101 1 MLELKNLSKTFNpgtvNEKRAldG-LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeykrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 71 KDLAKI-----------LSILrqENHFITKLtvR-QLVGFGRfpyshgRLTKKDEEIISTYIDFFGLrELENRfLDQ--- 135
Cdd:COG1101 80 KYIGRVfqdpmmgtapsMTIE--ENLALAYR--RgKRRGLRR------GLTKKRRELFRELLATLGL-GLENR-LDTkvg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 136 -LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:COG1101 148 lLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-229 |
3.70e-21 |
|
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: 92.09 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQLVGFGR 100
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANNIAYGR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 fpyshgRLTKKDEEIISTYIDFFgLRELENRF---LDQ--------LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIA 169
Cdd:TIGR02203 431 ------TEQADRAEIERALAAAY-AQDFVDKLplgLDTpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 170 HSVQMMQHLQRAAAefGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:TIGR02203 504 SERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGL 560
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-223 |
6.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAG--YDVSSTKSKDLAKILSILRQE-NHFITKLTVRQLVG 97
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDpDNQLFSASVYQDVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 FGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQH 177
Cdd:PRK13636 106 FG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1899776741 178 LQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK13636 184 LVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
7.29e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID---EGTIEVAGYDVSSTKS------K 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREGRlardirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 72 DLAKILSILRQENhFITKLTVRQ--LVG-FGRFPYSHGRL---TKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAY 145
Cdd:PRK09984 84 SRANTGYIFQQFN-LVNRLSVLEnvLIGaLGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-224 |
8.22e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILR 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRqlvgFGRFP-YSHGRLTkkdEEIISTYIDFFGL-----RELENRFLDQ--------------LSGGQR 141
Cdd:PRK10619 86 QLRLLRTRLTMV----FQHFNlWSHMTVL---ENVMEAPIQVLGLskqeaRERAVKYLAKvgideraqgkypvhLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 142 QRAYVAMVLCQETDYVLLDEPLNNLD---IAHSVQMMQHLqraaAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQL----AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
....*.
gi 1899776741 219 PAEEIM 224
Cdd:PRK10619 235 APEQLF 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-214 |
9.70e-21 |
|
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: 86.21 E-value: 9.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDY--NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKsKDLAKILSI 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENH-FITklTVRQLVGfgrfpyshgrltkkdeeiistyidffglrelenrflDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:cd03247 80 LNQRPYlFDT--TLRNNLG------------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEfgRTIIVVLHDINfASKYADNICAVKDGQI 214
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLT-GIEHMDKILFLENGKI 174
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-224 |
1.01e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.02 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKilsiLRQENHFI---------TKLTV 92
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRMQMVfqdpyaslnPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 93 RQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIah 170
Cdd:COG4608 115 GDIIAEP--LRIHGLASKAErRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV-- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 171 SVQ-----MMQHLQRaaaEFGRTIIVVLHDINFASKYADNIcAVKD-GQICAFGPAEEIM 224
Cdd:COG4608 191 SIQaqvlnLLEDLQD---ELGLTYLFISHDLSVVRHISDRV-AVMYlGKIVEIAPRDELY 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
1.56e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.61 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTkSKDLAKI 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPAlqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-GADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LsilrQENHFITKLTVRQLVGFG-RFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:COG4525 82 F----QKDALLPWLNVLDNVAFGlRL---RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDI 196
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
1.58e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVR--IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLL---DIDEGTIEVAGYDVSSTKSKDLAKI 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpaLNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQ--ENHFITKlTVRQLVGFGRfpysHGRLTKKDE--EIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQ 152
Cdd:PRK13640 86 VGIVFQnpDNQFVGA-TVGDDVAFGL----ENRAVPRPEmiKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 153 ETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASkYADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-242 |
1.61e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.12 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkdLAKILSIL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFG----RFPysHGRLTKKDEEIIStyidFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGlkqdKLP--KAEIASRVNEMLG----LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM-HAET-LSEIFN 234
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYeHPTTrYSAEFI 250
|
....*...
gi 1899776741 235 TPVQIVDG 242
Cdd:PRK11607 251 GSVNVFEG 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
1.84e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 4 LNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIevagydvssTKSKDLaKIlSILRQE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV---------SIPKGL-RI-GYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 84 NHFITKLTVRQLV--GFGRFPYSHGRLTKKDEEIISTYIDFFGLRELENRF----------------------------- 132
Cdd:COG0488 70 PPLDDDLTVLDTVldGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFealggweaearaeeilsglgfpeedldrp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 133 LDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIaHSVQMM-QHLQRaaaeFGRTIIVVLHDINFASKYADNICAVKD 211
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLeEFLKN----YPGTVLVVSHDRYFLDRVATRILELDR 224
|
...
gi 1899776741 212 GQI 214
Cdd:COG0488 225 GKL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
2.97e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEV-----RIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYD------------ 64
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 65 ------VSSTKSKDLAKILSILRQ-------ENHFITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRElenR 131
Cdd:PRK13651 83 vleklvIQKTRFKKIKKIKEIRRRvgvvfqfAEYQLFEQTIEKDIIFG--PVSMGVSKEEAKKRAAKYIELVGLDE---S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 132 FLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNIC 207
Cdd:PRK13651 158 YLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*..
gi 1899776741 208 AVKDGQICAFGPAEEIM 224
Cdd:PRK13651 237 FFKDGKIIKDGDTYDIL 253
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-226 |
2.99e-20 |
|
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: 89.54 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:TIGR03375 464 IEFRNVSFAYPGQET--PAldnvSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKlTVRQLVGFGRfPYShgrltkKDEEIISTyIDFFGLRELENRF---LD--------QLSGGQRQRAYV 146
Cdd:TIGR03375 542 GYVPQDPRLFYG-TLRDNIALGA-PYA------DDEEILRA-AELAGVTEFVRRHpdgLDmqigergrSLSGGQRQAVAL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFAsKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
4.15e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDE--VRIGPANLEIPAGGITALVGPNGAGKSTLLT-MVGrLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:PRK13648 7 IIVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKlMIG-IEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQ--ENHFITKlTVRQLVGFGRfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:PRK13648 86 GIVFQnpDNQFVGS-IVKYDVAFGL--ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIM-HAETLSEI 232
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFdHAEELTRI 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
4.56e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.05 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID-----EGTIEVAGYDVSSTKSKDLA-- 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 -KILSILRQENHFiTKLTVRQLVGFGRfpYSHGRLTKKDE--EIISTYIDFFGL-RELENRFLD---QLSGGQRQRAYVA 147
Cdd:PRK14267 85 rEVGMVFQYPNPF-PHLTIYDNVAIGV--KLNGLVKSKKEldERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 148 MVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFgrTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-237 |
8.25e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKdlakilsilrqenhfiTKLTVRQL-VGF 98
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKG----------------ICLPPEKRrIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 ----GR-FP-YS-HGRLT----KKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD 167
Cdd:PRK11144 81 vfqdARlFPhYKvRGNLRygmaKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 168 IAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI-----MHA----ETLSEIFNTPV 237
Cdd:PRK11144 161 LPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVwassaMRPwlpkEEQSSILKVTV 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
8.66e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIlSILR 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQ-LVGFGRFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLD 160
Cdd:PRK13537 87 QFDNLDPDFTVREnLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 161 EPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAE 227
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
8.66e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLtmvgRLLdidegtievAGYDVSS-----TKSKDLAKI 76
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLL---------AGLETPSagellAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILR---QENHFITKLTVRQLVGFGrfpyshgrLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQE 153
Cdd:PRK11247 80 REDTRlmfQDARLLPWKKVIDNVGLG--------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 154 TDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
9.17e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID-----EGTIEVAGYDVSSTKSKDLAKI 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFITKLTVRQLVGFGrfpYSHGRLTKKDEEI---ISTYIDFFGL-RELENRfLD----QLSGGQRQRAYVAM 148
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG---LKLNRLVKSKKELqerVRWALEKAQLwDEVKDR-LDapagKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 149 VLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFgrTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
1.18e-19 |
|
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: 84.18 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDE----VRIGpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:cd03245 3 IEFRNVSFSYPNQeipaLDNV--SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFItKLTVRQLVGFGRfPYShgrltkKDEEIISTyIDFFGLRELENRF---LD--------QLSGGQRQRAYV 146
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGA-PLA------DDERILRA-AELAGVTDFVNKHpngLDlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 147 AMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFASkYADNICAVKDGQICAFG 218
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-228 |
1.22e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID-----EGTIEVAGYDVSS--TKSKDL 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 AK-ILSILRQENHFitKLTVRQLVGFGRfpyshgRLTK-KDEEIISTYIDfFGLR------ELENRFLDQ---LSGGQRQ 142
Cdd:PRK14239 85 RKeIGMVFQQPNPF--PMSIYENVVYGL------RLKGiKDKQVLDEAVE-KSLKgasiwdEVKDRLHDSalgLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 143 RAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFgrTIIVVLHDINFASKYADNICAVKDGQICAFGPAEE 222
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233
|
250
....*....|
gi 1899776741 223 IM----HAET 228
Cdd:PRK14239 234 MFmnpkHKET 243
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-231 |
1.24e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 87.49 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDE--VRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSI 79
Cdd:TIGR01846 456 ITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENhFITKLTVRQLVGFGRFPYShgrltkkDEEIISTY-----IDFF-GLRELENRFLDQ----LSGGQRQRAYVAMV 149
Cdd:TIGR01846 536 VLQEN-VLFSRSIRDNIALCNPGAP-------FEHVIHAAklagaHDFIsELPQGYNTEVGEkganLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 150 LCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINfASKYADNICAVKDGQIcafgpAEEIMHAETL 229
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQI-----AESGRHEELL 679
|
..
gi 1899776741 230 SE 231
Cdd:TIGR01846 680 AL 681
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-226 |
1.67e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.47 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYND-EVRIGpANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSI 79
Cdd:COG4598 8 ALEVRDLHKSFGDlEVLKG-VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKL-------------TVRQLVGFGrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAY 145
Cdd:COG4598 87 RRQLQRIRTRLgmvfqsfnlwshmTVLENVIEA--PVHVLGRPKAEaIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLD---IAHSVQMMQHLqraaAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEE 222
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDpelVGEVLKVMRDL----AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
....
gi 1899776741 223 IMHA 226
Cdd:COG4598 241 VFGN 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
2.45e-19 |
|
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: 83.67 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLakilsILRQENHFITKLTVRQLVGFGR 100
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQR 180
Cdd:TIGR01184 80 DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|..
gi 1899776741 181 AAAEFGRTIIVVLHDINFASKYADNICAVKDG 212
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-231 |
2.70e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 11 YNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLA---KILSILRQENHFI 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 88 TKLTVRQLVGFG--RFPYSHGRLTKKDEEIIsTYIDFFGLRElenRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNN 165
Cdd:PRK13638 91 FYTDIDSDIAFSlrNLGVPEAEITRRVDEAL-TLVDAQHFRH---QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 166 LDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFG-PAEEIMHAETLSE 231
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGaPGEVFACTEAMEQ 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-225 |
5.15e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.08 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI----LSILRQENHFITKLTVRQL 95
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGFGRfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:PRK10070 127 TAFGM--ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1899776741 176 QHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-220 |
5.21e-19 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 83.23 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGIT-----ALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKilsilrqenhfiTKLTVRQLV 96
Cdd:cd03237 15 LEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD------------YEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 -----GFGRFPYshgrltkkdeeIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHS 171
Cdd:cd03237 83 ssitkDFYTHPY-----------FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1899776741 172 VQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNIcAVKDGQICAFGPA 220
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGVA 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-214 |
6.30e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYN-----DEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSStKSKDlaki 76
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lSILRQenhfitkltVRQLVGF-GRFPYSHGRLTKKDEEIISTYIDF-FGLRELENRFLD-----------------QLS 137
Cdd:PRK13646 78 -KYIRP---------VRKRIGMvFQFPESQLFEDTVEREIIFGPKNFkMNLDEVKNYAHRllmdlgfsrdvmsqspfQMS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 138 GGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK13646 148 GGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
6.35e-19 |
|
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: 85.24 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVR-----IGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYD--VSSTKSKDL 73
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRgvvkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 AK-----ILSILRQENHFITKLTV----RQLVGFgRFPYSHGRLtKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRA 144
Cdd:TIGR03269 359 GRgrakrYIGILHQEYDLYPHRTVldnlTEAIGL-ELPDELARM-KAVITLKMVGFDEEKAEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 145 YVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-224 |
6.80e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.48 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLL-TMVGRLLDIdEGTIEVAGYDVSSTKSKDLAKILSILRQENHFItKLTVRQLVG- 97
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLArLIVGIWPPT-SGSVRLDGADLKQWDRETFGKHIGYLPQDVELF-PGTVAENIAr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 FGRFPyshgrltkKDEEIISTyIDFFGLRELENRFLD-----------QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNL 166
Cdd:TIGR01842 415 FGENA--------DPEKIIEA-AKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 167 DIAHSVQMMQHLQRAAAEfGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:TIGR01842 486 DEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-232 |
8.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 8.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEV-----RIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSS-----TKSK 71
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 72 DLAKILSILRQENHF-ITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGL-RELENRFLDQLSGGQRQRAYVAMV 149
Cdd:PRK13645 87 RLRKEIGLVFQFPEYqLFQETIEKDIAFG--PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 150 LCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG-PAEEIMHAET 228
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGsPFEIFSNQEL 244
|
....
gi 1899776741 229 LSEI 232
Cdd:PRK13645 245 LTKI 248
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-229 |
9.57e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.90 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 18 GPANLEIPAGGITALVGPNGAGKSTLL-TMVGRLldIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFItKLTVRQLV 96
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLnALLGFL--PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFGRFPYShgrltkkDEEIIS----TYIDFFgLRELENRfLDQ--------LSGGQRQRAYVAMVLCQETDYVLLDEPLN 164
Cdd:PRK11174 444 LLGNPDAS-------DEQLQQalenAWVSEF-LPLLPQG-LDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 165 NLDiAHSVQ-MMQHLQRAAAefGRTIIVVLHDINFASKYaDNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:PRK11174 515 SLD-AHSEQlVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-247 |
1.18e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.51 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDV---SSTKSKDLAKILSILRQENHFITKLTVRQLVG 97
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 fgrFPY-SHGRLTkkdEEIISTYI----DFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD---IA 169
Cdd:PRK11831 107 ---YPLrEHTQLP---APLLHSTVmmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDpitMG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 170 HSVQMMQHLQRAaaeFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEiMHAETLSEIfntpVQIVDG-PDGPL 247
Cdd:PRK11831 181 VLVKLISELNSA---LGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPRV----RQFLDGiADGPV 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-226 |
1.52e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 84.35 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKS-TLLTMVgRLLD----IDEGTIEVAGYDVSSTKSKDLAKI----LSILRQENhfITKL- 90
Cdd:COG4172 30 SFDIAAGETLALVGESGSGKSvTALSIL-RLLPdpaaHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQEP--MTSLn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 91 ---TV-RQLVGFGRFpysHGRLTKKD--EEIIStYIDFFGLRELENRFLD---QLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:COG4172 107 plhTIgKQIAEVLRL---HRGLSGAAarARALE-LLERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLIADE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:COG4172 183 PTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
1.71e-18 |
|
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: 79.78 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSstkskdlakILSILR 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------FASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFItkltvrqlvgfgrfpyshgrltkkdeEIIStyidffglrelenrfldQLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:cd03216 72 ARRAGI--------------------------AMVY-----------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-223 |
1.86e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 6 NVKKDY---NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVA------GYDVSSTKSKDLAKI 76
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFITKLTVRQLVGfgrFPY-SHGRLTKKD-EEIISTYIDFFGL-RELENRF---LDQLSGGQRQRAYVAMVL 150
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIA---YPLkSHGIKEKREiKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSvqmmQHLQRAAAEFGR--TIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNS----QAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-194 |
2.23e-18 |
|
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: 80.29 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMV-GRLLD-IDEGTIEVAGYDVSStksKDLAKILSILRQENHFITKLTVRQLVGF 98
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGlGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 grfpyshgrlTKKdeeiistyidffglrelenrfLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHL 178
Cdd:cd03213 106 ----------AAK---------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170
....*....|....*.
gi 1899776741 179 qRAAAEFGRTIIVVLH 194
Cdd:cd03213 155 -RRLADTGRTIICSIH 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-226 |
2.64e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYdVSStkskdlakILSIlrqeNH-FITKLTVRQLVGF- 98
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSA--------LLEL----GAgFHPELTGRENIYLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 GRFpysHGrLTKKD-----EEIistyIDFFGLRElenrFLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLnnldia 169
Cdd:COG1134 113 GRL---LG-LSRKEidekfDEI----VEFAELGD----FIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVL------ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 170 hSV----------QMMQHLQRAaaefGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:COG1134 175 -AVgdaafqkkclARIRELRES----GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
2.76e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDlakilSIL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVGFGRFPYSHGRLTKkdEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLD 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQR--LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1899776741 161 EPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFA 199
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-218 |
2.85e-18 |
|
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: 80.65 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstkskdlaKILSILRQENHFITKLTVRQLVGF-G 99
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGLGGGFNPELTGRENIYLnG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RFpysHGRLTKKDEEIISTYIDFfglRELENrFLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:cd03220 110 RL---LGLSRKEIDEKIDEIIEF---SELGD-FIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1899776741 176 QHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFG 218
Cdd:cd03220 183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-213 |
4.99e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 79.44 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGRLlDIDEGTIEVAG---YdVSSTKskdlakilsilrqenhFITKLTVRQLV 96
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLsALLGEL-EKLSGSVSVPGsiaY-VSQEP----------------WIQNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFGRfPYSHGRLTK--------KDeeiistyidffgLRELENRflDQ---------LSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:cd03250 87 LFGK-PFDEERYEKvikacalePD------------LEILPDG--DLteigekginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 160 DEPLNNLDiAH-SVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQ 213
Cdd:cd03250 152 DDPLSAVD-AHvGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-224 |
1.29e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQLVGFGR 100
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFND-TIANNIAYAR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 fpysHGRLTKkdEEII-----STYIDFF-----GLREL--ENRFLdqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDI 168
Cdd:PRK11176 442 ----TEQYSR--EQIEeaarmAYAMDFInkmdnGLDTVigENGVL--LSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 169 A--HSVQ-MMQHLQRaaaefGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIM 224
Cdd:PRK11176 514 EseRAIQaALDELQK-----NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-232 |
2.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.02 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRI-GPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSST-KSKDLAK 75
Cdd:PRK13649 3 INLQNVSYTYQAGTPFeGRAlfdvNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 I-----LSILRQENHFITKlTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRE-LENRFLDQLSGGQRQRAYVAMV 149
Cdd:PRK13649 83 IrkkvgLVFQFPESQLFEE-TVLKDVAFG--PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 150 LCQETDYVLLDEPLNNLDIAHSVQMMQhLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFG-PAEEIMHAET 228
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGkPKDIFQDVDF 238
|
....
gi 1899776741 229 LSEI 232
Cdd:PRK13649 239 LEEK 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-236 |
3.87e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKi 76
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHAlnnvSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 lsiLRQE-----NHF--ITKLTVRQLVGfgrFPYshgRLTKKDEEIISTYI----DFFGLRELENRFLDQLSGGQRQRAY 145
Cdd:PRK11153 80 ---ARRQigmifQHFnlLSSRTVFDNVA---LPL---ELAGTPKAEIKARVtellELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPaeeimh 225
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT------ 224
|
250
....*....|.
gi 1899776741 226 aetLSEIFNTP 236
Cdd:PRK11153 225 ---VSEVFSHP 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-232 |
4.72e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSK--DLAKILSILRQ-ENHFITKLTVRQLVG 97
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQyPEYQLFEETIEKDIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 FGrfPyshGRLTKKDEEI---ISTYIDFFGL--RELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSV 172
Cdd:PRK13637 107 FG--P---INLGLSEEEIenrVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 173 QMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM-HAETLSEI 232
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFkEVETLESI 242
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
5.24e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ--PVlkglSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHfITKLTVRQLVGFGrfpyshgrLTKKDEEIISTYIDFFGLREL--ENRFLD--------QLSGGQRQRAYVA 147
Cdd:PRK11160 417 SVVSQRVH-LFSATLRDNLLLA--------APNASDEALIEVLQQVGLEKLleDDKGLNawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 148 MVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFASKYaDNICAVKDGQICAFGPAEEIM 224
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-229 |
7.23e-17 |
|
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: 77.14 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQLVGFGR 100
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SIRDNIALAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FPYSHGRLTKKDEeiISTYIDFF-GLRELENRFLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:cd03252 101 PGMSMERVIEAAK--LAGAHDFIsELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 176 QHLQRAAAefGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:cd03252 179 RNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-223 |
9.09e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.00 E-value: 9.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLD-ID----EGTIEVAGYDVSStKSKDLAKilsilrqenhfitkltVRQL 95
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPgarvEGEILLDGEDIYD-PDVDVVE----------------LRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VG--FGR---FPYS-----------HGRLTKKD-EEIISTYidffgLR------ELENRfLDQ----LSGGQRQRAYVAM 148
Cdd:COG1117 94 VGmvFQKpnpFPKSiydnvayglrlHGIKSKSElDEIVEES-----LRkaalwdEVKDR-LKKsalgLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 149 VLCQETDYVLLDEPLNNLD-IAHSV--QMMQHLqraAAEFgrTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDpISTAKieELILEL---KKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-218 |
9.93e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 77.02 E-value: 9.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPA-GGITALVGPNGAGKSTLLTMV--------GRLLDIDEGTiEVAGYDVSSTKSKDLAKIL------SILRQENHF 86
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWD-EILDEFRGSELQNYFTKLLegdvkvIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 87 ITKL---TVRQLvgfgrfpyshgrLTKKDE-EIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEP 162
Cdd:cd03236 99 IPKAvkgKVGEL------------LKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 163 LNNLDIAHSVQMMQhLQRAAAEFGRTIIVVLHDINFASKYADNICavkdgqiCAFG 218
Cdd:cd03236 167 SSYLDIKQRLNAAR-LIRELAEDDNYVLVVEHDLAVLDYLSDYIH-------CLYG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-233 |
1.18e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLN--NVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLA-KIL 77
Cdd:PRK10895 1 MATLTakNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVgFGRFPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNL-MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 158 LLDEPLNNLD---IAHSVQMMQHLQraaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIF 233
Cdd:PRK10895 160 LLDEPFAGVDpisVIDIKRIIEHLR----DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-224 |
1.92e-16 |
|
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: 78.25 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQEnhfiTKL---TVRQLV 96
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLArLLVG-VWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD----VELfdgTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GfgRFPyshgrlTKKDEEIIS-------------------TYIDFFGLRelenrfldqLSGGQRQRAYVAMVLCQETDYV 157
Cdd:COG4618 427 A--RFG------DADPEKVVAaaklagvhemilrlpdgydTRIGEGGAR---------LSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASkYADNICAVKDGQICAFGPAEEIM 224
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
2.87e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgydvsstkskDLAKILSILR 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----------ETVKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVgfgrfpySHGR--LTKKDEEIIS-TYIDFFGLRELE-NRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:PRK11819 395 SRDALDPNKTVWEEI-------SGGLdiIKVGNREIPSrAYVGRFNFKGGDqQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170 180 190
....*....|....*....|....*....|....*...
gi 1899776741 158 LLDEPLNNLDiahsVQMMQHLQRAAAEFGRTIIVVLHD 195
Cdd:PRK11819 468 LLDEPTNDLD----VETLRALEEALLEFPGCAVVISHD 501
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-229 |
3.20e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQLVGFGr 100
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYG- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 fpyshgrLTKKDEEII------STYIDFFGlrELENRFL-------DQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD 167
Cdd:TIGR00958 579 -------LTDTPDEEImaaakaANAHDFIM--EFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 168 iahsVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:TIGR00958 650 ----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-219 |
4.27e-16 |
|
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: 74.45 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQ-LVGFG 99
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSnLDPFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RFPyshgrltkkDEEIISTyIDFFGLRELENRFLDQL-----------SGGQRQRAYVAMVLCQETDYVLLDEPLNNLDI 168
Cdd:cd03244 103 EYS---------DEELWQA-LERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 169 AHSVQMMQHLQRAAAefGRTIIVVLHDINFASKYaDNICAVKDGQICAFGP 219
Cdd:cd03244 173 ETDALIQKTIREAFK--DCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDS 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-212 |
4.42e-16 |
|
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: 74.67 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGRLLDIdEGTI---EVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQLV 96
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFGRfPYSHGRLTK-KDEEIISTYIDF--FGLR-ELENRFLDqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSV 172
Cdd:cd03290 100 TFGS-PFNKQRYKAvTDACSLQPDIDLlpFGDQtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1899776741 173 QMMQH-LQRAAAEFGRTIIVVLHDINFASkYADNICAVKDG 212
Cdd:cd03290 178 HLMQEgILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-214 |
4.65e-16 |
|
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: 74.78 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYND---EVRI-GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI 76
Cdd:COG4181 8 IIELRGLTKTVGTgagELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LS----ILRQENHFITKLTVR-------QLVGfgrfpysHGRLTKKDEEIISTYidffGLRELENRFLDQLSGGQRQRAY 145
Cdd:COG4181 88 RArhvgFVFQSFQLLPTLTALenvmlplELAG-------RRDARARARALLERV----GLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQI 214
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-241 |
5.89e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.02 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVrigPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSS-TKSKDLAK 75
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PAleniNLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 ILSILRQ--ENHFITKlTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQE 153
Cdd:PRK13644 78 LVGIVFQnpETQFVGR-TVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 154 TDYVLLDEPLNNLDIAHSVQMMQHLQRaAAEFGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIMHAETLSEIF 233
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
....*...
gi 1899776741 234 NTPVQIVD 241
Cdd:PRK13644 233 LTPPSLIE 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-196 |
9.43e-16 |
|
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: 75.98 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 6 NVKKDYND---EVRIGpanlEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgydvsstkskdlAKIlSILRQ 82
Cdd:COG1245 346 DLTKSYGGfslEVEGG----EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------LKI-SYKPQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 83 ENHFITKLTVRQL---VGFGRFPYSHGRltkkdEEIISTyidfFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:COG1245 409 YISPDYDGTVEEFlrsANTDDFGSSYYK-----TEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190
....*....|....*....|....*....|....*..
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDI 196
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-194 |
1.19e-15 |
|
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: 72.78 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 18 GPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstksKDLAKILSILRQENHFI-------TKL 90
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG--------TPLAEQRDEPHENILYLghlpglkPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 91 TVRQLVGFGRfpyshgRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAh 170
Cdd:TIGR01189 89 SALENLHFWA------AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA- 161
|
170 180
....*....|....*....|....
gi 1899776741 171 SVQMMQHLQRAAAEFGRTIIVVLH 194
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
29-229 |
1.45e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 29 ITALVGPNGAGKSTLLTMVGRLLDIDEGTIEV----AGYDVSSTKS------------KDLAKILSILRQENHF-ITKLT 91
Cdd:PRK13631 54 IYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELitnpyskkiknfKELRRRVSMVFQFPEYqLFKDT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 92 VRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRElenRFLD----QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD 167
Cdd:PRK13631 134 IEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLDD---SYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 168 IAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:PRK13631 209 PKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-194 |
1.69e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 26 AGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVsstkskdlakILSILRQENHFI-------TKLTVRQLVGF 98
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----------DDPDVAEACHYLghrnamkPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 GRfpyshgRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHSVQMMQHL 178
Cdd:PRK13539 97 WA------AFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVALFAEL 169
|
170
....*....|....*.
gi 1899776741 179 QRAAAEFGRTIIVVLH 194
Cdd:PRK13539 170 IRAHLAQGGIVIAATH 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
6.08e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYN-----DEVrigpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD-LA 74
Cdd:COG1129 4 LLEMRGISKSFGgvkalDGV-----SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 KILSILRQENHFITKLTVRQLVGFGRFPYSHGRL-TKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQrayvaMV---- 149
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGREPRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ-----LVeiar 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 150 -LCQETDYVLLDEP---LNNLDIAHSVQMMQHLQRAaaefGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:COG1129 154 aLSRDARVLILDEPtasLTEREVERLFRIIRRLKAQ----GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-196 |
6.61e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYND---EVRIGpanlEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVA---GY-------DVSS 67
Cdd:PRK13409 340 LVEYPDLTKKLGDfslEVEGG----EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkiSYkpqyikpDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 68 TKSKDLAKILSILRqENHFITkltvrqlvgfgrfpyshgrltkkdeEIISTyidfFGLRELENRFLDQLSGGQRQRAYVA 147
Cdd:PRK13409 416 TVEDLLRSITDDLG-SSYYKS-------------------------EIIKP----LQLERLLDKNVKDLSGGELQRVAIA 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1899776741 148 MVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDI 196
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-214 |
6.83e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 71.35 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQLVGFGRF 101
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAYGLQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 PYSHGRLTkkdeEIISTYIDFFGLRELENRFLD-------QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHSVQM 174
Cdd:cd03248 114 SCSFECVK----EAAQKAHAHSFISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD-AESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1899776741 175 MQHLQRAAAEfGRTIIVVLHDINFASKyADNICAVKDGQI 214
Cdd:cd03248 189 VQQALYDWPE-RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-213 |
7.33e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDID-----EGTIEVAGYDVSSTKSKDLAKI----LSILRQEN-------H 85
Cdd:PRK15134 30 LQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPmvslnplH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 86 FITKLTVRQLV---GFGRFPyshgrltkKDEEIISTyIDFFGLRELENRFLD---QLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:PRK15134 110 TLEKQLYEVLSlhrGMRREA--------ARGEILNC-LDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-206 |
8.05e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIP-AGGITALVGPNGAGKSTLLTMV-GRL----------LDIDE------GTiEVAGY--DVSSTKSKDLAKIlsil 80
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILsGELkpnlgdydeePSWDEvlkrfrGT-ELQDYfkKLANGEIKVAHKP---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 rQENHFITKL---TVRQLvgfgrfpyshgrLTKKDEE-IISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:COG1245 167 -QYVDLIPKVfkgTVREL------------LEKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNI 206
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYV 282
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-206 |
1.16e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDY-----NDEVrigpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD-LA 74
Cdd:COG3845 5 ALELRGITKRFggvvaNDDV-----SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 KILSILRQenHF--ITKLTVRQLVGFGRFPYSHGRLTKKD-EEIISTYIDFFGLrELE-NRFLDQLSGGQRQRAYVAMVL 150
Cdd:COG3845 80 LGIGMVHQ--HFmlVPNLTVAENIVLGLEPTKGGRLDRKAaRARIRELSERYGL-DVDpDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNI 206
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
1.52e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.83 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYN-----DEVrigpaNLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSstkskDL-- 73
Cdd:COG1137 3 TLEAENLVKSYGkrtvvKDV-----SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-----HLpm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 ---AKI-LSILRQENHFITKLTVRQ-------LVGFGRfpyshgrltKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQ 142
Cdd:COG1137 73 hkrARLgIGYLPQEASIFRKLTVEDnilavleLRKLSK---------KEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 143 RAYVAMVLCQETDYVLLDEPLNNLD-IAhsVQMMQHLQRAAAEFGrtiIVVL---HDINFASKYADNICAVKDGQICAFG 218
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDpIA--VADIQKIIRHLKERG---IGVLitdHNVRETLGICDRAYIISEGKVLAEG 218
|
....*
gi 1899776741 219 PAEEI 223
Cdd:COG1137 219 TPEEI 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-214 |
2.11e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 68.78 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGRLLDIdEGTIEVAGYDVSSTKSKDLAKILSILRQenhfitkltvrqlvgfg 99
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLArLILGLLRPT-SGRVRLDGADISQWDPNELGDHVGYLPQ----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 rfpyshgrltkkDEEIISTYIdffglreLENrfldQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQ 179
Cdd:cd03246 84 ------------DDELFSGSI-------AEN----ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1899776741 180 RAAAEfGRTIIVVLHDINfASKYADNICAVKDGQI 214
Cdd:cd03246 141 ALKAA-GATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-232 |
2.17e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPAN---LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQ--ENHFITKlTVRQLVGFGRFPYSHGR---LTKKDEEIISTYIDFFGLRELEnrfldQLSGGQRQRAYVAMVLCQ 152
Cdd:PRK13642 84 GMVFQnpDNQFVGA-TVEDDVAFGMENQGIPReemIKRVDEALLAVNMLDFKTREPA-----RLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 153 ETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQICA-FGPAEEIMHAETLSE 231
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKeAAPSELFATSEDMVE 236
|
.
gi 1899776741 232 I 232
Cdd:PRK13642 237 I 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-197 |
2.29e-14 |
|
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: 69.44 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 26 AGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkDLAKILSILRQENHFITKLTVRQLVGFgrFPYSH 105
Cdd:cd03231 25 AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIKTTLSVLENLRF--WHADH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 106 GRltkkdeEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEF 185
Cdd:cd03231 102 SD------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARG 175
|
170
....*....|..
gi 1899776741 186 GRTIIVVLHDIN 197
Cdd:cd03231 176 GMVVLTTHQDLG 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
2.55e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDY-----------------NDEVRIGPA----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIE 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalkglfRREYREVEAvddiSFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 60 VAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQlvGFgrfpyshgRLTKK-----DEEI---ISTYIDFFGLRELENR 131
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVFGQRSQLWWDLPAID--SF--------RLLKAiyripDAEYkkrLDELVELLDLGELLDT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 132 FLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDIN 197
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-214 |
2.94e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKS---KDLAKILSILRQE--NHFITKLTVRQLV 96
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRaqrKAFRRDIQMVFQDsiSAVNPRKTVREII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 gfgRFPYSHgrLTKKDE----EIISTYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHS 171
Cdd:PRK10419 113 ---REPLRH--LLSLDKaerlARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1899776741 172 VQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-214 |
2.96e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.53 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYN---DEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIL 77
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQ--ENHFITKlTVRQLVGFGRfpYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:PRK13650 84 GMVFQnpDNQFVGA-TVEDDVAFGL--ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASkYADNICAVKDGQI 214
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
3.13e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.52 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDY-NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD---LAKI 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFITKLTVRQLVGFgrfPYSHGRLTKKD-EEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETD 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMqhlqRAAAEFGR---TIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGIL----RLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
3.68e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.12 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDE------VRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKskDLA 74
Cdd:PRK13633 4 MIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--NLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 KILS----ILRQENHFITKLTVRQLVGFGrfPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVL 150
Cdd:PRK13633 82 DIRNkagmVFQNPDNQIVATIVEEDVAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 151 CQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEI 223
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-214 |
3.86e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 23 EIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI----LSILRQENHFITKLTVRQLVGF 98
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFTALENVAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 grfPYSHGRltKKDEEIISTYIDFF---GLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:PRK11629 111 ---PLLIGK--KKPAEINSRALEMLaavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1899776741 176 QHLQRAAAEFGRTIIVVLHDINFASKYADNIcAVKDGQI 214
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-226 |
3.99e-14 |
|
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: 71.25 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDiDEGTIEVAGYDVSSTKSKDLAKilsiLRQE------------Nhfi 87
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRP----LRRRmqvvfqdpfgslS--- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 88 TKLTVRQLVGFGRfpYSHGR-LTKKD-EEIISTYIDFFGL-RELENRFLDQLSGGQRQRAYVA--MVLcqETDYVLLDEP 162
Cdd:COG4172 377 PRMTVGQIIAEGL--RVHGPgLSAAErRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIAraLIL--EPKLLVLDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 163 LNNLDIahSVQM-----MQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:COG4172 453 TSALDV--SVQAqildlLRDLQR---EHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
4.06e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.73 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKStlLTMVGRLLDIDEGTIEVAG--------YDVSSTKSKDLAKILSILRQEnhFITKLT 91
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGrvlldgkpVAPCALRGRKIATIMQNPRSA--FNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 92 VRqlvgfgrfpySHGRLTKK------DEEIISTYIDFFGLRELEnRFLD----QLSGGQRQRAYVAMVLCQETDYVLLDE 161
Cdd:PRK10418 98 MH----------THARETCLalgkpaDDATLTAALEAVGLENAA-RVLKlypfEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 162 PLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
4.74e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID-----EGTIEVAGYDVSSTKskdlAKI 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERR----VNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENHFITK-----LTVRQLVGFG-RFPYSHGRLTKKDeeIISTYIDFFGL-RELENRF----LDqLSGGQRQRAY 145
Cdd:PRK14258 84 NRLRRQVSMVHPKpnlfpMSVYDNVAYGvKIVGWRPKLEIDD--IVESALKDADLwDEIKHKIhksaLD-LSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKD-----GQICAFGpa 220
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG-- 238
|
250
....*....|....*..
gi 1899776741 221 eeimhaeTLSEIFNTPV 237
Cdd:PRK14258 239 -------LTKKIFNSPH 248
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-229 |
4.80e-14 |
|
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: 71.00 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLltmvGRLL----DIDEGTIEVAGYDVSSTKSKDLAKILSILRQEnhfiTKL---TVR 93
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTL----ARLLfrfyDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD----TVLfndTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 94 QLVGFgrfpyshGRLTKKDEEII----STYIDFF---------------GLRelenrfldqLSGGQRQRAYVAMVLCQET 154
Cdd:COG5265 450 YNIAY-------GRPDASEEEVEaaarAAQIHDFieslpdgydtrvgerGLK---------LSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 155 DYVLLDEPLNNLDiAHSVQMMQH-LQRAAAefGRTIIVVLH------DinfaskyADNICAVKDGQIcafgpAEEIMHAE 227
Cdd:COG5265 514 PILIFDEATSALD-SRTERAIQAaLREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRI-----VERGTHAE 578
|
..
gi 1899776741 228 TL 229
Cdd:COG5265 579 LL 580
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
5.53e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI-LSI 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKLTVRQLVGFGRFPyshgrlTKK-----------DEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAM 148
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHL------TKKvcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 149 VLCQETDYVLLDEP---LNNLDIAHSVQMMQHLQRAaaefGRTIIVVLHDINFASKYADNICAVKDG 212
Cdd:PRK09700 159 TLMLDAKVIIMDEPtssLTNKEVDYLFLIMNQLRKE----GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-219 |
6.04e-14 |
|
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: 71.20 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 29 ITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVsSTKSKDLAKILSILRQENHFITKLTVRQLVGFgrFPYSHGRL 108
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF--YAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 109 TKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRT 188
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRT 1112
|
170 180 190
....*....|....*....|....*....|..
gi 1899776741 189 IIVVLHDINFASKYADNICAVKDGQI-CAFGP 219
Cdd:TIGR01257 1113 IIMSTHHMDEADLLGDRIAIISQGRLyCSGTP 1144
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-206 |
7.31e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIP-AGGITALVGPNGAGKSTLLTMV-GRLL----------DIDE------GTiEVAGY--DVSSTKSKDLAKIlsil 80
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKILsGELIpnlgdyeeepSWDEvlkrfrGT-ELQNYfkKLYNGEIKVVHKP---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 rQENHFITKL---TVRQLvgfgrfpyshgrLTKKDEE-IISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:PRK13409 167 -QYVDLIPKVfkgKVREL------------LKKVDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDINFASKYADNI 206
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV 281
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
1.00e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGpanleIPAGGITALVGPNGAGKSTLLTMVGRLLDidegtiEVAGYDVSstkskdlAKILSILR 81
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMG-----FPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYRYS-------GDVLLGGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 82 QENHFITKLTVRQLVG--FGR---FPYS-----------HGRLTKKD-EEIISTYIDFFGLRE-LENRFLD---QLSGGQ 140
Cdd:PRK14271 89 SIFNYRDVLEFRRRVGmlFQRpnpFPMSimdnvlagvraHKLVPRKEfRGVAQARLTEVGLWDaVKDRLSDspfRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 141 RQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFgrTIIVVLHDINFASKYADNICAVKDGQICAFGPA 220
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
250
....*....|..
gi 1899776741 221 EEIM----HAET 228
Cdd:PRK14271 247 EQLFsspkHAET 258
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-214 |
1.06e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSS-TKSKDLAKILSI 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITKLTVRQLVGFGRFpysHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGF---FAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-213 |
1.89e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD-LAKILSILRQENHFITKLTVRQLVGFGR 100
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEMTVAENLYLGQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FPYSHGRLTKKDeeiistyIDFFGLRELENRFLD--------QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSV 172
Cdd:PRK11288 105 LPHKGGIVNRRL-------LNYEAREQLEHLGVDidpdtplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1899776741 173 QMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:PRK11288 178 QLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-168 |
1.89e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 12 NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSST-KSKDLAKI--LSILRQ-----E 83
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRFMAYLghLPGLKAdlstlE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 84 N-HFITKLtvrqlvgfgrfpysHGRLTKKdeeIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEP 162
Cdd:PRK13543 102 NlHFLCGL--------------HGRRAKQ---MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*.
gi 1899776741 163 LNNLDI 168
Cdd:PRK13543 165 YANLDL 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-217 |
3.03e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLL-TMVGRlLDIDEGTIEVA-----GY---DVSSTKSKD 72
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLrTLVGE-LEPDSGTVKWSenaniGYyaqDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 73 LAKI--LSILRQENHfiTKLTVRQLVgfgrfpyshGRLTKKDEEIistyidffglreleNRFLDQLSGGQRQRAYVAMVL 150
Cdd:PRK15064 399 LTLFdwMSQWRQEGD--DEQAVRGTL---------GRLLFSQDDI--------------KKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 151 CQETDYVLLDEPLNNLDIahsvQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAF 217
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDF 516
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-217 |
3.13e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.66 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVA-----GYDVSSTkskdlak 75
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQ------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 iLSILRQENHFITKLTvrqlvgfgrfpyshgRLTKKD-EEIISTYIDFFGLR-----ELENRFldqlSGGQRQRAYVAMV 149
Cdd:PRK10636 385 -LEFLRADESPLQHLA---------------RLAPQElEQKLRDYLGGFGFQgdkvtEETRRF----SGGEKARLVLALI 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 150 LCQETDYVLLDEPLNNLDIahsvQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAF 217
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPF 508
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-230 |
8.21e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEvagydvsstksKDLAKILSIL 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITK--LTVrqlvgfGRFPYSHGRLTKKDeeiISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVL 158
Cdd:PRK09544 73 PQKLYLDTTlpLTV------NRFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 159 LDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVkDGQICAFGPAEEI-MHAETLS 230
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVsLHPEFIS 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-223 |
9.23e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQeNHFITKLTVRQLVGFGR 100
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTVANNIALGR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FPYSH------GRLTKKDEEII---STYIDFFGLRELenrfldQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHS 171
Cdd:PRK10789 414 PDATQqeiehvARLASVHDDILrlpQGYDTEVGERGV------MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 172 VQMMQHLQRAAAefGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK10789 488 HQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-211 |
9.80e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 9.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMV-GRLLDI-DEGTIEVAGYDVSSTKSkdlakILSILRQENHFITKLTVRQLVG 97
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLaGALKGTpVAGCVDVPDNQFGREAS-----LIDAIGRKGDFKDAVELLNAVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 FGrfpyshgrltkkdeeiistyiDFFGLRelenRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQH 177
Cdd:COG2401 124 LS---------------------DAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170 180 190
....*....|....*....|....*....|....
gi 1899776741 178 LQRAAAEFGRTIIVVLHDINFASKYADNICAVKD 211
Cdd:COG2401 179 LQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-222 |
2.08e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLL-TMVGRL---LDIDeGTIEVAGYDVSstkSKDLAKILSILRQENHFITKLTVRQLVGFgrfp 102
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMnALAFRSpkgVKGS-GSVLLNGMPID---AKEMRAISAYVQQDDLFIPTLTVREHLMF---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 103 YSHGRL-----TKKDEEIISTYIDFFGLRELENRFLDQ------LSGGQRQRAYVAMVLCqeTDYVLL--DEPLNNLD-- 167
Cdd:TIGR00955 123 QAHLRMprrvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELL--TDPPLLfcDEPTSGLDsf 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 168 IAHSV-QMMQHLqraaAEFGRTIIVVLH----DI--NFaskyaDNICAVKDGQICAFGPAEE 222
Cdd:TIGR00955 201 MAYSVvQVLKGL----AQKGKTIICTIHqpssELfeLF-----DKIILMAEGRVAYLGSPDQ 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-221 |
2.43e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDID--EGTIEVAGYDVSSTKSKDL-AKIL 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVGFGRFPYSHGRLTKKDEEIISTYIdffGLRELE------NRFLDQLSGGQRQRAYVAMVLC 151
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKN---LLRELQldadnvTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 152 QETDYVLLDEPLNNLdIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAE 221
Cdd:TIGR02633 158 KQARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMS 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-218 |
3.54e-12 |
|
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: 63.59 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 23 EIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVR-QLVGFGRF 101
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG-TIRsNLDPFDEY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 pyshgrltkKDEEIistyidFFGLRELENRflDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIaHSVQMMQHLQRa 181
Cdd:cd03369 109 ---------SDEEI------YGALRVSEGG--LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY-ATDALIQKTIR- 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1899776741 182 aAEF-GRTIIVVLHDINFASKYaDNICAVKDGQICAFG 218
Cdd:cd03369 170 -EEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-207 |
3.91e-12 |
|
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: 65.34 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLL-TMVGrlLDID-EGTIEVA-GYDVSstkskdlakilsILRQENHFITKLTVRQLVGFG--------- 99
Cdd:TIGR03719 36 VLGLNGAGKSTLLrIMAG--VDKDfNGEARPQpGIKVG------------YLPQEPQLDPTKTVRENVEEGvaeikdald 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RFPYSHGRLTKKDEEI---------ISTYIDFFGLRELENRfLDQ----------------LSGGQRQRAYVAMVLCQET 154
Cdd:TIGR03719 102 RFNEISAKYAEPDADFdklaaeqaeLQEIIDAADAWDLDSQ-LEIamdalrcppwdadvtkLSGGERRRVALCRLLLSKP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 155 DYVLLDEPLNNLDiAHSVQMM-QHLQraaaEFGRTIIVVLHDINFaskyADNIC 207
Cdd:TIGR03719 181 DMLLLDEPTNHLD-AESVAWLeRHLQ----EYPGTVVAVTHDRYF----LDNVA 225
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-195 |
8.83e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLL-TMVGrlLDID-EGTIEVA-GYDVSstkskdlakilsILRQENHFITKLTVRQLV--GFG------- 99
Cdd:PRK11819 38 VLGLNGAGKSTLLrIMAG--VDKEfEGEARPApGIKVG------------YLPQEPQLDPEKTVRENVeeGVAevkaald 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RF-----PYSH------------GRLtkkdEEIIstyiDFFGLRELENRfLDQ----------------LSGGQRQRayV 146
Cdd:PRK11819 104 RFneiyaAYAEpdadfdalaaeqGEL----QEII----DAADAWDLDSQ-LEIamdalrcppwdakvtkLSGGERRR--V 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 147 AmvLC----QETDYVLLDEPLNNLDiAHSVQMM-QHLQRaaaeFGRTIIVVLHD 195
Cdd:PRK11819 173 A--LCrlllEKPDMLLLDEPTNHLD-AESVAWLeQFLHD----YPGTVVAVTHD 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-194 |
1.04e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.06 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVK-KDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgydvsstkskDLAKILsI 79
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP----------AGARVL-F 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENHFITkLTVRQLVgfgRFPYSHGRLTkkDEEIISTyIDFFGLRELENRfLDQ-------LSGGQRQRAYVAMVLCQ 152
Cdd:COG4178 431 LPQRPYLPL-GTLREAL---LYPATAEAFS--DAELREA-LEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1899776741 153 ETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLH 194
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGH 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-239 |
1.05e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 26 AGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTkSKDLAKILSI--LRQENHFITKLTVRQ--LVGFGRF 101
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQLGIylVPQEPLLFPNLSVKEniLFGLPKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 PYSHGRLTKKdeeiistyidffgLRELENRF-LDQLSG----GQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQ 176
Cdd:PRK15439 115 QASMQKMKQL-------------LAALGCQLdLDSSAGslevADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 177 HLqRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAETLSEIfnTPVQI 239
Cdd:PRK15439 182 RI-RELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI--TPAAR 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-238 |
1.52e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLLDI-----DEGTIEVAGYDVSSTKskdlakilsilrqenhfITKLTVRQLV 96
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPD-----------------VDPVEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 G--FGR---FPYShgrltKKDEEIISTYIDFF--GLRELENRFLDQ-----------------LSGGQRQRAYVAMVLCQ 152
Cdd:PRK14243 94 GmvFQKpnpFPKS-----IYDNIAYGARINGYkgDMDELVERSLRQaalwdevkdklkqsglsLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 153 ETDYVLLDEPLNNLDIAHSV---QMMQHLQRAaaefgRTIIVVLHDINFASKYAD-----NICAVKDGqicafGPAEEIM 224
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLrieELMHELKEQ-----YTIIIVTHNMQQAARVSDmtaffNVELTEGG-----GRYGYLV 238
|
250
....*....|....
gi 1899776741 225 HAETLSEIFNTPVQ 238
Cdd:PRK14243 239 EFDRTEKIFNSPQQ 252
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-194 |
1.78e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMV-GRLLDID-EGTIEVAGYDVSstksKDLAKILSILRQENHFITKLTVRQLVGFG---RF 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKPT----KQILKRTGFVTQDDILYPHLTVRETLVFCsllRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 PYShgrLTKKDEEIIS-TYIDFFGLRELEN-----RFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:PLN03211 170 PKS---LTKQEKILVAeSVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170
....*....|....*....
gi 1899776741 176 QHLQrAAAEFGRTIIVVLH 194
Cdd:PLN03211 247 LTLG-SLAQKGKTIVTSMH 264
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
1.98e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVsstkSKDLA---KIL 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCtyqKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 78 SILRQENHFITKLTVRQLVGFGrFPYSHGRLTkkdeeiISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYV 157
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYD-IHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1899776741 158 LLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDI 196
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-221 |
2.30e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.00 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGRL-LDIDEGTIEVAGYDvsstkskdlakilsilrqenhfITKLTV--RQLV 96
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAkTIMGHPkYEVTEGEILFKGED----------------------ITDLPPeeRARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 G-FGRFPYShgrltkkdEEIISTYIDFFgLRELENRFldqlSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIaHSVQMM 175
Cdd:cd03217 78 GiFLAFQYP--------PEIPGVKNADF-LRYVNEGF----SGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1899776741 176 QHLQRAAAEFGRTIIVVLHDINFAsKY--ADNICAVKDGQICAFGPAE 221
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLL-DYikPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-218 |
2.51e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.12 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 26 AGGITALVGPNGAGKSTLLTMVGRLLDID---EGTIEVAGYDVSSTKSKDLAKILSILRQENHFITkLTVRQLvgfgrfp 102
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPT-LTVRET------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 103 yshgrltkkdeeiistyIDFfGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAA 182
Cdd:cd03233 104 -----------------LDF-ALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1899776741 183 AEFGRTIIVVLHDinfASK--YA--DNICAVKDGQICAFG 218
Cdd:cd03233 166 DVLKTTTFVSLYQ---ASDeiYDlfDKVLVLYEGRQIYYG 202
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-214 |
2.81e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 5 NNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEvagYDVSSTKSKDLAKiLS------ 78
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH---YRMRDGQLRDLYA-LSeaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 79 ILRQENHFIT-------KLTV-------RQLVGFGRFPYSHGRLTKKD----EEIISTYIDffglrELENRFldqlSGGQ 140
Cdd:PRK11701 86 LLRTEWGFVHqhprdglRMQVsaggnigERLMAVGARHYGDIRATAGDwlerVEIDAARID-----DLPTTF----SGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 141 RQRAYVAMVLCQETDYVLLDEPLNNLDIahSVQ--MMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDV--SVQarLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-213 |
4.26e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVS--STKSKDLAKIlSILRQENHFITKLTVRQLVG 97
Cdd:PRK10762 23 AALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAGI-GIIHQELNLIPQLTIAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 FGR-FPYSHGRLT-KKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM 175
Cdd:PRK10762 102 LGReFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLF 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1899776741 176 QHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:PRK10762 182 RVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-215 |
4.70e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDE-VRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITkltvrQLVGFGRFPyshgrltkKDEEIISTYIDFFGLR---ELE-NRFLD-QLSGGQRQRAYVAMVLCQETD 155
Cdd:PRK10522 403 FTDFHLFD-----QLLGPEGKP--------ANPALVEKWLERLKMAhklELEdGRISNlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 156 YVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQIC 215
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLS 528
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-194 |
5.34e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.95 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLL-TMVGRLLD-IDEGTIEVAGYdvssTKSKDLAKILSILRQENHFITKLTVRQLVGFgrfpys 104
Cdd:cd03232 33 GTLTALMGESGAGKTTLLdVLAGRKTAgVITGEILINGR----PLDKNFQRSTGYVEQQDVHSPNLTVREALRF------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 105 hgrltkkdeeiiSTYidffgLRElenrfldqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAE 184
Cdd:cd03232 103 ------------SAL-----LRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170
....*....|
gi 1899776741 185 fGRTIIVVLH 194
Cdd:cd03232 158 -GQAILCTIH 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-219 |
5.72e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKskdlAKILSILRQENHFI-----TKLTVRQLVGfgrf 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS----PGKLQALRRDIQFIfqdpyASLDPRQTVG---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 102 pYS-------HGRLT-KKDEEIISTYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDI---A 169
Cdd:PRK10261 422 -DSimeplrvHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirG 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1899776741 170 HSVQMMQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGP 219
Cdd:PRK10261 501 QIINLLLDLQR---DFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-214 |
5.99e-11 |
|
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: 62.06 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 11 YNDEVrIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKL 90
Cdd:TIGR01193 485 YGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 91 TVRQLVgfgrfpysHGRLTKKDEEIISTYIDFFGLR-ELENRFL----------DQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:TIGR01193 564 ILENLL--------LGAKENVSQDEIWAACEIAEIKdDIENMPLgyqtelseegSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 160 DEPLNNLDIAHSVQMMQHLQRAAAefgRTIIVVLHDINFASKyADNICAVKDGQI 214
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKI 686
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-229 |
6.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLT-MVGRLLDIDEGTIEVAGydvsstkskDLAKILSIlrqenHFITKLTVRQLVGFG 99
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG---------SVAYVPQV-----SWIFNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RfPYSHGRLTKK-DEEIISTYIDFFG---LRELENRFLDqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD--IAHSV- 172
Cdd:PLN03232 703 S-DFESERYWRAiDVTALQHDLDLLPgrdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahVAHQVf 780
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 173 -QMMQHLQRaaaefGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:PLN03232 781 dSCMKDELK-----GKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-194 |
7.49e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.09 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVK-KDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEvagydvsstkskdlakilsIL 80
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-------------------MP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHF-------ITKLTVRQLVgfgRFPYShgrltkkdeeiistyidffglrelenrflDQLSGGQRQRAYVAMVLCQE 153
Cdd:cd03223 62 EGEDLLflpqrpyLPLGTLREQL---IYPWD-----------------------------DVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1899776741 154 TDYVLLDEPLNNLDIAHSVQMMQHLQraaaEFGRTIIVVLH 194
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-225 |
7.83e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.26 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKIlsilRQENHFI---------TKLT 91
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV----RSDIQMIfqdplaslnPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 92 VRQLVGFGRFPYsHGRLTKKD-EEIISTYIDFFGLRE-LENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDI- 168
Cdd:PRK15079 117 IGEIIAEPLRTY-HPKLSRQEvKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVs 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 169 --AHSVQMMQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMH 225
Cdd:PRK15079 196 iqAQVVNLLQQLQR---EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYH 251
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-206 |
9.39e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTI-----------------EVAG- 62
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqqdpprNVEGt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 63 -YDVSSTKSKDLAKILSILRQENHFI-TKLTVRQLvgfgrfpyshGRLTKKDEEIistyiDFFGLRELENRF-------- 132
Cdd:PRK11147 83 vYDFVAEGIEEQAEYLKRYHDISHLVeTDPSEKNL----------NELAKLQEQL-----DHHNLWQLENRInevlaqlg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 133 ------LDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIahsvQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNI 206
Cdd:PRK11147 148 ldpdaaLSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-228 |
1.21e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRqlvgFGRFPYSHGRLTKK 111
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVR----FNIDPFSEHNDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 112 DEEIISTYI------DFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiahsVQMMQHLQRAAAEF 185
Cdd:PLN03232 1342 WEALERAHIkdvidrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQRTIREE 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1899776741 186 GR--TIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMHAET 228
Cdd:PLN03232 1418 FKscTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-224 |
1.45e-10 |
|
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: 61.11 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstkskdlaKILSILRQEnhFITKLTVRQLVGFGR 100
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQA--WIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 F---PYSHGRLTK----KDEEIISTyidffGLR-ELENRFLDqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSV 172
Cdd:TIGR00957 724 AlneKYYQQVLEAcallPDLEILPS-----GDRtEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 173 QMMQHLQRAAAEF-GRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIM 224
Cdd:TIGR00957 798 HIFEHVIGPEGVLkNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
131-226 |
1.59e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 131 RFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVK 210
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY 243
|
90
....*....|....*.
gi 1899776741 211 DGQICAFGPAEEIMHA 226
Cdd:PRK10261 244 QGEAVETGSVEQIFHA 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-206 |
1.74e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKLTVRQLVgfgrFPYSHgRLTKKDEEIISTYIDFFGLRE-LENRFLDQLSGGQRQRA-------YVAMVLcq 152
Cdd:PRK10247 87 AQTPTLFGDTVYDNLI----FPWQI-RNQQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRIslirnlqFMPKVL-- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 153 etdyvLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINfASKYADNI 206
Cdd:PRK10247 160 -----LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKV 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-210 |
2.64e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.39 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 28 GITALVGPNGAGKSTLLtmvgrlldidEGtIEVAGYDVSSTKSKDLAKILSILR-QENHFITKLTVRqlvgfgrfpyshg 106
Cdd:cd03240 23 PLTLIVGQNGAGKTTII----------EA-LKYALTGELPPNSKGGAHDPKLIReGEVRAQVKLAFE------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 107 rLTKKDEEIISTYIDFF---------GLRELENRFLDQLSGGQRQ------RAYVAMVLCQETDYVLLDEPLNNLDIAH- 170
Cdd:cd03240 79 -NANGKKYTITRSLAILenvifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENi 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1899776741 171 SVQMMQHLQRAAAEFGRTIIVVLHDINFAsKYADNICAVK 210
Cdd:cd03240 158 EESLAEIIEERKSQKNFQLIVITHDEELV-DAADHIYRVE 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-214 |
4.65e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 25 PAGGItALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKilsiLRQEN--------HFITKLTVR--- 93
Cdd:PRK10584 35 RGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK----LRAKHvgfvfqsfMLIPTLNALenv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 94 QLVGFGRfpyshGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQ 173
Cdd:PRK10584 110 ELPALLR-----GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1899776741 174 MMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQI 214
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-223 |
4.79e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKiLSILRQENHF--------ITKLTV 92
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRTFQHVrlfremtvIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 93 RQ--------LVGFGRFPySHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLN 164
Cdd:PRK11300 104 AQhqqlktglFSGLLKTP-AFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 165 NLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-225 |
5.86e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLT-MVGRLLDIDEGTIEVAGydvsstkskDLAKILSIlrqenHFITKLTVRQLVGFG 99
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG---------TVAYVPQV-----SWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RfPYSHGRLTKKdeeiistyIDFFGLR------------ELENRFLDqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLD 167
Cdd:PLN03130 703 S-PFDPERYERA--------IDVTALQhdldllpggdltEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 168 iAHSVQMM------QHLQraaaefGRTIIVVLHDINFASkYADNICAVKDGQICAFGPAEEIMH 225
Cdd:PLN03130 773 -AHVGRQVfdkcikDELR------GKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-223 |
6.69e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 20 ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD-LAKILSILRQENHFITKLTVRQLVGF 98
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDNMWL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 GRFP-----YSHGRLTKKDEEIISTY-IDFFGLRELENrfldqLSGGQRQRAYVAMVLCQETDYVLLDEPLNNL---DIA 169
Cdd:PRK10982 97 GRYPtkgmfVDQDKMYRDTKAIFDELdIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 170 HSVQMMQHLQraaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK10982 172 HLFTIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-228 |
6.89e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKS-TLLTMVGRLLD--IDEGTIEVAGYDVSSTKSKDLAKI----LSILRQENhfITKLTvr 93
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKELNKLraeqISMIFQDP--MTSLN-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 94 qlvgfgrfPYS------------HGRLTKKD--EEIISTyIDFFGLRELENR---FLDQLSGGQRQRAYVAMVLCQETDY 156
Cdd:PRK09473 112 --------PYMrvgeqlmevlmlHKGMSKAEafEESVRM-LDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 157 VLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHAET 228
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-194 |
1.27e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.05 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 23 EIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQE----NHFITK-LTVrqlvg 97
Cdd:PRK13657 357 EAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDaglfNRSIEDnIRV----- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 fgrfpyshGRLTKKDEEI-----ISTYIDFFGLRelENRFL-------DQLSGGQRQRAYVAMVLCQETDYVLLDEPLNN 165
Cdd:PRK13657 432 --------GRPDATDEEMraaaeRAQAHDFIERK--PDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190
....*....|....*....|....*....|.
gi 1899776741 166 LDIAHSVQmmqhLQRAAAEF--GRTIIVVLH 194
Cdd:PRK13657 502 LDVETEAK----VKAALDELmkGRTTFIIAH 528
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-223 |
2.00e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 23 EIPAGGITALVGPNGAGKSTLltmvGRLLDIDE----GTIEVAGYDV---SSTKSKDLAKILSILRQeNHFiTKLTVRQL 95
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTL----ARLLTMIEtptgGELYYQGQDLlkaDPEAQKLLRQKIQIVFQ-NPY-GSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 96 VGF--GRFPYSHGRLTKKD-EEIISTYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIahS 171
Cdd:PRK11308 111 VGQilEEPLLINTSLSAAErREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV--S 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1899776741 172 VQ-----MMQHLQRaaaEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK11308 189 VQaqvlnLMMDLQQ---ELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-168 |
3.84e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 55.34 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLL-TMVGR-LLDIDEGTIEVAGYDVSSTKSKDLAKI-LSILRQENHFITKLTVRQlvg 97
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSkTIAGHpSYEVTSGTILFKGQDLLELEPDERARAgLFLAFQYPEEIPGVSNLE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 98 FGRFPYShGRLTKKDEEIISTYiDFFGL-----------RELENRFLDQ-LSGGQRQRAYVAMVLCQETDYVLLDEPLNN 165
Cdd:TIGR01978 97 FLRSALN-ARRSARGEEPLDLL-DFEKLlkeklalldmdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSG 174
|
...
gi 1899776741 166 LDI 168
Cdd:TIGR01978 175 LDI 177
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
4.31e-09 |
|
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: 55.13 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYN----DEVRIGP---ANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgydvSSTKSKDL 73
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRLPVldgVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 AK-----ILSILRQENHFITK-LTV------RQLV-------GFGRfpyshGRLTKKDEEIISTyidfFGLRELenrfLD 134
Cdd:COG4778 80 AQaspreILALRRRTIGYVSQfLRViprvsaLDVVaepllerGVDR-----EEARARARELLAR----LNLPER----LW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 135 QL-----SGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHS----VQMMQHLQRAaaefGRTIIVVLHDINFASKYADN 205
Cdd:COG4778 147 DLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLD-AANravvVELIEEAKAR----GTAIIGIFHDEEVREAVADR 221
|
....*...
gi 1899776741 206 ICAVKDGQ 213
Cdd:COG4778 222 VVDVTPFS 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-248 |
4.39e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTL-LTMVGRLLdIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHfiTKLTVRQLVGFG 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALaRALAGELP-LLSGERQSQFSHITRLSFEQLQKLVSDEWQRNN--TDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RFPYSHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQ 179
Cdd:PRK10938 100 RTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 180 RAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM---------HAETLSEIfntpvqIVDGPDGPLA 248
Cdd:PRK10938 180 SLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILqqalvaqlaHSEQLEGV------QLPEPDEPSA 250
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-227 |
4.79e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDY-NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 81 RQENHFITKlTVRQLVGFGRfpyshgrltKKDEEIISTYIDFFGLRELENRFLD-----------QLSGGQRQRAYVAMV 149
Cdd:PRK10790 421 QQDPVVLAD-TFLANVTLGR---------DISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899776741 150 LCQETDYVLLDEPLNNLDiAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMHAE 227
Cdd:PRK10790 491 LVQTPQILILDEATANID-SGTEQAIQQALAAVRE-HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-217 |
6.66e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 31 ALVGPNGAGKSTLLTMVGRLLDIDEGTIevagydVSSTKSKdlakiLSILRQENHFITKLTVRQLVGFGR-FPyshGRLT 109
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MAVFSQHHVDGLDLSSNPLLYMMRcFP---GVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 110 KKdeeiISTYIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLqraaAEFGRT 188
Cdd:PLN03073 605 QK----LRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL----VLFQGG 676
|
170 180
....*....|....*....|....*....
gi 1899776741 189 IIVVLHDINFASKYADNICAVKDGQICAF 217
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-222 |
7.61e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 8 KKDYNDEVRI-GPANLEIPAGGITALVGPNGAGKSTLL-TMVGRL---LDIDEGTIEVAGYDVSSTKSKDLAKILSILRQ 82
Cdd:TIGR00956 67 KFRDTKTFDIlKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTdgfHIGVEGVITYDGITPEEIKKHYRGDVVYNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 83 ENHFiTKLTVRQLVGFG---RFPYSHGRLTKKDE---EIISTYIDFFGLR-----ELENRFLDQLSGGQRQRAYVAMVLC 151
Cdd:TIGR00956 147 DVHF-PHLTVGETLDFAarcKTPQNRPDGVSREEyakHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 152 QETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDinfASKYA----DNICAVKDGQICAFGPAEE 222
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQ---CSQDAyelfDKVIVLYEGYQIYFGPADK 297
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-200 |
9.48e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIevagydvsSTKSKDLAKilsiLRQENHfitkltvRQLVGFG- 99
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV--------LWQGEPIRR----QRDEYH-------QDLLYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 --------------RFPYSHGRLTkkDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNN 165
Cdd:PRK13538 82 qpgikteltalenlRFYQRLHGPG--DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1899776741 166 LDiAHSVQMMQHLQRAAAEFGRTIIVVLH-DINFAS 200
Cdd:PRK13538 160 ID-KQGVARLEALLAQHAEQGGMVILTTHqDLPVAS 194
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-219 |
3.47e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLL-TMVGRLL-DIDEGTIEVAGYdvsSTKSKDLAKILSILRQENHFITKLTVRQLVGFGRFPys 104
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMdVLAGRKTgGYIEGDIRISGF---PKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFL-- 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 105 hgRLTK---KDEEIIstYID-FFGLRELEN--------RFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHSV 172
Cdd:PLN03140 981 --RLPKevsKEEKMM--FVDeVMELVELDNlkdaivglPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAA 1055
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1899776741 173 QMMQHLQRAAAEFGRTIIVVLH--DINFASKYADNICAVKDGQICAFGP 219
Cdd:PLN03140 1056 AIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGP 1104
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
4.15e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMV------GRLldidEGTIEVAGYDVSSTKSKDL- 73
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphGTY----EGEIIFEGEELQASNIRDTe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 AKILSILRQENHFITKLTVRQLVGFGRFPYSHGRL-----TKKDEEIistyidffgLRELE-----NRFLDQLSGGQRQR 143
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIMdydamYLRAQKL---------LAQLKldinpATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 144 AYVAMVLCQETDYVLLDEPLNNL---DIAHSVQMMQHLQRAaaefGRTIIVVLHDINFASKYADNICAVKDGQICAFGPA 220
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAH----GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPA 227
|
...
gi 1899776741 221 EEI 223
Cdd:PRK13549 228 AGM 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-162 |
5.41e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD------------LAKilsilrqeNHFIT 88
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRavcpriaympqgLGK--------NLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 89 kLTVRQLVGFgrfpysHGRLtkkdeeiistyidfFGLRELENR--------------FLD----QLSGGQRQRayvaMVL 150
Cdd:NF033858 93 -LSVFENLDF------FGRL--------------FGQDAAERRrridellratglapFADrpagKLSGGMKQK----LGL 147
|
170
....*....|....*.
gi 1899776741 151 C----QETDYVLLDEP 162
Cdd:NF033858 148 CcaliHDPDLLILDEP 163
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-194 |
1.12e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLL-TMVGRLLD--IDEGTIEVAGYDVSSTkskdLAKILSILRQENHFITKLTVRQLVGFGRFPY 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLnVLAERVTTgvITGGDRLVNGRPLDSS----FQRSIGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 104 SHGRLTKKDE-EIISTYIDFFGLRELENRFL----DQLSGGQRQRAYVAMVLCQETDYVL-LDEPLNNLDIAHSVQMMQh 177
Cdd:TIGR00956 865 QPKSVSKSEKmEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK- 943
|
170
....*....|....*..
gi 1899776741 178 LQRAAAEFGRTIIVVLH 194
Cdd:TIGR00956 944 LMRKLADHGQAILCTIH 960
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
135-226 |
1.15e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 135 QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|..
gi 1899776741 215 CAFGPAEEIMHA 226
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-225 |
1.70e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLtmvGRLLdideGTIEVAGYDVSSTKSkdlakILSILRQEnhFITKLTVRQLVGFgr 100
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLL---QSLL----SQFEISEGRVWAERS-----IAYVPQQA--WIMNATVRGNILF-- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FpyshgrltkkDEEIISTYIDFFGLRELENRfLDQL---------------SGGQRQRAYVAMVLCQETDYVLLDEPLNN 165
Cdd:PTZ00243 744 F----------DEEDAARLADAVRVSQLEAD-LAQLgggleteigekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 166 LDiAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKyADNICAVKDGQICAFGPAEEIMH 225
Cdd:PTZ00243 813 LD-AHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
2.42e-07 |
|
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: 49.35 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 16 RIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDL--AKILSIL--RQENHFITKLT 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAirAGIAYVPedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 92 VRqlvgfgrfpyshgrltkkdeeiistyidffglrelENRFL-DQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAH 170
Cdd:cd03215 95 VA-----------------------------------ENIALsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1899776741 171 SVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-238 |
2.48e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKlTVRQLVGfgrfPYshgrLTKK 111
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVD----PF----LEAS 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 112 DEEIISTyIDFFGLRE--------LENRFLD---QLSGGQRQRAYVAMVLCQE-TDYVLLDEPLNNLDIAHSVQMMQHLQ 179
Cdd:PTZ00243 1412 SAEVWAA-LELVGLRErvasesegIDSRVLEggsNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVM 1490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 180 RAAAEFgrTIIVVLHDINFASKYaDNICAVKDGQICAFGPAEEImhAETLSEIFNTPVQ 238
Cdd:PTZ00243 1491 SAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL--VMNRQSIFHSMVE 1544
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
3.11e-07 |
|
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: 50.57 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTM--------------------------------VGR 49
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrgmdqyeptsgriiyhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 50 LLDIDEGT---IEVAGYDVSSTKSKDLAKILSILRQ------ENHFITKLTVRQLVGFGRfpyshgrltkKDEEIISTYI 120
Cdd:TIGR03269 81 PCPVCGGTlepEEVDFWNLSDKLRRRIRKRIAIMLQrtfalyGDDTVLDNVLEALEEIGY----------EGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 121 DFFGLRELENRFLD---QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDIN 197
Cdd:TIGR03269 151 DLIEMVQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 1899776741 198 FASKYADNICAVKDGQICAFGPAEEI 223
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-194 |
3.34e-07 |
|
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: 50.90 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 12 NDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIevagydvssTKSKDlAKILSILRQEnhFITKLT 91
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL---------TKPAK-GKLFYVPQRP--YMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 92 VR-QLVgfgrFPYSHGRLTKKD--EEIISTYIDFFGLRELENR---------FLDQLSGGQRQRAYVAMVLCQETDYVLL 159
Cdd:TIGR00954 531 LRdQII----YPDSSEDMKRRGlsDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 1899776741 160 DEPLNnldiAHSVQMMQHLQRAAAEFGRTIIVVLH 194
Cdd:TIGR00954 607 DECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-206 |
3.54e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 30 TALVGPNGAGKSTLLTMVGRLLDI------------------------------------------------------DE 55
Cdd:PTZ00265 1197 TAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNS 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 56 GTIEVAGYDVSSTKSKDLAKILSILRQENhFITKLTVRQLVGFGRfpyshGRLTKKDEEIISTY--IDFFgLRELENRFL 133
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYENIKFGK-----EDATREDVKRACKFaaIDEF-IESLPNKYD 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 134 -------DQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDInfAS-KYADN 205
Cdd:PTZ00265 1350 tnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI--ASiKRSDK 1427
|
.
gi 1899776741 206 I 206
Cdd:PTZ00265 1428 I 1428
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-238 |
6.48e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLLTMVGRLLDiDEGTIEVAGYDVSSTKSKDL----AKILSILRQENHFIT-KLTVRQLVGFG-RFPYSH 105
Cdd:PRK15134 317 LVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvrHRIQVVFQDPNSSLNpRLNVLQIIEEGlRVHQPT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 106 GRLTKKDEEIISTyIDFFGLR-ELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAE 184
Cdd:PRK15134 396 LSAAQREQQVIAV-MEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 185 FGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEeimhaetlsEIFNTPVQ 238
Cdd:PRK15134 475 HQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE---------RVFAAPQQ 519
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-220 |
9.52e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 9 KDYND---EVRIGpanlEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkdlakilsilrqenh 85
Cdd:cd03222 8 KRYGVfflLVELG----VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 86 fitkltvrqlvgfgrfpyshgrltkkdeeiistYIDffglrelenrfldqLSGGQRQRAYVAMVLCQETDYVLLDEPLNN 165
Cdd:cd03222 69 ---------------------------------YID--------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 166 LDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNIcAVKDGQICAFGPA 220
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI-HVFEGEPGVYGIA 155
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-224 |
1.41e-06 |
|
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: 48.79 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNdevRIGPA-----NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKI 76
Cdd:TIGR03796 478 VELRNITFGYS---PLEPPlienfSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANS 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENhFITKLTVRQLVGF--GRFPYSHGRLTKKDEEI---ISTYIDFFGLRELE---NrfldqLSGGQRQRAYVAM 148
Cdd:TIGR03796 555 VAMVDQDI-FLFEGTVRDNLTLwdPTIPDADLVRACKDAAIhdvITSRPGGYDAELAEggaN-----LSGGQRQRLEIAR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899776741 149 VLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAaaefGRTIIVVLHDINfASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:TIGR03796 629 ALVRNPSILILDEATSALDPETEKIIDDNLRRR----GCTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELW 699
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-194 |
1.43e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.75 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTL-LTMVGR-LLDIDEGTIEVAGYDVSSTKSKDLAK---ILSilrqenhF-----ITKL 90
Cdd:COG0396 20 NLTIKPGEVHAIMGPNGSGKSTLaKVLMGHpKYEVTSGSILLDGEDILELSPDERARagiFLA-------FqypveIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 91 TVRQLVgfgRFPYSHGRLTKKD----EEIISTYIDFFGL-RELENRFLDQ-LSGGQRQRAYVAMVLCQETDYVLLDEPLN 164
Cdd:COG0396 93 SVSNFL---RTALNARRGEELSarefLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190
....*....|....*....|....*....|
gi 1899776741 165 NLDIAhSVQMMQHLQRAAAEFGRTIIVVLH 194
Cdd:COG0396 170 GLDID-ALRIVAEGVNKLRSPDRGILIITH 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-206 |
1.61e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 17 IGPANLEIPAGGITALVGPNGAGKSTLLTMVGrlldidegtievagydvsstkskdlakilsilrqenhfitkltvrqLV 96
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG----------------------------------------------LA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 97 GFGRFPYSHGRLTKKdEEIISTYIDFFGLRelenrFLDQLSGGQRQRAYVAMVL----CQETDYVLLDEPLNNLDIAHSV 172
Cdd:cd03227 45 LGGAQSATRRRSGVK-AGCIVAAVSAELIF-----TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....
gi 1899776741 173 QMMQHLQRAAAEfGRTIIVVLHDINFASKYADNI 206
Cdd:cd03227 119 ALAEAILEHLVK-GAQVIVITHLPELAELADKLI 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
135-226 |
1.70e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 135 QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
90
....*....|..
gi 1899776741 215 CAFGPAEEIMHA 226
Cdd:PRK15093 238 VETAPSKELVTT 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-222 |
1.79e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKD-LAK-ILSIL--RQENHFITKLTVRQ---LVGFG 99
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANgIVYISedRKRDGLVLGMSVKEnmsLTALR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 100 RFPYSHGRLTKKDEEI-ISTYIDFFGLRELEnrfLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQM 174
Cdd:PRK10762 358 YFSRAGGSLKHADEQQaVSDFIRLFNIKTPS---MEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1899776741 175 MQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEE 222
Cdd:PRK10762 435 YQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-196 |
1.81e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.31 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKdYNDEVRIgpaNLEipaGGITALVGPNGAGKSTLL---TMV--GRLLDIDEGTIEVAGYDVSSTkSKDL--- 73
Cdd:COG0419 5 LRLENFRS-YRDTETI---DFD---DGLNLIVGPNGAGKSTILeaiRYAlyGKARSRSKLRSDLINVGSEEA-SVELefe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 74 --AKILSILRQENHFITKLT---------VRQLVGFGRFPYSHGRLTKKDEEIISTYIDFFGLRELENRFL--------- 133
Cdd:COG0419 77 hgGKRYRIERRQGEFAEFLEakpserkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILaqlsgldpi 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 134 DQLSGGQRQRAYVAMVLcqetdYVLLDepLNNLDIAHSVQMMQHLqraaaefgRTIIVVLHDI 196
Cdd:COG0419 157 ETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDAL--------EELAIITHVI 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-223 |
1.82e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGydvsstkSKDLAKILSILrqeNHFITKLTVRQLVGFgr 100
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAISSGL---NGQLTGIENIELKGL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 fpySHGRLTKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQR 180
Cdd:PRK13545 112 ---MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1899776741 181 aAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:PRK13545 189 -FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.92e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTL-LTMVGRL-LDIDEGTIEVAGYDVSSTKSKDLAK--- 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSPEDRAGegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 76 ------ILSILRQENHFITKLTV------RQLVGFGRFPYshgrltkkdEEIISTYIDFFGLRE-LENRFLDQ-LSGGQR 141
Cdd:PRK09580 81 fmafqyPVEIPGVSNQFFLQTALnavrsyRGQEPLDRFDF---------QDLMEEKIALLKMPEdLLTRSVNVgFSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1899776741 142 QRAYVAMVLCQETDYVLLDEPLNNLDIaHSVQMMQHLQRAAAEFGRTIIVVLH 194
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDI-DALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-214 |
3.15e-06 |
|
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: 47.49 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEV-----RIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSstkskdlAKI 76
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-------ADN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQenHFITKLT----VRQLVGFGRFPyshgrltkkDEEIISTYIDFFGLREL----ENRFLD-QLSGGQRQRayVA 147
Cdd:COG4615 401 REAYRQ--LFSAVFSdfhlFDRLLGLDGEA---------DPARARELLERLELDHKvsveDGRFSTtDLSQGQRKR--LA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 148 MVLC--QETDYVLLDE------PlnnldiahsV-------QMMQHLQRAaaefGRTIIVVLHDinfaSKY---ADNICAV 209
Cdd:COG4615 468 LLVAllEDRPILVFDEwaadqdP---------EfrrvfytELLPELKAR----GKTVIAISHD----DRYfdlADRVLKM 530
|
....*
gi 1899776741 210 KDGQI 214
Cdd:COG4615 531 DYGKL 535
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-206 |
3.92e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTI-------------EVAGYDVSS 67
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 68 T--------KSKDLAKILSILRQEN--HFITKLtvrqlvgfgrfpysHGRLTKKDEEII----STYIDFFGL-RELENRF 132
Cdd:PRK10636 81 LeyvidgdrEYRQLEAQLHDANERNdgHAIATI--------------HGKLDAIDAWTIrsraASLLHGLGFsNEQLERP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899776741 133 LDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQmmqhLQRAAAEFGRTIIVVLHDINFASKYADNI 206
Cdd:PRK10636 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIW----LEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-227 |
4.27e-06 |
|
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: 47.26 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEvriGPA-----NLEIPAGGITALVGPNGAGKSTLLtmvgRLL----DIDEGTIEVAGYDVSSTKSKD 72
Cdd:TIGR03797 452 IEVDRVTFRYRPD---GPLilddvSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 73 LAKILSILRQENHFITKLTVRQLVGfgrfpysHGRLTKKD----------EEIIS-------TYIDFFGlrelenrflDQ 135
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIAG-------GAPLTLDEaweaarmaglAEDIRampmgmhTVISEGG---------GT 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 136 LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefgrTIIVVLHDINfASKYADNICAVKDGQIC 215
Cdd:TIGR03797 589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV----TRIVIAHRLS-TIRNADRIYVLDAGRVV 663
|
250
....*....|..
gi 1899776741 216 AFGPAEEIMHAE 227
Cdd:TIGR03797 664 QQGTYDELMARE 675
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-229 |
4.38e-06 |
|
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: 47.63 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQENHFITKLTVRQLVGFGR 100
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 101 FpyshgrltkKDEEI-----ISTYIDFF-----GLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIaH 170
Cdd:TIGR00957 1386 Y---------SDEEVwwaleLAHLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL-E 1455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 171 SVQMMQHLQRAAAEfGRTIIVVLHDINFASKYAdNICAVKDGQICAFGPAEEIMHAETL 229
Cdd:TIGR00957 1456 TDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRGI 1512
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-196 |
5.27e-06 |
|
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: 46.39 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEvriGPANLE-----IPAGGITALVGPNGAGKSTLLTMVGRLLDIdEGTIEVAGYDVSSTKSKDLAKI 76
Cdd:cd03289 3 MTVKDLTAKYTEG---GNAVLEnisfsISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 77 LSILRQENhFITKLTVRQLVGfgrfPYSHgrltKKDEEIISTyIDFFGLRELENRFLDQ-----------LSGGQRQRAY 145
Cdd:cd03289 79 FGVIPQKV-FIFSGTFRKNLD----PYGK----WSDEEIWKV-AEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 146 VAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAefGRTIIVVLHDI 196
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRI 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-198 |
6.73e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 31 ALVGPNGAGKSTLLT-MVGRLlDIDEGTI------EVAGYDvsstkskdlaKILSILRQENhfitklTVRQLVGFGrfpy 103
Cdd:PRK11147 349 ALIGPNGCGKTTLLKlMLGQL-QADSGRIhcgtklEVAYFD----------QHRAELDPEK------TVMDNLAEG---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 104 shgrltKKDEEI------ISTYI-DFFglrelenrF--------LDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDI 168
Cdd:PRK11147 408 ------KQEVMVngrprhVLGYLqDFL--------FhpkramtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
170 180 190
....*....|....*....|....*....|
gi 1899776741 169 ahsvQMMQHLQRAAAEFGRTIIVVLHDINF 198
Cdd:PRK11147 474 ----ETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-226 |
7.68e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.55 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 16 RIGPANLEIPAG---GITALVGpngAGKSTLL-TMVGrLLDIDEGTIEVAGYDVSSTKSKD-----------------LA 74
Cdd:COG1129 267 VVRDVSFSVRAGeilGIAGLVG---AGRTELArALFG-ADPADSGEIRLDGKPVRIRSPRDairagiayvpedrkgegLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 75 KILSIlrQENhfitkLTVRQLVGFGRFpyshGRLTKKDE-EIISTYIDFFGLR----ELEnrfLDQLSGGQRQRAYVAMV 149
Cdd:COG1129 343 LDLSI--REN-----ITLASLDRLSRG----GLLDRRRErALAEEYIKRLRIKtpspEQP---VGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 150 LCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQICAFGPA-----EEIM 224
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDReeateEAIM 487
|
..
gi 1899776741 225 HA 226
Cdd:COG1129 488 AA 489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-167 |
8.13e-06 |
|
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: 46.83 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLE--IPAGGITALVGPNGAGKSTLLTMVGRLLDIdEGTIEVAGYDVSSTKSKDLAKILSI 79
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSfsVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 80 LRQENhFITKLTVRQLVGfgrfPYSHgrltKKDEEIISTyIDFFGLRELENRFLDQ-----------LSGGQRQRAYVAM 148
Cdd:TIGR01271 1297 IPQKV-FIFSGTFRKNLD----PYEQ----WSDEEIWKV-AEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLAR 1366
|
170
....*....|....*....
gi 1899776741 149 VLCQETDYVLLDEPLNNLD 167
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLD 1385
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-198 |
1.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLLTMVG-----------RLLDIDEgtiEVAGYDVSSTK---SKDLAKILsILRQENHFITK---LTVRQ 94
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAmhaidgipkncQILHVEQ---EVVGDDTTALQcvlNTDIERTQ-LLEEEAQLVAQqreLEFET 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 95 LVGFGRFPYSHG----RLTKKDEEIIS--TYIDFF-----------GLR---ELENRFLDQLSGGQRQRAYVAMVLCQET 154
Cdd:PLN03073 284 ETGKGKGANKDGvdkdAVSQRLEEIYKrlELIDAYtaearaasilaGLSftpEMQVKATKTFSGGWRMRIALARALFIEP 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1899776741 155 DYVLLDEPLNNLDIaHSVQMmqhLQRAAAEFGRTIIVVLHDINF 198
Cdd:PLN03073 364 DLLLLDEPTNHLDL-HAVLW---LETYLLKWPKTFIVVSHAREF 403
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-82 |
1.35e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 32 LVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSILRQ 82
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ 1320
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-231 |
1.49e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAK----ILSILRQENHFITKLTVRQLVGF---- 98
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmaYITESRRDNGFFPNFSIAQNMAIsrsl 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 99 --GRFPYSHGRLTKKDEEIISTyidffGLRELE-------NRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIA 169
Cdd:PRK09700 369 kdGGYKGAMGLFHEVDEQRTAE-----NQRELLalkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVG 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899776741 170 HSVQMMQhLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQIcafgpAEEIMHAETLSE 231
Cdd:PRK09700 444 AKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL-----TQILTNRDDMSE 499
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-224 |
1.54e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGyDVSstkskdLAKILSILRQENHFITKLTVRQL-VGFGRfpysh 105
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVS------VIAISAGLSGQLTGIENIEFKMLcMGFKR----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 106 grltKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAaEF 185
Cdd:PRK13546 118 ----KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQ 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 1899776741 186 GRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIM 224
Cdd:PRK13546 193 NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
135-236 |
1.78e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.90 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 135 QLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQI 214
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
90 100
....*....|....*....|....*.
gi 1899776741 215 CAFGPAEEI----MHAETLSEIFNTP 236
Cdd:COG4170 238 VESGPTEQIlkspHHPYTKALLRSMP 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-196 |
1.86e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.77 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 31 ALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSkDLAKILSILRQENHFITKLTVRQLVgfgrfpYSHGRL-- 108
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMGYCPQFDAIDDLLTGREHL------YLYARLrg 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 109 --TKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDiAHSVQMMQHLQRAAAEFG 186
Cdd:TIGR01257 2042 vpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD-PQARRMLWNTIVSIIREG 2120
|
170
....*....|
gi 1899776741 187 RTIIVVLHDI 196
Cdd:TIGR01257 2121 RAVVLTSHSM 2130
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-213 |
3.35e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 21 NLEIPAGGITALVGPNGAGKSTL---LTMV---GRLldidEGTIEvagYDVSSTKSKDL----AKILSILRQENHFITKL 90
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLmkvLSGVyphGSY----EGEIL---FDGEVCRFKDIrdseALGIVIIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 91 TVRQLVGFGRFPYSHG-----RLTKKDEEIISTyidfFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEP--- 162
Cdd:NF040905 94 SIAENIFLGNERAKRGvidwnETNRRARELLAK----VGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPtaa 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 163 LNNLDIAHSVQMMQHLQraaaEFGRTIIVVLHDINFASKYADNICAVKDGQ 213
Cdd:NF040905 170 LNEEDSAALLDLLLELK----AQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-47 |
1.16e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1899776741 2 ITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTLLTMV 47
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-44 |
1.34e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.34e-04
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-226 |
2.79e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.31 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 31 ALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVS----STKSKdlaKILSILRQENhfiTKLTVRQLVG-FGRFPYsh 105
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQ---RIRMIFQDPS---TSLNPRQRISqILDFPL-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 106 gRL------TKKDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQ 179
Cdd:PRK15112 115 -RLntdlepEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLML 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1899776741 180 RAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEIMHA 226
Cdd:PRK15112 194 ELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-51 |
3.01e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 3.01e-04
10 20 30
....*....|....*....|....*....|
gi 1899776741 22 LEIPAGGITALVGPNGAGKSTLLTMVGRLL 51
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
116-250 |
4.19e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 116 ISTYIDFfGLRELE-NRFLDQLSGGQRQRAYVAMVLCQETDYV--LLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVV 192
Cdd:PRK00635 457 LSILIDL-GLPYLTpERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLV 534
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1899776741 193 LHDINFASkYADNICAVkdgqicafGPAEEIMHAETLseiFN-TPVQIVDGPDGPLACY 250
Cdd:PRK00635 535 EHDEQMIS-LADRIIDI--------GPGAGIFGGEVL---FNgSPREFLAKSDSLTAKY 581
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-198 |
6.36e-04 |
|
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: 39.28 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 27 GGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAgydvsstkskdlakilsilrqenhfitkltvrqlvgfgrfpyshg 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 107 rltkkDEEIISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMM-----QHLQRA 181
Cdd:smart00382 37 -----DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLL 111
|
170
....*....|....*..
gi 1899776741 182 AAEFGRTIIVVLHDINF 198
Cdd:smart00382 112 KSEKNLTVILTTNDEKD 128
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-44 |
8.56e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 8.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1899776741 2 ITLNNVKkdyndevriGPANLEIP---AGGITALVGPNGAGKSTLL 44
Cdd:COG3950 6 LTIENFR---------GFEDLEIDfdnPPRLTVLVGENGSGKTTLL 42
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-227 |
1.19e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.89 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 19 PANLEIPAGGITALVGPNGAGKSTLLTMVGRLLDIDEGTIEVAGYDVSSTKSKDLAKILSIL----RQENHFITKLTVRQ 94
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcpedRKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 95 LVGFG-RFPYSHGRL---TKKDEEIISTYIDFFGLReleNRFLDQ----LSGGQRQRAYVAMVLCQETDYVLLDEPLNNL 166
Cdd:PRK11288 351 NINISaRRHHLRAGClinNRWEAENADRFIRSLNIK---TPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899776741 167 DIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQIcafgpAEEIMHAE 227
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI-----AGELAREQ 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-198 |
1.34e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 32 LVGPNGAGKSTLLTMVGrlldideGTIEVAGYDVSSTKSKDLAKilsiLRQENHFITKLTVRQLVGFGrfpysHGRLTKK 111
Cdd:PRK15064 32 LIGANGCGKSTFMKILG-------GDLEPSAGNVSLDPNERLGK----LRQDQFAFEEFTVLDTVIMG-----HTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 112 DEE---IIS----TYIDFFGLRELENRF----------------------LDQLSG-------GQRQRAYVAMVLCQETD 155
Cdd:PRK15064 96 KQErdrIYAlpemSEEDGMKVADLEVKFaemdgytaearagelllgvgipEEQHYGlmsevapGWKLRVLLAQALFSNPD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1899776741 156 YVLLDEPLNNLDIaHSVQMMQHL--QRAAaefgrTIIVVLHDINF 198
Cdd:PRK15064 176 ILLLDEPTNNLDI-NTIRWLEDVlnERNS-----TMIIISHDRHF 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-43 |
1.75e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 1.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1899776741 1 MITLNNVKKDYNDEVRIGPANLEIPAGGITALVGPNGAGKSTL 43
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTL 49
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-44 |
3.69e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 3.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1899776741 2 ITLNNVKKdYNDEvrigpanlEI-PAGGITALVGPNGAGKSTLL 44
Cdd:pfam13476 1 LTIENFRS-FRDQ--------TIdFSKGLTLITGPNGSGKTTIL 35
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-44 |
3.70e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.06 E-value: 3.70e-03
10 20
....*....|....*....|....*
gi 1899776741 21 NLEIP-AGGITALVGPNGAGKSTLL 44
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSIL 40
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
87-227 |
4.62e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 87 ITKLTVRQLVGFgrfpYSHGRLTKKDEEIiSTYIdffgLRELENR--FLDQ--------------LSGGQRQRAYVAM-- 148
Cdd:COG0178 430 LTALSIDEALEF----FENLELTEREAEI-AERI----LKEIRSRlgFLVDvgldyltldrsagtLSGGEAQRIRLATqi 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 149 ------VLcqetdYVLlDEPLNNL---DIAHSVQMMQHLQRAaaefGRTIIVVLHD---InfasKYADNIC-----A-VK 210
Cdd:COG0178 501 gsglvgVL-----YVL-DEPSIGLhqrDNDRLIETLKRLRDL----GNTVIVVEHDedtI----RAADYIIdigpgAgEH 566
|
170
....*....|....*..
gi 1899776741 211 DGQICAFGPAEEIMHAE 227
Cdd:COG0178 567 GGEVVAQGTPEEILKNP 583
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-129 |
4.90e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 29 ITALVGPNGAGKSTLL----------TMVGRLLDIDEGTIEVAGYDVSST----KSKDLAKILSILRQENHFITKLTV-R 93
Cdd:pfam13304 1 INVLIGPNGSGKSNLLealrfladfdALVIGLTDERSRNGGIGGIPSLLNgidpKEPIEFEISEFLEDGVRYRYGLDLeR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1899776741 94 QLVGFGRFPYSHGRLT------KKDEEIISTYIDFFGLRELE 129
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKrlllreDSEEREPKFPPEAEELRLGL 122
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
28-80 |
5.18e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.17 E-value: 5.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1899776741 28 GITALVGPNGAGKSTLLTMVGRLLDIDEgtIEVAGYDV-SSTKSKDLA-KILSIL 80
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVR--DSVVFVDLpSGTSPKDLLrALLRAL 58
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-223 |
5.23e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 136 LSGGQRQRAYVAMVLCQ----ETDYVLlDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFAsKYADNIC---- 207
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstgRTLYIL-DEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIEHNLDVI-KTADYIIdlgp 906
|
90
....*....|....*...
gi 1899776741 208 --AVKDGQICAFGPAEEI 223
Cdd:TIGR00630 907 egGDGGGTVVASGTPEEV 924
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
136-216 |
6.27e-03 |
|
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: 37.50 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 136 LSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHLQRAAAEfGRTIIVVLHDINFASKYADNICAVKDGQIC 215
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
.
gi 1899776741 216 A 216
Cdd:TIGR02633 483 G 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
103-223 |
6.41e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 37.41 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899776741 103 YSHGR---LTKKDEEI-ISTYIDFFGLRELENRFLDQLSGGQRQRAYVAMVLCQETDYVLLDEPLNNLDIAHSVQMMQHL 178
Cdd:NF000106 108 YMIGR*ldLSRKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1899776741 179 qRAAAEFGRTIIVVLHDINFASKYADNICAVKDGQICAFGPAEEI 223
Cdd:NF000106 188 -RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-44 |
6.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 6.53e-03
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
18-41 |
9.98e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 35.90 E-value: 9.98e-03
|
| |
