|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-252 |
6.92e-132 |
|
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: 372.45 E-value: 6.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDVV 240
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|..
gi 446325904 241 VKQDEDTGLYMV 252
Cdd:COG1120 241 VIEDPVTGRPLV 252
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-246 |
6.00e-97 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 283.90 E-value: 6.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:COG4604 2 IEIKNVSKRYGG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKnifspQ---TDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYS-----KgrlTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGV 237
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDT 235
|
....*....
gi 446325904 238 DVVVKQDED 246
Cdd:COG4604 236 DIEVEEIDG 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-256 |
5.46e-96 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 281.90 E-value: 5.46e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK11231 3 LRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDVV 240
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|....*.
gi 446325904 241 VKQDEDTGlymVPMGI 256
Cdd:PRK11231 241 IHPEPVSG---TPMCV 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-220 |
1.00e-86 |
|
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: 255.44 E-value: 1.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:cd03214 1 EVENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QqneapaditveklisfgrmpyknifspqtdedreaierALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:cd03214 80 Q--------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-255 |
4.21e-83 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 249.52 E-value: 4.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 4 KNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQ 83
Cdd:PRK10253 11 EQLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 84 NEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDE 163
Cdd:PRK10253 90 ATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 164 PTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDVVVKQ 243
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIID 249
|
250
....*....|...
gi 446325904 244 DEDTGL-YMVPMG 255
Cdd:PRK10253 250 DPVAGTpLVVPLG 262
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-248 |
8.38e-80 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 240.79 E-value: 8.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:COG4559 2 LEAENLSVRLGGRT-LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYknifSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ------ 154
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 155 NTP-MLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKA 233
Cdd:COG4559 157 GGPrWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250
....*....|....*
gi 446325904 234 IYGVDVVVKQDEDTG 248
Cdd:COG4559 236 VYGADLRVLAHPEGG 250
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-248 |
1.76e-74 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 227.35 E-value: 1.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNEAPADITVEKLI 96
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFGRMPYknifSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ------NTPMLFLDEPTTYLDI 170
Cdd:PRK13548 98 AMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 171 YYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDVVVKQDEDTG 248
Cdd:PRK13548 174 AHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADVLVQPHPETG 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-256 |
3.00e-73 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 224.28 E-value: 3.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 5 NVTFSYDNVTNR------LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLA 78
Cdd:PRK10575 9 DTTFALRNVSFRvpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGvd 238
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG-- 246
|
250
....*....|....*...
gi 446325904 239 vvvkqdedtglymVPMGI 256
Cdd:PRK10575 247 -------------IPMGI 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-241 |
1.18e-69 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 214.57 E-value: 1.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaiseyKPKEFARKLAVVH 81
Cdd:COG1121 8 ELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPAD--ITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPML 159
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMkDGEIVTKGNPNDVITEEMVKAIYGVDV 239
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYGGPV 239
|
..
gi 446325904 240 VV 241
Cdd:COG1121 240 AL 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-229 |
3.35e-64 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 199.87 E-value: 3.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:COG1122 2 ELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQneaPAD----ITVEKLISFGrmPyKNI-FSPqtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:COG1122 82 QN---PDDqlfaPTVEEDVAFG--P-ENLgLPR--EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-248 |
1.82e-63 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 203.53 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK09536 4 IDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDVV 240
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
....*...
gi 446325904 241 VKQDEDTG 248
Cdd:PRK09536 242 VGTDPATG 249
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-215 |
2.82e-61 |
|
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: 191.91 E-value: 2.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:cd03225 1 ELKNLSFSYPDGARPaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQneaPAD----ITVEKLISFGrmpYKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:cd03225 81 FQN---PDDqffgPTVEEEVAFG---LENLGLPE-EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-212 |
1.20e-60 |
|
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: 190.44 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaiseyKPKEFARKLAVVH 81
Cdd:cd03235 1 EVEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPAD--ITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMK 212
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-236 |
2.58e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 187.96 E-value: 2.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FARKLA 78
Cdd:COG3638 4 ELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrLRRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISFGRMPY----KNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:COG3638 84 MIFQQFNLVPRLSVLTNVLAGRLGRtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDViTEEMVKAI 234
Cdd:COG3638 164 EPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVLREI 242
|
..
gi 446325904 235 YG 236
Cdd:COG3638 243 YG 244
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-235 |
4.45e-56 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 179.69 E-value: 4.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FARKLA 78
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISFGRMPYKN----IFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRStwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDvITEEMVKAI 234
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEI 240
|
.
gi 446325904 235 Y 235
Cdd:cd03256 241 Y 241
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1-239 |
1.16e-55 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 178.88 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTfsydnVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSrNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:COG4138 1 LQLNDVA-----VAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMA-GLLPGQGEILLNGRPLSDWSAAELARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPyknifSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP--- 157
Cdd:COG4138 75 SQQQSPPFAMPVFQYLALHQPA-----GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtin 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 ----MLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKA 233
Cdd:COG4138 150 pegqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSE 228
|
....*.
gi 446325904 234 IYGVDV 239
Cdd:COG4138 229 VFGVKF 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
2.67e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.17 E-value: 2.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKLAVVH 81
Cdd:COG1131 2 EVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLISFgrmpYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:COG1131 80 QEPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-227 |
2.01e-50 |
|
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: 172.40 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR----LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKP---KEFA 74
Cdd:COG1123 262 EVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLAVVHQQNEA---PADiTVEKLISFgrmPYKNIFSPQTDEDREAIERALVCTNLQSK-RDKPIYALSGGERQRVWIAM 150
Cdd:COG1123 342 RRVQMVFQDPYSslnPRM-TVGDIIAE---PLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-217 |
6.81e-50 |
|
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: 163.82 E-value: 6.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLA 78
Cdd:COG1124 3 EVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPAD--ITVEKLISfgrMPYKNIFSPQTDEDreaIERALVCTNLQSK-RDKPIYALSGGERQRVWIAMTLAQN 155
Cdd:COG1124 83 MVFQDPYASLHprHTVDRILA---EPLRIHGLPDREER---IAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 156 TPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-220 |
8.23e-48 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 158.05 E-value: 8.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN---VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKP---KEFAR 75
Cdd:cd03257 3 EVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQ-----NeaPAdITVEKLIsfgRMPYKNIFSPQTDEDREAIERALVCTNLQSKR--DKPIYALSGGERQRVWI 148
Cdd:cd03257 83 EIQMVFQDpmsslN--PR-MTIGEQI---AEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-227 |
1.81e-47 |
|
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: 164.31 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTL-LSVM--SRNHAPSSGEVILDGKAISEYKPKEFARKL 77
Cdd:COG1123 6 EVRDLSVRYPGGDVPaVDGVSLTIAPGETVALVGESGSGKSTLaLALMglLPHGGRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPAD-ITVEKLISFGRMpyknIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:COG1123 86 GMVFQDPMTQLNpVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
8.04e-47 |
|
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: 155.92 E-value: 8.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:cd03295 2 EFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLIsfGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:cd03295 82 QQIGLFPHMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE---EMVKAIYGVD 238
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSpanDFVAEFVGAD 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-216 |
1.01e-46 |
|
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: 154.96 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA---- 74
Cdd:cd03255 2 ELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLAVVHQQNEAPADITVEKLISFGrMPYKNIFSPQTDED-REAIERAlvctNLQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:cd03255 82 RHIGFVFQSFNLLPDLTALENVELP-LLLAGVPKKERRERaEELLERV----GLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDiNQAIRYSDHIIVMKDGEI 216
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
1.14e-46 |
|
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: 155.53 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF---ARKL 77
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITVEKLISFGRMPYKN----IFSPQTDEDREaieRALVC---TNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsLLGRFSEEDKE---RALSAlerVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDvITEEM 230
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEV 237
|
....*.
gi 446325904 231 VKAIYG 236
Cdd:TIGR02315 238 LRHIYG 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-229 |
1.47e-46 |
|
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: 155.40 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYkPKEFARKLAVVH 81
Cdd:COG4555 3 EVENLSKKYGKVPA-LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLISFgrmpYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:COG4555 81 DERGLYDRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1-239 |
1.00e-45 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 153.16 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTfsydnVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSrNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK03695 1 MQLNDVA-----VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMA-GLLPGSGSIQFAGQPLEAWSAAELARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPyknifSPQTDEDREAIERalVCT--NLQSKRDKPIYALSGGERQRVWIAMTLAQNTP- 157
Cdd:PRK03695 75 SQQQTPPFAMPVFQYLTLHQPD-----KTRTEAVASALNE--VAEalGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 ------MLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMV 231
Cdd:PRK03695 148 inpagqLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
....*...
gi 446325904 232 KAIYGVDV 239
Cdd:PRK03695 227 AQVFGVNF 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-217 |
1.02e-45 |
|
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: 152.29 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFG----RMPYKNIfspqtdedREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGlklrGVPKAEI--------RARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-231 |
1.23e-45 |
|
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: 152.59 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LAVV 80
Cdd:cd03219 2 EVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITV-EKLI--SFGRMPYKNIFSPQTDEDREAIERALVC---TNLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:cd03219 81 FQIPRLFPELTVlENVMvaAQARTGSGLLLARARREEREARERAEELlerVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMV 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-227 |
1.88e-45 |
|
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: 152.27 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FARKLA 78
Cdd:cd03261 2 ELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISF-----GRMPYKNIfspqtdedREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplrehTRLSEEEI--------REIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.89e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY---DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA--- 74
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 -RKLAVVHQQ-----------N-EAPADItveklisfGRMPYKnifspqtdEDREAIERALVCTNLQSKRDKPIYALSGG 141
Cdd:COG1136 85 rRHIGFVFQFfnllpeltaleNvALPLLL--------AGVSRK--------ERRERARELLERVGLGDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 142 ERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDiNQAIRYSDHIIVMKDGEIV 217
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
2-217 |
1.95e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 151.83 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvtnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVH 81
Cdd:COG3840 3 RLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLISFGRMPYKNIfspqTDEDREAIERALVCTNLQSKRD-KPiYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGLKL----TAEQRAQVEQALERVGLAGLLDrLP-GQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-245 |
5.55e-45 |
|
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: 151.39 E-value: 5.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVI------LDGKAISEYKpkefaR 75
Cdd:COG1119 5 ELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELR-----K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVV--HQQNEAPADITVEKLI------SFGRmpYKNIfspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVW 147
Cdd:COG1119 79 RIGLVspALQLRFPRDETVLDVVlsgffdSIGL--YREP----TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
250
....*....|....*...
gi 446325904 228 EEMVKAIYGVDVVVKQDE 245
Cdd:COG1119 233 SENLSEAFGLPVEVERRD 250
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-225 |
2.01e-44 |
|
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: 149.25 E-value: 2.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR-----NHAPSSGEVILDGKAISE--YKPKEF 73
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 ARKLAVVHQQnEAPADITVEKLISFG----RMPYKNIFSpqtDEDREAIERALVCTNLqsKRDKPIYALSGGERQRVWIA 149
Cdd:cd03260 80 RRRVGMVFQK-PNPFPGSIYDNVAYGlrlhGIKLKEELD---ERVEEALRKAALWDEV--KDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYglTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-215 |
3.46e-44 |
|
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: 146.95 E-value: 3.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIS--EYKPKEFARKLA 78
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQneapaditveklisFGRMPYKNIfspqtdedreaieralvctnlqskRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:cd03229 80 MVFQD--------------FALFPHLTV------------------------LENIALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-233 |
4.37e-44 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 148.59 E-value: 4.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA---RKLA 78
Cdd:COG1127 7 EVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNeapA---DITVEK-----LISFGRMPYKNIfspqtdedREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:COG1127 86 MLFQGG---AlfdSLTVFEnvafpLREHTDLSEAEI--------RELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI--TE 228
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDD 234
|
....*
gi 446325904 229 EMVKA 233
Cdd:COG1127 235 PWVRQ 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-239 |
5.21e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 149.50 E-value: 5.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDG-KAISEYKPKEFARKLAV 79
Cdd:TIGR04520 2 EVENVSFSYPESEKPaLKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQqNeaPAD----ITVEKLISFG----RMPYKNIfspqtdedREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:TIGR04520 82 VFQ-N--PDNqfvgATVEDDVAFGlenlGVPREEM--------RKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 152 LAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVIT-EEM 230
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSqVEL 229
|
....*....
gi 446325904 231 VKAIyGVDV 239
Cdd:TIGR04520 230 LKEI-GLDV 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-215 |
8.47e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.47 E-value: 8.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QqneapaditveklisfgrmpyknifspqtdedreaieralvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-216 |
2.35e-43 |
|
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: 144.85 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKLAVVH 81
Cdd:cd03230 2 EVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKlisfgrmpyknifspqtdedreaieralvctNLQskrdkpiyaLSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:cd03230 80 EEPSLYENLTVRE-------------------------------NLK---------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-216 |
5.80e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.96 E-value: 5.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:COG4619 2 ELEGLSFRVGG-KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADiTVEKLISFgrmPYKniFSPQTDeDREAIERALVCTNLQ-SKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:COG4619 81 QEPALWGG-TVRDNLPF---PFQ--LRERKF-DRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-253 |
5.82e-43 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 146.90 E-value: 5.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--------RNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNEAPA 88
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggaPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 89 DITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP---------ML 159
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpprYL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDV 239
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGFAV 256
|
250
....*....|....*
gi 446325904 240 -VVKQDEDTGLYMVP 253
Cdd:PRK13547 257 rLVDAGDGVPPVIVP 271
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.96e-42 |
|
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: 151.83 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:COG4988 338 ELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADiTVEKLISFGRmpyknifspqTDEDREAIERAL-------VCTNLQSKRDKPI----YALSGGERQRVWIAM 150
Cdd:COG4988 418 QNPYLFAG-TIRENLRLGR----------PDASDEELEAALeaagldeFVAALPDGLDTPLgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDInQAIRYSDHIIVMKDGEIVTKGNP 222
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTH 555
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-215 |
5.13e-42 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 141.37 E-value: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKPvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQneapaditveklisfgrmPYknIFSpqtdedreaierALVCTNLqskrdkpiyaLSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03228 81 VPQD------------------PF--LFS------------GTIRENI----------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGE 215
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-211 |
6.53e-41 |
|
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: 139.91 E-value: 6.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkefarKL 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQneaPADI---TVEKLISFG----RMPYKnifspqtdEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:cd03293 76 GYVFQQ---DALLpwlTVLDNVALGlelqGVPKA--------EARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 151 TLAQNTPMLFLDEPTTYLDI----YYQIEILELVKElnevYGLTIVMVLHDINQAIRYSDHIIVM 211
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE----TGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-235 |
8.80e-41 |
|
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: 140.56 E-value: 8.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LAVV 80
Cdd:COG0411 6 EVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEK------LISFGRMPYKNIFSP--QTDEDREAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIA 149
Cdd:COG0411 85 FQNPRLFPELTVLEnvlvaaHARLGRGLLAALLRLprARREEREARERAeelLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADP 244
|
....*.
gi 446325904 230 MVKAIY 235
Cdd:COG0411 245 RVIEAY 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-217 |
9.59e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 140.61 E-value: 9.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkefarKLA 78
Cdd:COG1116 9 ELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----DRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQneaPADI---TVEKLISFG----RMPyknifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:COG1116 84 VVFQE---PALLpwlTVLDNVALGlelrGVP--------KAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 152 LAQNTPMLFLDEPTTYLD----IYYQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKD--GEIV 217
Cdd:COG1116 153 LANDPEVLLMDEPFGALDaltrERLQDELLRLWQET----GKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
4.60e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 139.60 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIsEYKPK---EFARKL 77
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPA-DITVEKLISFGRMpykNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK13636 85 GMVFQDPDNQLfSASVYQDVSFGAV---NLKLPE-DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE-EMVKAI 234
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEkEMLRKV 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.38e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.29 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeYKPK---EFARKL 77
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQ----QNEAPadiTVEKLISFGRMpykNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:PRK13639 81 GIVFQnpddQLFAP---TVEEDVAFGPL---NLGLSK-EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-225 |
2.02e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVH 81
Cdd:COG3842 7 ELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 qQNEA--PaDITVEKLISFG----RMPyknifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQN 155
Cdd:COG3842 84 -QDYAlfP-HLTVAENVAFGlrmrGVP--------KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 156 TPMLFLDEPTTYLD----IYYQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:COG3842 154 PRVLLLDEPLSALDaklrEEMREELRRLQREL----GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-225 |
4.92e-39 |
|
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: 135.44 E-value: 4.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVH 81
Cdd:cd03300 2 ELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLISFG-RMPYKNIfspqtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:cd03300 79 QNYALFPHLTVFENIAFGlRLKKLPK-----AEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 161 LDEPTTYLDI----YYQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:cd03300 154 LDEPLGALDLklrkDMQLELKRLQKEL----GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
2.04e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 135.25 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQneaPAD----ITVEKLISFGrmPYKNIFSPqtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK13647 85 FQD---PDDqvfsSTVWDDVAFG--PVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKA 233
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-211 |
2.14e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 132.74 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGkaiseykpkefARKLAVVHQQNEAPAD--ITVEK 94
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSlpLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 95 LISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQI 174
Cdd:NF040873 77 LVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 446325904 175 EILELVKELNEVyGLTIVMVLHDINqAIRYSDHIIVM 211
Cdd:NF040873 157 RIIALLAEEHAR-GATVVVVTHDLE-LVRRADPCVLL 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-220 |
3.33e-38 |
|
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: 132.62 E-value: 3.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLksvSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNIfspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
3.90e-38 |
|
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: 141.12 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:COG2274 475 ELENVSFRYPGDSPPvLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEapadI---TVEKLISFGRmpyknifsPQTDEDR--EAIERA----LVCtNLQSKRDKPIY----ALSGGERQRVW 147
Cdd:COG2274 555 LQDVF----LfsgTIRENITLGD--------PDATDEEiiEAARLAglhdFIE-ALPMGYDTVVGeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDInQAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-217 |
1.49e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.33 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA---RKLA 78
Cdd:COG2884 3 RFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQqneapaDItveKLIsFGRMPYKNI--------FSPqtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:COG2884 83 VVFQ------DF---RLL-PDRTVYENValplrvtgKSR--KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-217 |
1.54e-37 |
|
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: 130.84 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIseyKPKEFARKLAVVH 81
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQneaPADI----TVEKLISFGrmpyknifSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:cd03226 78 QD---VDYQlftdSVREELLLG--------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-226 |
7.52e-37 |
|
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: 130.01 E-value: 7.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FAR 75
Cdd:cd03258 3 ELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQNEAPADITVEKLISFgrmPYKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQN 155
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVAL---PLEIAGVPK-AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 156 TPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-228 |
1.63e-36 |
|
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: 130.07 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF----ARKLAVVHQqneapaditv 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQ---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 93 ekliSFGRMPYKNIFSPQT----------DEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLD 162
Cdd:cd03294 110 ----SFALLPHRTVLENVAfglevqgvprAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 163 EPTTYLD----IYYQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:cd03294 186 EAFSALDplirREMQDELLRLQAEL----QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-226 |
2.73e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 128.61 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVHQQNEAPADITVEKLI 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFGrMPYKNIFSPQTDEDREAIERALVCTNLQSKrdKPIyALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEI 176
Cdd:cd03299 93 AYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNR--KPE-TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446325904 177 LELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-225 |
2.60e-35 |
|
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: 125.62 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LAVV 80
Cdd:cd03224 2 EVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNifspqtDEDREAIERAL-VCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVYeLFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-220 |
3.23e-35 |
|
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: 123.96 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKpKEFARKLAV 79
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQneapaditveklisfgrmPYknIFSpqtdedreaieralvcTNLQSKRDKPiyaLSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03247 80 LNQR------------------PY--LFD----------------TTLRNNLGRR---FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDInQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-226 |
4.49e-35 |
|
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: 125.42 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:cd03253 2 EFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQ----NEapadiTVEKLISFGRMpyknifsPQTDED-REAIERALVCTNLQSKRDKpiYA---------LSGGERQRVW 147
Cdd:cd03253 82 QDtvlfND-----TIGYNIRYGRP-------DATDEEvIEAAKAAQIHDKIMRFPDG--YDtivgerglkLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLS-TIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-239 |
4.79e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.36 E-value: 4.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-----LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPK-EFA 74
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLAVVHQQ--NEAPADItVEKLISFGRmpyKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTL 152
Cdd:PRK13633 85 NKAGMVFQNpdNQIVATI-VEEDVAFGP---ENLGIPP-EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 153 AQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVITE-EMV 231
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvEMM 238
|
....*...
gi 446325904 232 KAIyGVDV 239
Cdd:PRK13633 239 KKI-GLDV 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
5.71e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 5.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQneaPAD----ITVEKLISFGrmpYKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQN 155
Cdd:PRK13635 86 VFQN---PDNqfvgATVQDDVAFG---LENIGVPR-EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 156 TPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVITE-EMVKAI 234
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSgHMLQEI 237
|
....*
gi 446325904 235 yGVDV 239
Cdd:PRK13635 238 -GLDV 241
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
2-228 |
7.14e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 126.74 E-value: 7.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNeapaditveklisfGRMP----YKNI-FSPQ-TDEDREAI-ERA-----LVctNLqskrDKPIYA------LSGGER 143
Cdd:COG1125 83 QQI--------------GLFPhmtvAENIaTVPRlLGWDKERIrARVdelleLV--GL----DPEEYRdrypheLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 144 QRVWIAMTLAQNTPMLFLDEPTTYLD------IyyQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:COG1125 143 QRVGVARALAADPPILLMDEPFGALDpitreqL--QDELLRLQREL----GKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
250
....*....|.
gi 446325904 218 TKGNPNDVITE 228
Cdd:COG1125 217 QYDTPEEILAN 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-166 |
8.28e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.99 E-value: 8.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNEAPADITVEKLI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 97 SFGRmpykNIFSPQTDEDREAIERALVCTNLQSKRDKPI----YALSGGERQRVWIAMTLAQNTPMLFLDEPTT 166
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
1.09e-34 |
|
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: 130.66 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN-VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:COG4987 335 ELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQneapADI---TVEKLISFGRmpyknifsPQ-TDED-REAIERA----LVCTnLQSKRDKPIY----ALSGGERQRVW 147
Cdd:COG4987 415 PQR----PHLfdtTLRENLRLAR--------PDaTDEElWAALERVglgdWLAA-LPDGLDTWLGeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDInQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLA 558
|
..
gi 446325904 228 EE 229
Cdd:COG4987 559 QN 560
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-226 |
1.21e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.67 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:COG1132 341 EFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QqneapaDI-----TVEKLISFGRMPYknifspqTDED-REAIERALVCTNLQSKRDK---PI----YALSGGERQRVWI 148
Cdd:COG1132 421 Q------DTflfsgTIRENIRYGRPDA-------TDEEvEEAAKAAQAHEFIEALPDGydtVVgergVNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-226 |
1.32e-34 |
|
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: 124.27 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN-VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:cd03251 2 EFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 hQQNEAPADITVEKLISFGRmpyknifspqTDEDREAIERAL-------VCTNLQSKRDKPI----YALSGGERQRVWIA 149
Cdd:cd03251 82 -SQDVFLFNDTVAENIAYGR----------PGATREEVEEAAraanaheFIMELPEGYDTVIgergVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-216 |
2.45e-34 |
|
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: 122.90 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA---RKL 77
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITVEKLISFG-RMPYKnifSPQtdEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlEVTGV---PPR--EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-239 |
3.66e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.95 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN-VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK13632 9 KVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQneaPAD----ITVEKLISFGrMPYKNIfSPQtdEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK13632 89 FQN---PDNqfigATVEDDIAFG-LENKKV-PPK--KMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVITEEMVKAIYG 236
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEKAK 240
|
...
gi 446325904 237 VDV 239
Cdd:PRK13632 241 IDS 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
4.13e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.36 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEI--KNVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIS-EYKPKEF 73
Cdd:PRK13634 1 MDItfQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 A---RKLAVV-----HQQNEApadiTVEKLISFGRMpykNIFSPQTDEDREAIER-ALVCTNlQSKRDKPIYALSGGERQ 144
Cdd:PRK13634 81 KplrKKVGIVfqfpeHQLFEE----TVEKDICFGPM---NFGVSEEDAKQKAREMiELVGLP-EELLARSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 145 RVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPND 224
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
250
....*....|....*..
gi 446325904 225 VI--TEEMVKaiYGVDV 239
Cdd:PRK13634 233 IFadPDELEA--IGLDL 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-249 |
4.87e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 126.10 E-value: 4.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkeFARKLAVV 80
Cdd:PRK11607 20 LEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFG----RMPyknifspqTDEDREAIERALVCTNLQ--SKRdKPiYALSGGERQRVWIAMTLAQ 154
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGlkqdKLP--------KAEIASRVNEMLGLVHMQefAKR-KP-HQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEI-LELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV-------I 226
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIyehpttrY 245
|
250 260
....*....|....*....|...
gi 446325904 227 TEEMVKAIYGVDVVVKQDEDTGL 249
Cdd:PRK11607 246 SAEFIGSVNVFEGVLKERQEDGL 268
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-228 |
6.04e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.00 E-value: 6.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPK--EFA 74
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLAVVHQQNEAPA-DITVEKLISFGrmPYKNIFSPQTDEDR--EAIEraLVCTNLQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:PRK13637 83 KKVGLVFQYPEYQLfEETIEKDIAFG--PINLGLSEEEIENRvkRAMN--IVGLDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 152 LAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-224 |
6.77e-34 |
|
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: 121.71 E-value: 6.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKLAVV 80
Cdd:cd03265 1 IEVENLVKKYGDFE-AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADIT-VEKLISFGRmpyknIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03265 79 FQDLSVDDELTgWENLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPND 224
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
7.13e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.32 E-value: 7.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTN-RLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAP-ADITVEKLISFGrmpYKNiFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK13648 88 VFQNPDNQfVGSIVKYDVAFG---LEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-235 |
1.68e-33 |
|
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: 121.24 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LAVV 80
Cdd:COG0410 5 EVENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVE---KLISFGRmpyknifsPQTDEDREAIERalVCT---NLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:COG0410 84 PEGRRIFPSLTVEenlLLGAYAR--------RDRAEVRADLER--VYElfpRLKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAI 234
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREA 232
|
.
gi 446325904 235 Y 235
Cdd:COG0410 233 Y 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-222 |
1.89e-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: 120.69 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeYKPKEFARKLAV 79
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADITV-EKLISFGRMpyKNIfsPQTDEDREaIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:cd03263 80 CPQFDALFDELTVrEHLRFYARL--KGL--PKSEIKEE-VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNP 222
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-229 |
2.58e-33 |
|
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: 120.72 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03249 2 EFKNVSFRYPSRPDVpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQneaPA--DITVEKLISFGRmpykniFSPQTDEDREAIERAL---VCTNLQSKRDKPIYA----LSGGERQRVWIAM 150
Cdd:cd03249 82 VSQE---PVlfDGTIAENIRYGK------PDATDEEVEEAAKKANihdFIMSLPDGYDTLVGErgsqLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 151 TLAQNTPMLFLDEPTTYLDiyYQIEilELVKE-LNEVY-GLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:cd03249 153 ALLRNPKILLLDEATSALD--AESE--KLVQEaLDRAMkGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
.
gi 446325904 229 E 229
Cdd:cd03249 228 K 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-225 |
3.19e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.26 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVH 81
Cdd:COG3839 5 ELENVSKSYGGVEA-LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQneaPA---DITVEKLISFG----RMPyknifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:COG3839 82 QS---YAlypHMTVYENIAFPlklrKVP--------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 155 NTPMLFLDEPTTYLDiyYQ------IEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:COG3839 151 EPKVFLLDEPLSNLD--AKlrvemrAEIKRLHRRL----GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
3.30e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.91 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNH-----APSSGEVILDGKAIseYKPK---- 71
Cdd:COG1117 12 IEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDI--YDPDvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 72 EFARKLAVVHQQ-NEAPADItveklisfgrmpYKNI-FSPQTDEDR------EAIERAL--------VCTNLqskrDKPI 135
Cdd:COG1117 89 ELRRRVGMVFQKpNPFPKSI------------YDNVaYGLRLHGIKskseldEIVEESLrkaalwdeVKDRL----KKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 136 YALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIY--YQIEilELVKELNEVYglTIVMVLHDINQAIRYSDHIIVMKD 213
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIstAKIE--ELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYL 228
|
250 260 270
....*....|....*....|....*....|
gi 446325904 214 GEIV----TK---GNPNDVITEEMVKAIYG 236
Cdd:COG1117 229 GELVefgpTEqifTNPKDKRTEDYITGRFG 258
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-227 |
8.47e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.33 E-value: 8.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAI--SEYKPKEFARKLAV 79
Cdd:COG1126 3 EIENLHKSFGDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQ-----------N--EAPadITVEKlisfgrMPYKnifspqtdedrEAIERAL-----VctNLQSKRDKPIYALSGG 141
Cdd:COG1126 82 VFQQfnlfphltvleNvtLAP--IKVKK------MSKA-----------EAEERAMellerV--GLADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 142 ERQRVWIAMTLAQNtP--MLFlDEPTTYLDiyyqiEILELVKEL-NEvyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT 218
Cdd:COG1126 141 QQQRVAIARALAME-PkvMLF-DEPTSALDpelvgEVLDVMRDLaKE--GMTMVVVTHEMGFAREVADRVVFMDGGRIVE 216
|
....*....
gi 446325904 219 KGNPNDVIT 227
Cdd:COG1126 217 EGPPEEFFE 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-226 |
9.31e-33 |
|
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: 125.21 E-value: 9.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADiTVEKLISFGRMpyknifspqTDEDREAIERALVCTNLQSKRDK-------PI----YALSGGERQRVWI 148
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRT---------EQADRAEIERALAAAYAQDFVDKlplgldtPIgengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
10-201 |
1.06e-32 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 117.91 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 10 YDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIsEYKPK---EFARKLAVVHQQnea 86
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKgllERRQRVGLVFQD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 87 PAD----ITVEKLISFGRMpykNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLD 162
Cdd:TIGR01166 77 PDDqlfaADVDQDVAFGPL---NLGLSE-AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 446325904 163 EPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQA 201
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-216 |
1.76e-32 |
|
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: 118.02 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN--VtnrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPK--EFARKL 77
Cdd:cd03262 2 EIKNLHKSFGDfhV---LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITVEKLISFGRMPYKNIfspqtdEDREAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKVKGM------SKAEAEERAlelLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
2-215 |
2.86e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 117.35 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA---RKLA 78
Cdd:TIGR02673 3 EFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVeklisfgrmpYKNIFSP------QTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTL 152
Cdd:TIGR02673 83 VVFQDFRLLPDRTV----------YENVALPlevrgkKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 153 AQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-225 |
2.98e-32 |
|
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: 118.21 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNrLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:cd03296 3 IEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-220 |
4.22e-32 |
|
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: 116.91 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGkITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYkPKEFARKLAVVH 81
Cdd:cd03264 2 QLENLTKRYGK-KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLISF-GRMpyKNIfsPQTDEDREaIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:cd03264 79 QEFGVYPNFTVREFLDYiAWL--KGI--PSKEVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
3-197 |
5.71e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 116.56 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGK---AISEYKPKEFAR-KLA 78
Cdd:TIGR03608 1 LKNISKKFGDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFRReKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISFGrMPYKNIfspQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLG-LKYKKL---SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHD 197
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVTHD 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
6.50e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 122.40 E-value: 6.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:TIGR02857 323 EFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADiTVEKLISFGRmPYknifspQTDED-REAIERALVCTNLQSKR---DKPI----YALSGGERQRVWIAMTLA 153
Cdd:TIGR02857 403 QHPFLFAG-TIAENIRLAR-PD------ASDAEiREALERAGLDEFVAALPqglDTPIgeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYsDHIIVM 211
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-217 |
7.01e-32 |
|
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: 116.59 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFG----RMPYKNIfspqtDEDREAIERALVCTNLQSKRDKpiyALSGGERQRVWIAMTLAQNT 156
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGlklrKVPKDEI-----DERVREVAELLQIEHLLDRKPK---QLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
9.18e-32 |
|
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: 114.45 E-value: 9.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKL--AV 79
Cdd:cd03216 2 ELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAgiAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQqneapaditveklisfgrmpyknifspqtdedreaieralvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-237 |
1.03e-31 |
|
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: 116.49 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 23 EIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAiseykPKEFARKLAVVHQQNEAPAD--ITVEKLISFGR 100
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAWDfpISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 101 MPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELV 180
Cdd:TIGR03771 77 TGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 181 KELNEVyGLTIVMVLHDINQAIRYSDHIIVMkDGEIVTKGNPNDVITEEMVKAIYGV 237
Cdd:TIGR03771 157 IELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-229 |
2.61e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 121.09 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADITVEKLIsfgrmpyknIFSPQTDEdrEAIERALVCTNLQS--KRDKPIYA--------LSGGERQRVWIA 149
Cdd:PRK11160 419 VSQRVHLFSATLRDNLL---------LAAPNASD--EALIEVLQQVGLEKllEDDKGLNAwlgeggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-216 |
3.06e-31 |
|
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: 115.26 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN--VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03248 13 KFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADiTVEKLISFGrmpyknIFSPQTDEDREAIERALVCTNLQSKRDKPIYA-------LSGGERQRVWIAMTL 152
Cdd:cd03248 93 VGQEPVLFAR-SLQDNIAYG------LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 153 AQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYglTIVMVLHDINqAIRYSDHIIVMKDGEI 216
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-226 |
6.22e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 114.24 E-value: 6.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADiTVEKLISFGRmpyknifSPQTDEDREAIERALVCTNLQSKRDKPIYA--------LSGGERQRVWIAMTLA 153
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGR-------PNATDEEVIEAAKEAGAHDFIMKLPNGYDTvlgenggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1-216 |
7.72e-31 |
|
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: 113.80 E-value: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLksvSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEF---DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRMPYKNIfspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:TIGR01277 76 FQENNLFAHLTVRQNIGLGLHPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:TIGR01277 152 LDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
9.58e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 9.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLA 78
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAP-ADITVEKLISFGR----MPYKnifspqtdEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:PRK13650 85 MVFQNPDNQfVGATVEDDVAFGLenkgIPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQaIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-216 |
1.01e-30 |
|
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: 112.31 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTN-RLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEklisfgrmpykNIfspqtdedreaieralvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPMLF 160
Cdd:cd03246 82 PQDDELFSGSIAE-----------NI-------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNeVYGLTIVMVLHDINqAIRYSDHIIVMKDGEI 216
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-228 |
1.41e-30 |
|
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: 115.54 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLK---SVSSEIEIGKITTIIGPNGCGKSTL-LSVMsRNHAP---SSGEVILDGKAISEYKPKEF- 73
Cdd:COG0444 3 EVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLaRAIL-GLLPPpgiTSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 ---ARKLAVVHQqneAPA----------DITVEKLISFGRMPYKnifspqtdEDREAIERALVCTNLQSKRDkpiYA--- 137
Cdd:COG0444 82 kirGREIQMIFQ---DPMtslnpvmtvgDQIAEPLRIHGGLSKA--------EARERAIELLERVGLPDPER---RLdry 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 ---LSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDG 214
Cdd:COG0444 148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAG 227
|
250
....*....|....
gi 446325904 215 EIVTKGNPNDVITE 228
Cdd:COG0444 228 RIVEEGPVEELFEN 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
1.79e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.85 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR-----NHAPSSGEVILDGKAISEYKPKEFAR 75
Cdd:PRK14247 4 IEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDR--EAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERvrWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-214 |
2.16e-30 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 112.94 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFarklaVVHQQNEAPADITVEKLI 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFG---RMPYKNifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQ 173
Cdd:TIGR01184 76 ALAvdrVLPDLS-----KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446325904 174 IEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDG 214
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-223 |
2.44e-30 |
|
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: 114.79 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKLAVVHQQNEAPADIT-VEKL 95
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDLTgRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFGRMpykniFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIE 175
Cdd:TIGR01188 88 EMMGRL-----YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446325904 176 ILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPN 223
Cdd:TIGR01188 163 IWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
3.13e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.26 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNV--TFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK 76
Cdd:COG1101 2 LELKNLskTFNPGTVNEKraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 LAVVHQ---QNEAPaDITVEK--LISFGRMPYKNIFSPQTDEDREAIeRALVCT---NLQSKRDKPIYALSGGERQRVWI 148
Cdd:COG1101 82 IGRVFQdpmMGTAP-SMTIEEnlALAYRRGKRRGLRRGLTKKRRELF-RELLATlglGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-229 |
3.66e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.81 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKefARKLAVVH 81
Cdd:PRK09452 16 ELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADITVEKLISFG-RM---PyknifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGlRMqktP--------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 158 MLFLDEPTTYLDiyY------QIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDvITEE 229
Cdd:PRK09452 165 VLLLDESLSALD--YklrkqmQNELKALQRKL----GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE-IYEE 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
4.24e-30 |
|
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: 111.42 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvtnR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKLA 78
Cdd:COG4133 3 LEAENLSCRRGE---RllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISFGRMPYKnifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYG------LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHD 197
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQ 190
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-217 |
4.44e-30 |
|
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: 112.06 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 4 KNVTFSY---DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA----RK 76
Cdd:TIGR02211 5 ENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 LAVVHQQNEAPADITVEKLISfgrMPYknIFSPQTDEdrEAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVA---MPL--LIGKKSVK--EAKERAyemLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDInQAIRYSDHIIVMKDGEIV 217
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQLF 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-220 |
4.67e-30 |
|
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: 111.98 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS---RNHAPSSGEVILDGKAIseyKPKEFARKLAVVHQQNEAPADITVE 93
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLISFG---RMPYKniFSPQTDEDREAIERALVCtNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDI 170
Cdd:cd03234 100 ETLTYTailRLPRK--SSDAIRKKRVEDVLLRDL-ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446325904 171 YYQIEILELVKELNEvYGLTIVMVLH----DInqaIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03234 177 FTALNLVSTLSQLAR-RNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-239 |
7.23e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.02 E-value: 7.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FAR 75
Cdd:COG1135 3 ELENLSKTFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQ-NeapaditvekLISfGRMPYKNIFSP--QTDEDREAIER------ALVctNLQSKRDKpiY--ALSGGERQ 144
Cdd:COG1135 83 KIGMIFQHfN----------LLS-SRTVAENVALPleIAGVPKAEIRKrvaellELV--GLSDKADA--YpsQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 145 RVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDIN--QAIrySDHIIVMKDGEIVTKG-- 220
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvvRRI--CDRVAVLENGRIVEQGpv 225
|
250 260
....*....|....*....|....
gi 446325904 221 -----NPNDVITEEMVKAIYGVDV 239
Cdd:COG1135 226 ldvfaNPQSELTRRFLPTVLNDEL 249
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
8.59e-30 |
|
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: 111.14 E-value: 8.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNV-TNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:cd03245 4 EFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQqneapaDITvekLIsFGRMpYKNI--FSPQTDEDR--EAIERALVcTNLQSKR----DKPI----YALSGGERQRVWI 148
Cdd:cd03245 84 PQ------DVT---LF-YGTL-RDNItlGAPLADDERilRAAELAGV-TDFVNKHpnglDLQIgergRGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHdinqaiRYS-----DHIIVMKDGEIVTKG 220
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITH------RPSlldlvDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-228 |
9.08e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.53 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAI-SEYKPKEFA- 74
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 --RKLAVVHQQNEAPA-DITVEKLISFGrmpyknifsPQ----TDEDREAIER---ALVCTNlQSKRDKPIYALSGGERQ 144
Cdd:PRK13649 83 irKKVGLVFQFPESQLfEETVLKDVAFG---------PQnfgvSQEEAEALAReklALVGIS-ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 145 RVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPND 224
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
....
gi 446325904 225 VITE 228
Cdd:PRK13649 232 IFQD 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-236 |
9.47e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 9.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKL--AV 79
Cdd:COG1129 6 EMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQ-NEAPaDITVEKLISFGRMPYKNIFspqTDeDREAIERAL-VCTNLQSKRD--KPIYALSGGERQRVWIAMTLAQN 155
Cdd:COG1129 84 IHQElNLVP-NLSVAENIFLGREPRRGGL---ID-WRAMRRRAReLLARLGLDIDpdTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 156 TPMLFLDEPTTYLDIyYQIEIL-ELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAI 234
Cdd:COG1129 159 ARVLILDEPTASLTE-REVERLfRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
|
..
gi 446325904 235 YG 236
Cdd:COG1129 237 VG 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.43 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQneaPAD----ITVEKLISFGrmPYKNIFSPQTDEDReaIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK13652 84 FQN---PDDqifsPTVEQDIAFG--PINLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.13e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 111.72 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVIL------DGKAISEY-- 68
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 69 ----------------KPKEFARKLAVVHQQNEAPA-DITVEKLISFGRMPYKniFSPQtdedrEAIERALVCTNL---- 127
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQFAEYQLfEQTIEKDIIFGPVSMG--VSKE-----EAKKRAAKYIELvgld 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 128 QSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDH 207
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKR 234
|
250 260
....*....|....*....|..
gi 446325904 208 IIVMKDGEIVTKGNPNDVITEE 229
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDILSDN 256
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-221 |
3.65e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.59 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:TIGR00958 480 EFQDVSFSYPNRPDVpvLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNeapaditveklISFGRMPYKNI---FSPQTDEDREAIERALVCTNLQSKRDKPIYA--------LSGGERQRVWI 148
Cdd:TIGR00958 560 VGQEP-----------VLFSGSVRENIaygLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAI 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDiyyqIEILELVKELNEVYGLTIVMVLHDInQAIRYSDHIIVMKDGEIVTKGN 221
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGT 696
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-228 |
8.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADI--TVEKLISFGRmpyKNIFSPQTdEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK13644 82 VFQNPETQFVgrTVEEDLAFGP---ENLCLPPI-EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQaIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-239 |
1.16e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.05 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FAR 75
Cdd:PRK11153 3 ELKNISKVFPQGGRTihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQ-NeapaditvekLISfGRMPYKNIFSPQT--DEDREAIER------ALVctNLQSKRDKPIYALSGGERQRV 146
Cdd:PRK11153 83 QIGMIFQHfN----------LLS-SRTVFDNVALPLElaGTPKAEIKArvtellELV--GLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 147 WIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG------ 220
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGtvsevf 229
|
250 260
....*....|....*....|
gi 446325904 221 -NPNDVITEEMVKAIYGVDV 239
Cdd:PRK11153 230 sHPKHPLTREFIQSTLHLDL 249
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-227 |
1.41e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 5 NVTFSYDNVTNRLksvSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVHQQN 84
Cdd:PRK10771 6 DITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 85 EAPADITVEKLISFGRMPYKNIFSPQTDEdREAIERALVCTNLQSKRDKpiyALSGGERQRVWIAMTLAQNTPMLFLDEP 164
Cdd:PRK10771 81 NLFSHLTVAQNIGLGLNPGLKLNAAQREK-LHAIARQMGIEDLLARLPG---QLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 165 TTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-227 |
1.65e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE--FARKLAV 79
Cdd:PRK09493 3 EFKNVSKHFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADITVEKLISFGRMPYKNifspQTDEDREAIERALVC-TNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRG----ASKEEAEKQARELLAkVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-226 |
2.23e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 112.80 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADiTVEKLISFGRmpyKNIFSpqtdedREAIERAL---VCTNLQSKRDKPI--------YALSGGERQRVWI 148
Cdd:PRK11176 422 VSQNVHLFND-TIANNIAYAR---TEQYS------REQIEEAArmaYAMDFINKMDNGLdtvigengVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-228 |
2.48e-28 |
|
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: 109.89 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 32 IIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVHQQNEAPADITVEKLISFG-RMpyknifspq 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGlKM--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 111 TDEDREAI-ER---ALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEV 186
Cdd:TIGR01187 70 RKVPRAEIkPRvleALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446325904 187 YGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-235 |
6.62e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 106.47 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARkLAVVHQQNEAPA--DITVEK 94
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-LGIGYLPQEASIfrKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 95 LISFgrmpyknIFSPQTDEDREAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIY 171
Cdd:cd03218 95 NILA-------VLEIRGLSKKEREEKLeelLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 172 YQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIY 235
Cdd:cd03218 168 AVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-217 |
1.12e-27 |
|
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: 106.81 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKP---KEFARKLAVVHQqnEAPADI--- 90
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrRAFRRDVQLVFQ--DSPSAVnpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 -TVEKLIsfgRMPYKNIFSPQTDEDREAIERALVCTNLQSK-RDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYL 168
Cdd:TIGR02769 105 mTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446325904 169 DIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-239 |
1.95e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVT--NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLA 78
Cdd:PRK13642 5 LEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAP-ADITVEKLISFGrmpYKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDVAFG---MENQGIPR-EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVI--TEEMVKAiy 235
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFatSEDMVEI-- 237
|
....
gi 446325904 236 GVDV 239
Cdd:PRK13642 238 GLDV 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-226 |
2.02e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.05 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVH 81
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QqnEAPA-DITVEKLISFGRmpyknifSPQTDED-REAIERALVCTNLQSKRDKpiY---------ALSGGERQRVWIAM 150
Cdd:PRK13657 416 Q--DAGLfNRSIEDNIRVGR-------PDATDEEmRAAAERAQAHDFIERKPDG--YdtvvgergrQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDELV 557
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-225 |
2.93e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.15 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMsrnhA----PSSGEVILDGK-AISEYKPKEfaRK 76
Cdd:COG1118 4 EVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRII----AgletPDSGRIVLNGRdLFTNLPPRE--RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 LAVVHQQneaPA---DITVEKLISFG---RMPYKnifspqtDEDREAIERALVCTNLQS--KRdkpiY--ALSGGERQRV 146
Cdd:COG1118 77 VGFVFQH---YAlfpHMTVAENIAFGlrvRPPSK-------AEIRARVEELLELVQLEGlaDR----YpsQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 147 WIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-235 |
3.62e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.96 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LAV 79
Cdd:PRK11614 6 LSFDKVSAHYGKI-QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADITVEKLISFGRmpykniFSPQTDEDREAIERAL-VCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGG------FFAERDQFQERIKWVYeLFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIY 235
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-225 |
3.86e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.02 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIK--NVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA 74
Cdd:PRK13646 1 MTIRfdNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 R----KLAVVHQQNEAPA-DITVEKLISFGRmpyKNiFSPQTDEDREAIERALVctNLQSKRD---KPIYALSGGERQRV 146
Cdd:PRK13646 81 RpvrkRIGMVFQFPESQLfEDTVEREIIFGP---KN-FKMNLDEVKNYAHRLLM--DLGFSRDvmsQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 147 WIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-249 |
6.81e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDN--VTNRLksvSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARkLA 78
Cdd:PRK13537 8 IDFRNVEKRYGDklVVDGL---SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITV-EKLISFGRMpykniFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:PRK13537 84 VVPQFDNLDPDFTVrENLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELnEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEM---VKAI 234
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEI 237
|
250
....*....|....*
gi 446325904 235 YGVDVVVKQDEDTGL 249
Cdd:PRK13537 238 YGPDPVALRDELAPL 252
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-220 |
7.98e-27 |
|
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: 103.14 E-value: 7.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF----ARKLAVVHQQNEAPADITVEKLISFGrMP 102
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQQYALFPHLNVRENLAFG-LK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 103 YKnifspQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKE 182
Cdd:cd03297 102 RK-----RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 446325904 183 LNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03297 177 IKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
1.32e-26 |
|
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: 107.46 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKN--VTF-SYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKS-TLLSVMS---RNHAPSSGEVILDGKAISEYKPKEF 73
Cdd:COG4172 7 LSVEDlsVAFgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRllpDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 AR----KLAVVHQQ-----NeaPAdITVEKLIS-----FGRMPyknifspqtdeDREAIERALVCTNLQSKRD--KPIYA 137
Cdd:COG4172 87 RRirgnRIAMIFQEpmtslN--PL-HTIGKQIAevlrlHRGLS-----------GAAARARALELLERVGIPDpeRRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 ----LSGGERQRVWIAMTLAqNTPMLFL-DEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMK 212
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALA-NEPDLLIaDEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMR 231
|
....*...
gi 446325904 213 DGEIVTKG 220
Cdd:COG4172 232 QGEIVEQG 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-220 |
1.45e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.86 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 4 KNVTFSYDNVTNR-----LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--RNHAPSSGEVILDGKAISeykPKEFARK 76
Cdd:cd03213 7 RNLTVTVKSSPSKsgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 LAVVHQQNEAPADITVeklisfgrmpyknifspqtdedREAIERALvctNLQSkrdkpiyaLSGGERQRVWIAMTLAQNT 156
Cdd:cd03213 84 IGYVPQDDILHPTLTV----------------------RETLMFAA---KLRG--------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDI-NQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-211 |
1.81e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.40 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeyKPKefARKlA 78
Cdd:COG4525 5 TVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPG--ADR-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQqNEApaditveklisfgRMPYKNI-----FSPQ-----TDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWI 148
Cdd:COG4525 80 VVFQ-KDA-------------LLPWLNVldnvaFGLRlrgvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVM 211
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
2.77e-26 |
|
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: 102.41 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKpKEFARKLAVVH-QQNEAPADITVEKL 95
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR-KKFLRRIGVVFgQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFgrmpYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIE 175
Cdd:cd03267 116 FYL----LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446325904 176 ILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-220 |
2.98e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.70 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGK--------AISEYKPKE 72
Cdd:PRK11701 7 LSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 73 FAR-KLAVVHQQneaPAD---ITV-------EKLISFGRMPYKNIfspqtdedREAIERALVCTNLQSKR--DKPiYALS 139
Cdd:PRK11701 86 LLRtEWGFVHQH---PRDglrMQVsaggnigERLMAVGARHYGDI--------RATAGDWLERVEIDAARidDLP-TTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 140 GGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTK 219
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
.
gi 446325904 220 G 220
Cdd:PRK11701 234 G 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
3.05e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYdNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDG------KAISEYKPKEFAR 75
Cdd:COG4161 4 QLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQNEAPADITV-EKLISfgrMPYKNIfsPQTDEdrEAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVmENLIE---APCKVL--GLSKE--QAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 152 LAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGN 221
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-206 |
5.27e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.17 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR-----NHAPSSGEVILDGKAI--SEYKPKEFARKLAVVHQQ-NEAPA 88
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndliPGFRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKpNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 89 DITVEklISFGrmPYKNIFSPQTDEDRE-AIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:PRK14243 106 SIYDN--IAYG--ARINGYKGDMDELVErSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 446325904 168 LDIYYQIEILELVKELNEVYglTIVMVLHDINQAIRYSD 206
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-244 |
6.43e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKLAV-- 79
Cdd:COG3845 7 ELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-AIALGIgm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQneaPADI---TVEKLISFGRMPYKNIFSPqTDEDREAIERAlvctnlqSKR-------DKPIYALSGGERQRVWIA 149
Cdd:COG3845 85 VHQH---FMLVpnlTVAENIVLGLEPTKGGRLD-RKAARARIREL-------SERygldvdpDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 150 MTLAQNTPMLFLDEPTTYL-----DIYYQIeILELVKElnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPND 224
Cdd:COG3845 154 KALYRGARILILDEPTAVLtpqeaDELFEI-LRRLAAE-----GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
250 260
....*....|....*....|
gi 446325904 225 VITEEMVKAIYGVDVVVKQD 244
Cdd:COG3845 228 TSEEELAELMVGREVLLRVE 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-216 |
9.06e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.05 E-value: 9.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 14 TNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA----RKLAVVHQQNEAPAD 89
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 90 ITVEKLISfgrMPYKnIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:PRK11629 102 FTALENVA---MPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446325904 170 IYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHiIVMKDGEI 216
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRL 223
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1-226 |
9.64e-26 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 105.36 E-value: 9.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:TIGR01192 335 VEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQqNEAPADITVEKLISFGRmpyknifSPQTDEDREAIERALVCTNLQSKRDKPIYA--------LSGGERQRVWIAMTL 152
Cdd:TIGR01192 415 FQ-DAGLFNRSIRENIRLGR-------EGATDEEVYEAAKAAAAHDFILKRSNGYDTlvgergnrLSGGERQRLAIARAI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 153 AQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLS-TVRNADLVLFLDQGRLIEKGSFQELI 557
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-197 |
1.30e-25 |
|
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: 104.75 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEApADITVEKLISFGRmpyknifsPQ-TDED-REAIERALVCTNLQSKRD---KPIY----ALSGGERQRVWIAMT 151
Cdd:TIGR02868 415 AQDAHL-FDTTVRENLRLAR--------PDaTDEElWAALERVGLADWLRALPDgldTVLGeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446325904 152 LAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHD 197
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-239 |
2.10e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.10 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFAR-KLAV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCT---NLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLlrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 157 PMLFLDEPTTYL---DIYYQIEIL-ELVKElnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVK 232
Cdd:PRK09700 165 KVIIMDEPTSSLtnkEVDYLFLIMnQLRKE-----GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
....*..
gi 446325904 233 AIYGVDV 239
Cdd:PRK09700 240 LMVGREL 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-211 |
2.28e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.79 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK10247 8 LQLQNVGYLAGD-AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQqneAPAditvekliSFGRMPYKNIFSP----QTDEDREAIERALVCTNL-QSKRDKPIYALSGGERQRVWIAMTLaQN 155
Cdd:PRK10247 87 AQ---TPT--------LFGDTVYDNLIFPwqirNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNL-QF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 156 TP-MLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQaIRYSDHIIVM 211
Cdd:PRK10247 155 MPkVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-239 |
2.61e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKST---LLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK 76
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 LAVVHQQNEAP-ADITVEKLISFGrmpYKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQN 155
Cdd:PRK13640 86 VGIVFQNPDNQfVGATVGDDVAFG---LENRAVPR-PEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 156 TPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIrYSDHIIVMKDGEIVTKGNPNDVIT-EEMVKAI 234
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSkVEMLKEI 240
|
....*
gi 446325904 235 yGVDV 239
Cdd:PRK13640 241 -GLDI 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-225 |
2.82e-25 |
|
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: 104.00 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTL-LSVMsRNHaPSSGEVILDGKAISEYKPKEFA---RKLAVVHQqneapaD--- 89
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLI-PSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQ------Dpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 90 -----ITVEKLISFGRMpyknIFSPQ-TDEDREA-IERALVCTNLQ-SKRDKPIYALSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:COG4172 374 slsprMTVGQIIAEGLR----VHGPGlSAAERRArVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 162 DEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDInQAIRY-SDHIIVMKDGEIVTKGNPNDV 225
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL-AVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-225 |
2.86e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 100.16 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnrLKSVSSEIEIGKITTIIGPNGCGKS----TLLSVMSRNHAPSSGEVILDGKAISeykPKEF-AR 75
Cdd:PRK10418 5 IELRNIALQAAQPL--VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALrGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQQNEAP-------ADITVEKLISFGRMPyknifspqtdeDREAIERALVCTNLQS-KRDKPIYA--LSGGERQR 145
Cdd:PRK10418 80 KIATIMQNPRSAfnplhtmHTHARETCLALGKPA-----------DDATLTAALEAVGLENaARVLKLYPfeMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-224 |
2.99e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFG-RMPYKNifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPML 159
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGlKMLGVP-----KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPND 224
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-255 |
3.19e-25 |
|
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: 102.11 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 20 VSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF----ARKLAVVHQQNEAPADITVEKL 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFGrmpYKNIFSPQTDEDREAIERALvctNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIE 175
Cdd:TIGR02142 96 LRYG---MKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 176 ILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI---------TEEMVKAIYGvdVVVKQDED 246
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWaspdlpwlaREDQGSLIEG--VVAEHDQH 247
|
....*....
gi 446325904 247 TGLYMVPMG 255
Cdd:TIGR02142 248 YGLTALRLG 256
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
3.35e-25 |
|
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: 98.98 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKL 77
Cdd:cd03266 2 ITADALTKRFRDVKKTvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITV-EKLISFGRMpykniFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:cd03266 81 GFVSDSTGLYDRLTArENLEYFAGL-----YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
3.36e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILdGKAIseykpkefarKLAVV 80
Cdd:COG0488 316 LELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEA-PADITV-------------EKLISF-GRMpyknIFSPqtdedreaiERAlvctnlqskrDKPIYALSGGERQR 145
Cdd:COG0488 384 DQHQEElDPDKTVldelrdgapggteQEVRGYlGRF----LFSG---------DDA----------FKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDiyyqIEILELVKELNEVYGLTIVMVLHDinqaiRY-----SDHIIVMKDGEIV 217
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-249 |
3.61e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.47 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA--RKLAVVHQQNEAPADIT-VE 93
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATVFQDPEQQIFYTdID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLISFGrmpYKNIFSPQtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQ 173
Cdd:PRK13638 97 SDIAFS---LRNLGVPE-AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 174 IEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI--TEEMVKAIYGVDVVVKQDEDTGL 249
Cdd:PRK13638 173 TQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFacTEAMEQAGLTQPWLVKLHTQLGL 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-221 |
5.49e-25 |
|
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: 103.36 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 4 KNVTFSYDnvTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVh 81
Cdd:COG5265 361 ENVSFGYD--PERpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 qqneaPADI-----TVEKLISFGRmpyknifsPQTDED--REAIERALVCTNLQSKRDKpiYA---------LSGGERQR 145
Cdd:COG5265 438 -----PQDTvlfndTIAYNIAYGR--------PDASEEevEAAARAAQIHDFIESLPDG--YDtrvgerglkLSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILElvkELNEV-YGLTIVMVLHdinqaiRYS-----DHIIVMKDGEIVTK 219
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQA---ALREVaRGRTTLVIAH------RLStivdaDEILVLEAGRIVER 573
|
..
gi 446325904 220 GN 221
Cdd:COG5265 574 GT 575
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-220 |
6.65e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.12 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISE-------YKPKE- 72
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIaarnrigYLPEEr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 73 -FARKLAVVHQqneapaditvekLISFGR---MPYKNIfspqtdedREAIERALVCTNLQSKRDKPIYALSGGERQRVWI 148
Cdd:cd03269 80 gLYPKMKVIDQ------------LVYLAQlkgLKKEEA--------RRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
17-235 |
2.11e-24 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 97.34 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARkLAVVHQQNEAPA--DITVEK 94
Cdd:TIGR04406 17 VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERAR-LGIGYLPQEASIfrKLTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 95 LIsfgrmpyKNIFSPQTDEDREAIERALVCT----NLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDI 170
Cdd:TIGR04406 96 NI-------MAVLEIRKDLDRAEREERLEALleefQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 171 YYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIY 235
Cdd:TIGR04406 169 IAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-248 |
2.70e-24 |
|
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: 97.48 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 16 RLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeYKPkefarklavvhQQNEAPADITVEKL 95
Cdd:cd03237 14 TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKP-----------QYIKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 IS-----FGRMPYKN--IFSPQtdedreAIERALvctnlqskrDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYL 168
Cdd:cd03237 82 LSsitkdFYTHPYFKteIAKPL------QIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 169 DIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMkDGE--IVTKGNPNDVITEEMVKAIYGVDVVVKQDED 246
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEpsVNGVANPPQSLRSGMNRFLKNLDITFRRDPE 225
|
..
gi 446325904 247 TG 248
Cdd:cd03237 226 TG 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-222 |
4.41e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVTNRlKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVHQ 82
Cdd:PRK11000 6 LRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 QNEAPADITVEKLISFGrMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKpiyALSGGERQRVWIAMTLAQNTPMLFLD 162
Cdd:PRK11000 83 SYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 163 EPTTYLD----IYYQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNP 222
Cdd:PRK11000 159 EPLSNLDaalrVQMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-233 |
5.70e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.03 E-value: 5.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSS-----GEVILDGKAISEYKPK--EF 73
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlnRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 ARKLAVVHQQ-NEAPadITVEKLISFGrmpYKNI-FSPQTDED---REAIERALVCTNLQSKRDKPIYALSGGERQRVWI 148
Cdd:PRK14258 87 RRQVSMVHPKpNLFP--MSVYDNVAYG---VKIVgWRPKLEIDdivESALKDADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKD-----GEIVTKG--- 220
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGltk 241
|
250
....*....|....*..
gi 446325904 221 ----NPNDVITEEMVKA 233
Cdd:PRK14258 242 kifnSPHDSRTREYVLS 258
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-225 |
5.80e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.62 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVV 80
Cdd:PRK10851 3 IEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGR--MPYKNifSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLtvLPRRE--RPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-239 |
7.40e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.95 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFA----RKLAVVHQQNEAPADITV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 93 EKLISFGrMPYKNIfspQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYY 172
Cdd:PRK10070 124 LDNTAFG-MELAGI---NAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 173 QIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI---TEEMVKAIY-GVDV 239
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFrGVDI 270
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
7.74e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.98 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDN--VTNRLksvSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEyKPKEFARKLA 78
Cdd:PRK13536 42 IDLAGVSKSYGDkaVVNGL---SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITV-EKLISFGRMpykniFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:PRK13536 118 VVPQFDNLDLEFTVrENLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELnEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEM---VKAI 234
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIgcqVIEI 271
|
....
gi 446325904 235 YGVD 238
Cdd:PRK13536 272 YGGD 275
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-227 |
8.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.00 E-value: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISE-----YKPKEF 73
Cdd:PRK13645 9 LDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 ARKLAVVHQQNEAPA-DITVEKLISFGRMpyknifspQTDEDREAIERAL--VCTNLQSKRD---KPIYALSGGERQRVW 147
Cdd:PRK13645 89 RKEIGLVFQFPEYQLfQETIEKDIAFGPV--------NLGENKQEAYKKVpeLLKLVQLPEDyvkRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-220 |
8.86e-24 |
|
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: 94.98 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeyKPKEFARKLAVVH 81
Cdd:cd03268 2 KTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 qqnEAPA----DITVEKLISFGRMPyknifspqtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:cd03268 79 ---EAPGfypnLTARENLRLLARLL---------GIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-218 |
1.58e-23 |
|
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: 94.81 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFAR--- 75
Cdd:COG4181 10 ELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlra 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 -KLAVVHQqneapaditvekliSFGRMP----YKNIFSP----QTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRV 146
Cdd:COG4181 90 rHVGFVFQ--------------SFQLLPtltaLENVMLPlelaGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 147 WIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVT 218
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-247 |
1.77e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.33 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTL----LSVMsrnhAPSSGEVILDGKAISE-------YKP 70
Cdd:COG4152 3 ELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGIL----APDSGEVLWDGEPLDPedrrrigYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 71 KEfaR----KLAVVHQqneapaditvekLISFGR---MPYKnifspqtdEDREAIERALVCTNLQSKRDKPIYALSGGER 143
Cdd:COG4152 78 EE--RglypKMKVGEQ------------LVYLARlkgLSKA--------EAKRRADEWLERLGLGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 144 QRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPN 223
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 446325904 224 DV--------------ITEEMVKAIYGVDVVVKQDEDT 247
Cdd:COG4152 215 EIrrqfgrntlrleadGDAGWLRALPGVTVVEEDGDGA 252
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
5.40e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYdNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDG------KAISEYKPKEFA 74
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLAVVHQQ-NEAPADITVEKLIsfgRMPYKNIfspQTDEDrEAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:PRK11124 82 RNVGMVFQQyNLWPHLTVQQNLI---EAPCRVL---GLSKD-QALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-229 |
8.22e-23 |
|
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: 93.32 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYD-NVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNE----------APAD--ITVEKLISFGRMPYKNIFSPQTDEDREAI--ERALvctnlqskrdkpiyALSGGERQR 145
Cdd:cd03252 81 VLQENVlfnrsirdniALADpgMSMERVIEAAKLAGAHDFISELPEGYDTIvgEQGA--------------GLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
|
....
gi 446325904 226 ITEE 229
Cdd:cd03252 224 LAEN 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-217 |
9.47e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.80 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 20 VSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKP---KEFARKLAVVHQqneapaD------- 89
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQ------Dpyaslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 90 -ITVEKLISFgrmPYKnIFSPQTDEDREAIERALvctnLQSKRDKPIYA------LSGGERQRVWIAMTLAQNTPMLFLD 162
Cdd:COG4608 111 rMTVGDIIAE---PLR-IHGLASKAERRERVAEL----LELVGLRPEHAdrypheFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 163 EPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINqAIRY-SDHIIVMKDGEIV 217
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS-VVRHiSDRVAVMYLGKIV 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-228 |
1.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDN----VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEV-ILDGKAISEYKPKEFA- 74
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIVVSSTSKQKEIKp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 --RKLAVVHQQNEAPA-DITVEKLISFGRmpyKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:PRK13643 82 vrKKVGVVFQFPESQLfEETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 152 LAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
1.23e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.98 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR-----NHAPSSGEVILDGKAI--SEYKPKEF 73
Cdd:PRK14267 5 IETVNLRVYYGS-NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllelnEEARVEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 ARKLAVVHQQNEAPADITVEKLISFGrMPYKNIFSPQTDEDrEAIERALVCTNLQSK-----RDKPiYALSGGERQRVWI 148
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELD-ERVEWALKKAALWDEvkdrlNDYP-SNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYglTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG-------N 221
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGptrkvfeN 238
|
250
....*....|....*
gi 446325904 222 PNDVITEEMVKAIYG 236
Cdd:PRK14267 239 PEHELTEKYVTGALG 253
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-249 |
4.27e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 93.24 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 29 ITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGK-----AISEYKPKEfARKLAVVHQqnEAP--ADITVEKLISFGRm 101
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPH-RRRIGYVFQ--EARlfPHLSVRGNLLYGR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 102 pyKNIFSPQTDEDREAIERALvctNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVK 181
Cdd:COG4148 103 --KRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 182 ELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVD--------VVVKQDEDTGL 249
Cdd:COG4148 178 RLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEeagsvleaTVAAHDPDYGL 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-216 |
4.62e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEvILDGKAiseykpkefarKLAvvhq 82
Cdd:PRK11247 15 LNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTA-----------PLA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 qnEAPADItveklisfgRM--------PYK----NIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:PRK11247 78 --EAREDT---------RLmfqdarllPWKkvidNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-222 |
5.24e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPS---SGEVILDGKAISEykpKEFARKLAVVHQQNEAPADITVE 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLISFG---RMPYknifSPQTDEDREAIERALVCTNLQSKRDKPI------YALSGGERQRVWIAMTLAQNTPMLFLDEP 164
Cdd:TIGR00955 118 EHLMFQahlRMPR----RVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 165 TTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAI-RYSDHIIVMKDGEIVTKGNP 222
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSP 251
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-225 |
5.48e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfaRKLAVVH 81
Cdd:PRK11650 5 KLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 qQNEA--PaDITVeklisFGRMPY--KNIFSPQtDEDREAIERALVCTNLQSKRD-KPiYALSGGERQRVwiAMTLA-QN 155
Cdd:PRK11650 83 -QNYAlyP-HMSV-----RENMAYglKIRGMPK-AEIEERVAEAARILELEPLLDrKP-RELSGGQRQRV--AMGRAiVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 156 TPMLFL-DEPTTYLD----IYYQIEILELVKELnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK11650 152 EPAVFLfDEPLSNLDaklrVQMRLEIQRLHRRL----KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
7.40e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVTnRLKSVSSEIE----IGkittIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAiseykpkefarKLA 78
Cdd:COG0488 1 LENLSKSFGGRP-LLDDVSLSINpgdrIG----LVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVEKLISFGRMPYKNIFS---------PQTDEDREAIERAL-----------------VCTNL---QS 129
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTVLDGDAELRALEAeleeleaklAEPDEDLERLAELQeefealggweaearaeeILSGLgfpEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 130 KRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIyYQIEILElvKELNEvYGLTIVMVLHDinqaiRY----- 204
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLE--EFLKN-YPGTVLVVSHD-----RYfldrv 215
|
250
....*....|....*...
gi 446325904 205 SDHIIVMKDGEIVT-KGN 221
Cdd:COG0488 216 ATRILELDRGKLTLyPGN 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-227 |
1.04e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR------NHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNEAPADI 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 TVEKLISFgrmPYKNIFSPQTDEDREAIERAL----VCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTT 166
Cdd:PRK14246 106 SIYDNIAY---PLKSHGIKEKREIKKIVEECLrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 167 YLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVIT 227
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
1.30e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.22 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYdNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR-----NHAPSSGEVILDGKAIseYKPK---- 71
Cdd:PRK14239 6 LQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnPEVTITGSIVYNGHNI--YSPRtdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 72 EFARKLAVVHQQNEaPADITVEKLISFGrMPYKNIFSPQTDEdrEAIERALVCTNLQSKRDKPIY----ALSGGERQRVW 147
Cdd:PRK14239 83 DLRKEIGMVFQQPN-PFPMSIYENVVYG-LRLKGIKDKQVLD--EAVEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYglTIVMVLHDINQAIRYSDHIIVMKDGEIV----TKG--- 220
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIeyndTKQmfm 236
|
250
....*....|....*.
gi 446325904 221 NPNDVITEEMVKAIYG 236
Cdd:PRK14239 237 NPKHKETEDYISGKFG 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-228 |
2.71e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVT----NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAI----SEYKPKE 72
Cdd:PRK13641 3 IKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 73 FARKLAVVHQQNEAPA-DITVEKLISFGrmPyKNiFSPQTDEDREAIERALVCTNL-QSKRDKPIYALSGGERQRVWIAM 150
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfENTVLKDVEFG--P-KN-FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
2.89e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.31 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAP---SSGEVILDGKAISEYKPKefARKL 77
Cdd:COG4136 2 LSLENLTITLGGRP-LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITVEKLISFGrMPYknifSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTP 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPP----TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQA 201
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-246 |
2.95e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.94 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFarkLAVVHQ 82
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 QNEAPAD--ITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:PRK15056 86 SEEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKdGEIVTKGNPNDVIT-EEMVKAIYGV-- 237
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTaENLELAFSGVlr 243
|
....*....
gi 446325904 238 DVVVKQDED 246
Cdd:PRK15056 244 HVALNGSEE 252
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-236 |
3.25e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE-FARKLAVVHQQNEAPADITVEKL 95
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFGRMPYKNIFspqTDEdREAIERALvctnLQSKR-------DKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYL 168
Cdd:PRK11288 100 LYLGQLPHKGGI---VNR-RLLNYEAR----EQLEHlgvdidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 169 DIyYQIEIL-ELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT-----KGNPNDVITEEMV----KAIYG 236
Cdd:PRK11288 172 SA-REIEQLfRVIRELRA-EGRVILYVSHRMEEIFALCDAITVFKDGRYVAtfddmAQVDRDQLVQAMVgreiGDIYG 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-248 |
3.27e-21 |
|
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: 92.15 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 6 VTFSYDNVTNRLKSVSSEIE-----IGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaISeYKPkefarklavv 80
Cdd:COG1245 340 TLVEYPDLTKSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-IS-YKP---------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 hQQNEAPADITVEKLIsfgRMPYKNIFSpqtdedrEAIERALVCTNLQSKR--DKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:COG1245 408 -QYISPDYDGTVEEFL---RSANTDDFG-------SSYYKTEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDInQAIRY-SDHIIVMkDGEIVTKGN---PNDvITEEMVKAI 234
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI-YLIDYiSDRLMVF-EGEPGVHGHasgPMD-MREGMNRFL 553
|
250
....*....|....
gi 446325904 235 YGVDVVVKQDEDTG 248
Cdd:COG1245 554 KELGITFRRDEETG 567
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-225 |
5.15e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.87 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNEAPADITVE--- 93
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRTRLTMVfqh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 -KLISFGRMpYKNIFSPQTD----EDREAIERALVCTNL----QSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEP 164
Cdd:PRK10619 101 fNLWSHMTV-LENVMEAPIQvlglSKQEARERAVKYLAKvgidERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 165 TTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-217 |
5.35e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE---FARKLAVVHQQNEAPADITVE 93
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLISfgrMPYknIFSPQTDED-REAIERALVCTNLQSK-RDKPIyALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIY 171
Cdd:PRK10908 98 DNVA---IPL--IIAGASGDDiRRRVSAALDKVGLLDKaKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446325904 172 YQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:PRK10908 172 LSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-221 |
7.75e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.38 E-value: 7.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKpKEFARKLAVVH-QQNEAPADITVekL 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGVVFgQRSQLWWDLPA--I 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFgRMpYKNIFSPQTDEDREAIERaLVCT-NLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQI 174
Cdd:COG4586 115 DSF-RL-LKAIYRIPDAEYKKRLDE-LVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446325904 175 EILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGN 221
Cdd:COG4586 192 AIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-236 |
8.02e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.12 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 19 SVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQN-EAPADITVEK--L 95
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHvRLFREMTVIEnlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFGRMPYKNIFS-----PQTDE-DREAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTT 166
Cdd:PRK11300 103 VAQHQQLKTGLFSgllktPAFRRaESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 167 YLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMV-KAIYG 236
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDViKAYLG 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-248 |
1.03e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.64 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaISeYKPkefarklavv 80
Cdd:PRK13409 341 VEYPDLTKKLGDF--SLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-IS-YKP---------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 hQQNEAPADITVEKLIS-----FGRMPYKN-IFSPQtdedreAIERALvctnlqskrDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:PRK13409 407 -QYIKPDYDGTVEDLLRsitddLGSSYYKSeIIKPL------QLERLL---------DKNVKDLSGGELQRVAIAACLSR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDInQAIRY-SDHIIVMkDGE--IVTKGNPNDVITEEMV 231
Cdd:PRK13409 471 DADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI-YMIDYiSDRLMVF-EGEpgKHGHASGPMDMREGMN 548
|
250
....*....|....*..
gi 446325904 232 KAIYGVDVVVKQDEDTG 248
Cdd:PRK13409 549 RFLKELGITFRRDEETG 565
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-217 |
1.30e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.82 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYK---PKEFARKLAVVHQqnEAPADI--- 90
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQ--DSISAVnpr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 -TVEKLIsfgRMPYKNIFSpQTDEDREAIERALV-CTNLQ-SKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:PRK10419 106 kTVREII---REPLRHLLS-LDKAERLARASEMLrAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446325904 168 LDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-214 |
2.22e-20 |
|
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: 86.23 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF-ARKLAV 79
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAP--ADITVEKLISFG----RMPYKNIF---SPQTDEDreaieraLVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:cd03290 81 VAYAAQKPwlLNATVEENITFGspfnKQRYKAVTdacSLQPDID-------LLPFGDQTEIGERGINLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIY-----YQIEILELVKELNEvyglTIVMVLHDInQAIRYSDHIIVMKDG 214
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-234 |
2.64e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKLAV- 79
Cdd:PRK15439 12 LCARSISKQYSGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 -VHQQNEAPADITVEKLISFGRmpyknifsPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK15439 90 lVPQEPLLFPNLSVKENILFGL--------PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 159 LFLDEPTTYLDiyyQIEILELVKELNEVY--GLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAI 234
Cdd:PRK15439 162 LILDEPTASLT---PAETERLFSRIRELLaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-214 |
3.57e-20 |
|
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: 84.99 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 4 KNVTFSYDNVTNR---LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS-RNHAPS-SGEVILDGKAiseyKPKEFARKLA 78
Cdd:cd03232 7 KNLNYTVPVKGGKrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgRKTAGViTGEILINGRP----LDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPADITVeklisfgrmpyknifspqtdedREAIE-RALvctnlqskrdkpIYALSGGERQRVWIAMTLAQNTP 157
Cdd:cd03232 83 YVEQQDVHSPNLTV----------------------REALRfSAL------------LRGLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAI-RYSDHIIVMKDG 214
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
4.23e-20 |
|
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: 83.65 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAiseykpkefarKLAVVH 81
Cdd:cd03221 2 ELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QqneapaditveklisfgrmpyknifspqtdedreaieralvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 162 DEPTTYLDIyYQIEILElvKELNEVYGlTIVMVLHD---INQAIrysDHIIVMKDGE 215
Cdd:cd03221 95 DEPTNHLDL-ESIEALE--EALKEYPG-TVILVSHDryfLDQVA---TKIIELEDGK 144
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-226 |
5.16e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 88.65 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVhqqneaPADI-----T 91
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYL------PQDVelfdgT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 92 VEKLISfgRMPyknifspqtDEDREAIERAlvctnlqSKR--------------DKPI----YALSGGERQRVWIAMTLA 153
Cdd:COG4618 422 IAENIA--RFG---------DADPEKVVAA-------AKLagvhemilrlpdgyDTRIgeggARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 154 QNTPMLFLDEPTTYLDiyYQIE------ILELVKElnevyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:COG4618 484 GDPRLVVLDEPNSNLD--DEGEaalaaaIRALKAR-----GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-220 |
1.00e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 18 KSVSSEIEIG----KITTIIGPNGCGKSTLLSVMSR-NHAPS----SGEVILDGKAISEYKPK-EFARKLAVVHQQ-NEA 86
Cdd:PRK14271 34 KTVLDQVSMGfparAVTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNYRDVlEFRRRVGMLFQRpNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 87 P--------ADITVEKLISfgRMPYKNIFSPQTDEDR--EAIERALvctnlqskRDKPiYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK14271 114 PmsimdnvlAGVRAHKLVP--RKEFRGVAQARLTEVGlwDAVKDRL--------SDSP-FRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-198 |
1.09e-19 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 87.92 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMS--------RNHAPSSGEVILD---GKAISEYKPKEFARKLAVVH--QQNEAPADI--- 90
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSgelkpnlgDYDEEPSWDEVLKrfrGTELQDYFKKLANGEIKVAHkpQYVDLIPKVfkg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 TVEKLISfgrmpyknifspQTDED---REAIERalvcTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:COG1245 179 TVRELLE------------KVDERgklDELAEK----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190
....*....|....*....|....*....|.
gi 446325904 168 LDIYYQIEILELVKELNEvYGLTIVMVLHDI 198
Cdd:COG1245 243 LDIYQRLNVARLIRELAE-EGKYVLVVEHDL 272
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-214 |
1.10e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeyKPkefARKLAVVHQQNeapaditvekli 96
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GP---GAERGVVFQNE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 sfGRMPYKNI-----FSPQ-----TDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTT 166
Cdd:PRK11248 80 --GLLPWRNVqdnvaFGLQlagveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446325904 167 YLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDG 214
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-211 |
1.65e-19 |
|
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: 84.73 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 25 EIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEV--------ILD---GKAISEYKPKEFARKLAVVHQ-----QNEAPA 88
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVIVKpqyvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 89 DITVEKLISfgrmpyknifspQTDEdREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYL 168
Cdd:cd03236 104 KGKVGELLK------------KKDE-RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446325904 169 DIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVM 211
Cdd:cd03236 171 DIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-222 |
1.95e-19 |
|
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: 87.38 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 28 KITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIsEYKPKEFARKLAVVHQQNEAPADITVEKLISFgrmpYKNIF 107
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF----YAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 108 SPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVkeLNEVY 187
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
170 180 190
....*....|....*....|....*....|....*
gi 446325904 188 GLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNP 222
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-235 |
2.26e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKlAVVHQQNEAPadiTVEKLI 96
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARR-GIGYLPQEAS---IFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFGR-MPYKNIFSPQTDEDREaiERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYY 172
Cdd:PRK10895 95 VYDNlMAVLQIRDDLSAEQRE--DRAnelMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 173 QIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIY 235
Cdd:PRK10895 173 VIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-236 |
2.98e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfarklavVHQ 82
Cdd:PRK09544 7 LENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-------LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 QNEAPadITVEKlisFGRMpyknifSPQTDedREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLD 162
Cdd:PRK09544 79 DTTLP--LTVNR---FLRL------RPGTK--KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 163 EPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMkDGEIVTKGNPNDVITEEMVKAIYG 236
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPEFISMFG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-220 |
3.23e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKST----LLSVMsrnhaPSSGEVILDGKAISEYKPKE---FARKLAVVHQQ-NEA-- 86
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDpNSSln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 87 PAdITVEKLISFGRMPYKNIFSPQTDEDR--EAIERalVCTNLQSKRDKPIyALSGGERQRVWIAMTLAQNTPMLFLDEP 164
Cdd:PRK15134 377 PR-LNVLQIIEEGLRVHQPTLSAAQREQQviAVMEE--VGLDPETRHRYPA-EFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 165 TTYLDIYYQIEILELVKELNEVYGLTIVMVLHDInQAIRYSDH-IIVMKDGEIVTKG 220
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL-HVVRALCHqVIVLRQGEVVEQG 508
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-225 |
4.12e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.05 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvtnrlKSVSSEIEI----GKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGK---AISEYKPKEF 73
Cdd:PRK11831 8 VDMRGVSFTRGN-----RCIFDNISLtvprGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 ARKLAVVHQQNEAPADITVeklisfgrmpYKNIFSPQTDEDR--EAIERALVCTNLQ------SKRDKPiYALSGGERQR 145
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNV----------FDNVAYPLREHTQlpAPLLHSTVMMKLEavglrgAAKLMP-SELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-220 |
4.49e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.52 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLL----SVMSRNHAPSSGEVILDGKAISEYKPKEFARK----LAVVHQQNEAPA 88
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTVQREGRLARDIRKsranTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 89 DITV-EKLI--SFGRMPY-KNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEP 164
Cdd:PRK09984 100 RLSVlENVLigALGSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 165 TTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
4.66e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 83.26 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSG-----EVILDG-KAISEYKP--KE 72
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQKGliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 73 FARKLAVVHQQ-NEAPADITVEKLISfGRMPYKNifspqtdEDRE-AIERA---LVCTNLQSKRDKPIYALSGGERQRVW 147
Cdd:PRK11264 83 LRQHVGFVFQNfNLFPHRTVLENIIE-GPVIVKG-------EPKEeATARArelLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIyyqieilELVKE-LNEVYGL-----TIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDP-------ELVGEvLNTIRQLaqekrTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-201 |
5.43e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.16 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkEFARKLAVV 80
Cdd:cd03231 1 LEADELTCERDGRA-LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLISFGRmpyknifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWH----------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446325904 161 LDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQA 201
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-233 |
7.69e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.55 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY---DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFAR-- 75
Cdd:PRK10535 5 LELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 --KLAVVHQQNEAPADITVEKlisfgrmpykNIFSPQT---DEDREAIERA---LVCTNLQSKRDKPIYALSGGERQRVW 147
Cdd:PRK10535 85 reHFGFIFQRYHLLSHLTAAQ----------NVEVPAVyagLERKQRLLRAqelLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHD---INQAIRysdhIIVMKDGEIVTkgNPND 224
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDpqvAAQAER----VIEIRDGEIVR--NPPA 227
|
....*....
gi 446325904 225 VITEEMVKA 233
Cdd:PRK10535 228 QEKVNVAGG 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-215 |
1.03e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 81.36 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTN----RLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGkaiseykpkefarK 76
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 LAVVHQ----QNEapadiTVEKLISFGRmPYknifspqtDEDR--EAIEralVCtnlQSKRDKPIYA------------- 137
Cdd:cd03250 68 IAYVSQepwiQNG-----TIRENILFGK-PF--------DEERyeKVIK---AC---ALEPDLEILPdgdlteigekgin 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 LSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD------IYYQIeILELVKElnevyGLTIVMVLHDInQAIRYSDHIIVM 211
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDahvgrhIFENC-ILGLLLN-----NKTRILVTHQL-QLLPHADQIVVL 200
|
....
gi 446325904 212 KDGE 215
Cdd:cd03250 201 DNGR 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-217 |
1.28e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKN--VTFSYDNVTNRLKS-VSSEIEIGKITTIIGPNGCGKS-TLLSVMSRNHAPS----SGEVILDGKAI---SEYK 69
Cdd:PRK15134 6 LAIENlsVAFRQQQTVRTVVNdVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaSEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 70 PKEF-ARKLAVVHQQNEAPADI--TVEKLISfgrmpykNIFSPQTDEDREA--------IERALVCTNLQSKRDKPiYAL 138
Cdd:PRK15134 86 LRGVrGNKIAMIFQEPMVSLNPlhTLEKQLY-------EVLSLHRGMRREAargeilncLDRVGIRQAAKRLTDYP-HQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 139 SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-182 |
1.33e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAvvHqQNEAPADITVEKLI 96
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--H-RNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFgrmpYKNIFspqtDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEI 176
Cdd:PRK13539 95 EF----WAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
....*.
gi 446325904 177 LELVKE 182
Cdd:PRK13539 167 AELIRA 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-198 |
1.83e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.09 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMS---------RNHAPSSGEVI--LDGKAISEYKPKEFARKLAVVH--QQNEAPADI--- 90
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSgelipnlgdYEEEPSWDEVLkrFRGTELQNYFKKLYNGEIKVVHkpQYVDLIPKVfkg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 TVEKLISfgrmpyknifspQTDE---DREAIERalvcTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:PRK13409 179 KVRELLK------------KVDErgkLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|.
gi 446325904 168 LDIYYQIEILELVKELNEvyGLTIVMVLHDI 198
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-222 |
2.42e-18 |
|
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: 80.62 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQqneapaditvEKLISFG--RmpyKNI--FSPQTDED-REAIERA---LVCTNLQSKRDKPIYA----LSGGERQRVW 147
Cdd:cd03244 83 IPQ----------DPVLFSGtiR---SNLdpFGEYSDEElWQALERVglkEFVESLPGGLDTVVEEggenLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKElnEVYGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNP 222
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-228 |
3.52e-18 |
|
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: 83.64 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKLIsFGRMPYKNIfspqtDEDREAIERALVCTN-------LQSKRDKPIYALSGGERQRVWIAMTLA 153
Cdd:TIGR01193 554 PQEPYIFSGSILENLL-LGAKENVSQ-----DEIWAACEIAEIKDDienmplgYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 154 QNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyglTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-222 |
4.20e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSV-MSR-NHAPSSGEVILDGKAISEYKPKEFARK-LA 78
Cdd:COG0396 2 EIKNLHVSVEGKE-ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVlMGHpKYEVTSGSILLDGEDILELSPDERARAgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQneaPADI---TVEKLIsfgrmpyKNIFSPQTDEDREAIE-RALVCTNL------QSKRDKPIYA-LSGGERQRVW 147
Cdd:COG0396 81 LAFQY---PVEIpgvSVSNFL-------RTALNARRGEELSAREfLKLLKEKMkelgldEDFLDRYVNEgFSGGEKKRNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 148 IAMTLAQNTPMLFLDEPTTYLDiyyqIEILELVKE-LNEVY--GLTIVMVLHdiNQAI-RY--SDHIIVMKDGEIVTKGN 221
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD----IDALRIVAEgVNKLRspDRGILIITH--YQRIlDYikPDFVHVLVDGRIVKSGG 224
|
.
gi 446325904 222 P 222
Cdd:COG0396 225 K 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
5.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR----LKSVSSEIEIGKITTIIGPNGCGKSTLLS-----VMSRNHAPSSGEVILDGKAISEYKP- 70
Cdd:PRK13631 22 LRVKNLYCVFDEKQENelvaLNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELIt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 71 ----------KEFARKLAVVHQQNEAPA-DITVEKLISFGRMPYKNifspQTDEDREAIERALVCTNLQSK-RDKPIYAL 138
Cdd:PRK13631 102 npyskkiknfKELRRRVSMVFQFPEYQLfKDTIEKDIMFGPVALGV----KKSEAKKLAKFYLNKMGLDDSyLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 139 SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKElNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT 218
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 446325904 219 KGNPNDVITEE 229
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-235 |
8.02e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.69 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKST-------LLSvmsrnhaPSSGEVILDGKAISE------------YKPKE---Fa 74
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVK-------PDSGRIFLDGEDITHlpmhkrarlgigYLPQEasiF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLavvhqqneapadiTVEKlisfgrmpykNI-----FSPQTDEDREA-IERALVCTNLQSKRDKPIYALSGGERQRVWI 148
Cdd:COG1137 91 RKL-------------TVED----------NIlavleLRKLSKKEREErLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLD---IyyqIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiaV---ADIQKIIRHLKE-RGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
250
....*....|
gi 446325904 226 ITEEMVKAIY 235
Cdd:COG1137 224 LNNPLVRKVY 233
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-228 |
1.29e-17 |
|
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: 81.63 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 16 RLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNEAPADITVEKL 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 ISFGRMPyknifspqtdEDREAIERAL------VCTNLQSKRDKPI----YALSGGERQRVWIAMTLAQNTPMLFLDEPT 165
Cdd:TIGR01842 413 ARFGENA----------DPEKIIEAAKlagvheLILRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 166 TYLDIYYQIEILELVKELnEVYGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-216 |
1.42e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.56 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFaRKL--A 78
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY-RKLfsA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 V---VH-------QQNEAPADITVEKLISFGRMPYKnifspqTDEDREAIeralvcTNLQskrdkpiyaLSGGERQRVWI 148
Cdd:PRK10522 402 VftdFHlfdqllgPEGKPANPALVEKWLERLKMAHK------LELEDGRI------SNLK---------LSKGQKKRLAL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 149 AMTLAQNTPMLFLDE------PtTYLDIYYQiEILELVKELnevyGLTIVMVLHDINQAIRySDHIIVMKDGEI 216
Cdd:PRK10522 461 LLALAEERDILLLDEwaadqdP-HFRREFYQ-VLLPLLQEM----GKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-235 |
2.30e-17 |
|
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: 77.57 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHA--PSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03217 2 EIKDLHVSVGGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNeaPADITVEKLISFGRmpYKNifspqtdedreaieralvctnlqskrdkpiYALSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03217 81 LAFQY--PPEIPGVKNADFLR--YVN------------------------------EGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLH--DINQAIRySDHIIVMKDGEIVTKGNPndviteEMVKAIY 235
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyqRLLDYIK-PDRVHVLYDGRIVKSGDK------ELALEIE 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-225 |
3.15e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 20 VSSEIEIGKITTIIGPNGCGKS-TLLSVMSRNHAP---SSGEVILDGKAISEYKPKEfARKL-----AVVHQQneapADI 90
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE-RRNLvgaevAMIFQD----PMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 TVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNL------QSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEP 164
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 165 TTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-216 |
5.91e-17 |
|
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: 76.32 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTfsydnVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKLAVV 80
Cdd:cd03215 5 LEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD-AIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HqqneAPADITVEKLisFGRMP-YKNIFSPQTdedreaieralvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPML 159
Cdd:cd03215 79 Y----VPEDRKREGL--VLDLSvAENIALSSL--------------------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-231 |
7.85e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.20 E-value: 7.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--RNHAPSSGEVILDGKAISEYKPKEFARK-L 77
Cdd:PRK13549 6 LEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGEELQASNIRDTERAgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITV-------EKLISFGRMPYKNIFspqtdedREAiERALVCTNLQSKRDKPIYALSGGERQRVWIAM 150
Cdd:PRK13549 85 AIIHQELALVKELSVleniflgNEITPGGIMDYDAMY-------LRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 151 TLAQNTPMLFLDEPTTYLdIYYQIEIL-ELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGE-IVTKG----NPND 224
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAVLlDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRhIGTRPaagmTEDD 234
|
....*..
gi 446325904 225 VITeEMV 231
Cdd:PRK13549 235 IIT-MMV 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-220 |
9.24e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKP---KEFARKLAVVHQ----------- 82
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQnpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 ---QNEAPADItveklisfgrmpyknifspQTD----EDREAIERALVCTNLQSKR-DKPIYALSGGERQRVWIAMTLAQ 154
Cdd:PRK11308 111 vgqILEEPLLI-------------------NTSlsaaERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-169 |
9.81e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.86 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 20 VSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkEFARKLAVVHQQNEAPADITVEKLISFg 99
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKPELSALENLHF- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 100 rmpYKNIFSPqtdEDReAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:TIGR01189 97 ---WAAIHGG---AQR-TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-197 |
1.02e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEV----ILDGKAISEYKpKEFARKL 77
Cdd:PRK11147 321 EMENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLEVAYFDQHR-AELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITVEklisfGR----MPYKN--IFSPQtdedreaieRALVctnlqskrdkPIYALSGGERQRVWIAMT 151
Cdd:PRK11147 399 TVMDNLAEGKQEVMVN-----GRprhvLGYLQdfLFHPK---------RAMT----------PVKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446325904 152 LAQNTPMLFLDEPTTYLDiyyqIEILELVKELNEVYGLTIVMVLHD 197
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-217 |
1.02e-16 |
|
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: 76.15 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 6 VTFSYDNVTNRLKSVSSEIEI----------GKITTIIGPNGCGKSTLLSVMSRNHAPS---SGEVILDGKAISEYKPKe 72
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPIlkdfsgvvkpGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 73 FARKLAVVHQQNEAPADITVEKLISFgrmpyknifspqtdedreaierALVCTNLQSKRdkpiyALSGGERQRVWIAMTL 152
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDF----------------------ALRCKGNEFVR-----GISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 153 AQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIrYS--DHIIVMKDGEIV 217
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEI-YDlfDKVLVLYEGRQI 199
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-222 |
2.03e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 75.14 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VhqqneaPADITvekLISFGRMPYKNIFSPQTDED-REAIERALVCTNlqskrdkpiyaLSGGERQRVWIAMTLAQNTPM 158
Cdd:cd03369 87 I------PQDPT---LFSGTIRSNLDPFDEYSDEEiYGALRVSEGGLN-----------LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKElnEVYGLTIVMVLHDINQAIRYsDHIIVMKDGEIVTKGNP 222
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-197 |
2.28e-16 |
|
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: 78.05 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvtnRL--KSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILdGKAIseykpkefarKLA 78
Cdd:TIGR03719 323 IEAENLTKAFGD---KLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEA-PADITVEKLISFGrmpyknifspqTDE----DREAIERALVCT-NLQ-SKRDKPIYALSGGERQRVWIAMT 151
Cdd:TIGR03719 389 YVDQSRDAlDPNKTVWEEISGG-----------LDIiklgKREIPSRAYVGRfNFKgSDQQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446325904 152 LAQNTPMLFLDEPTTYLDiyyqIEILELVKELNEVYGLTIVMVLHD 197
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
2.55e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--RNHAPSSGEVI------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGK-EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 60 --------------LDGKAISEYKPKEFARKLAVVHQQNEA--PADITVEKLI-SFGRMPYknifspqtdEDREAIERAL 122
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFAlyGDDTVLDNVLeALEEIGY---------EGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 123 VC---TNLQSKRDKPIYALSGGERQRVWIAMTLAQNtPMLFL-DEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDI 198
Cdd:TIGR03269 151 DLiemVQLSHRITHIARDLSGGEKQRVVLARQLAKE-PFLFLaDEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|..
gi 446325904 199 NQAIRYSDHIIVMKDGEIVTKGNPNDVITEEM 230
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVAVFM 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-236 |
2.67e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.94 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--RNHAPSSGEVILDGKAISEYKPKEFARK-L 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQQNEAPADITVEKLISFG--------RMPYknifsPQTDEDREAIERALVCTNLQSKRdkPIYALSGGERQRVWIA 149
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitlpggRMAY-----NAMYLRAKNLLRELQLDADNVTR--PVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
....*..
gi 446325904 230 MVKAIYG 236
Cdd:TIGR02633 233 IITMMVG 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-221 |
3.05e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKN-VTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSrNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PRK11174 350 IEAEDlEILSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEAPADiTVEKLISFGRmpyknifsPQTDEDR--EAIERALV---CTNLQSKRDKPI----YALSGGERQRVWIAM 150
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLLGN--------PDASDEQlqQALENAWVsefLPLLPQGLDTPIgdqaAGLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYsDHIIVMKDGEIVTKGN 221
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-226 |
3.50e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.98 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNV--TFSYDNVTNR------LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE 72
Cdd:PRK15112 5 LEVRNLskTFRYRTGWFRrqtveaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 73 FARKLAVVHQ--QNEAPADITVEKLISFgrmPYKnifsPQTDEDREAIERALVCTNLQS--KRDKPIY---ALSGGERQR 145
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRISQILDF---PLR----LNTDLEPEQREKQIIETLRQVglLPDHASYyphMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
.
gi 446325904 226 I 226
Cdd:PRK15112 238 L 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
139-225 |
4.12e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.30 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 139 SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT 218
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
....*..
gi 446325904 219 KGNPNDV 225
Cdd:PRK09473 243 YGNARDV 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-216 |
4.57e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 18 KSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKLAVVH-----QQN----EAPA 88
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSglylDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 89 DITVEKLiSFGRMPykniFSPQTDEDREAIERALVCTNLQ-SKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:PRK15439 359 AWNVCAL-THNRRG----FWIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446325904 168 LDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-203 |
3.98e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 11 DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIS----EYKPKEFARKLAVVHQqnea 86
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeEARAKLRAKHVGFVFQ---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 87 paditvekliSFGRMP----YKNIFSP---QTDEDREAIERA---LVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNT 156
Cdd:PRK10584 96 ----------SFMLIPtlnaLENVELPallRGESSRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIR 203
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-221 |
4.19e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.36 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 7 TFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNE 85
Cdd:PRK10789 320 QFTYPQTDHPaLENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 86 APADiTVEKLISFGRmpyknifspqTDEDREAIERALVCTNL-----------QSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:PRK10789 400 LFSD-TVANNIALGR----------PDATQQEIEHVARLASVhddilrlpqgyDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILELVKELNEvyGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGN 221
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGN 532
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
136-230 |
6.70e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.02 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 136 YALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
90
....*....|....*
gi 446325904 216 IVTKGNPNDVITEEM 230
Cdd:COG4170 237 TVESGPTEQILKSPH 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-217 |
6.81e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 20 VSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVhqqneAPADITVEKLISfG 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIML-----CPEDRKAEGIIP-V 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 100 RMPYKNI-------FSPQ---TDEDREA------IERALVCTnlqSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDE 163
Cdd:PRK11288 346 HSVADNInisarrhHLRAgclINNRWEAenadrfIRSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446325904 164 PTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1-222 |
6.82e-15 |
|
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: 71.91 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHA--PSSGEVILDGKAISEYKPKEFARKLA 78
Cdd:TIGR01978 1 LKIKDLHVSVEDK-EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELEPDERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQneAPADITVEKLISFGRMPYKNIFSPQTDEDREAIE-RALVCTNLQSKRDKPIYA-------LSGGERQRVWIAM 150
Cdd:TIGR01978 80 FLAFQ--YPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDfEKLLKEKLALLDMDEEFLnrsvnegFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 151 TLAQNTPMLFLDEPTTYLDIYYQIEILELVKEL-NEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNP 222
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLrEPDRSFLIITHYQRLLNYIK-PDYVHVLLDGRIVKSGDV 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-216 |
1.29e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSydnvtnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEfARKLAVV 80
Cdd:PRK10762 258 LKVDNLSGP------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLANGIV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPAD-----ITVEKLISFGRMPY--KNIFSPQTDEDREAIERALVCTNLQS-KRDKPIYALSGGERQRVWIAMTL 152
Cdd:PRK10762 331 YISEDRKRDglvlgMSVKENMSLTALRYfsRAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 153 AQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
136-221 |
2.21e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 136 YALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
....*.
gi 446325904 216 IVTKGN 221
Cdd:PRK10261 247 AVETGS 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-226 |
2.46e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeykPKEFArklAVVHqqneapADITvekli 96
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA---LLELG---AGFH------PELT----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 sfGRmpyKNIF---------SPQTDEDREAIErALvcTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:COG1134 105 --GR---ENIYlngrllglsRKEIDEKFDEIV-EF--AELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 168 LDIYYQI----EILELVKElnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:COG1134 177 GDAAFQKkclaRIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-217 |
3.56e-14 |
|
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: 69.48 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeykPKEFARKLAvvhqqneapADITVEKLI 96
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---LLGLGGGFN---------PELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFGRMpyknIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEI 176
Cdd:cd03220 106 YLNGR----LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446325904 177 LELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:cd03220 182 QRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-221 |
4.68e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVV 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADiTVEKLISFGRmpyknifspqtDEDREAIERALVCTNLQS-KRDKP--IYA--------LSGGERQRVWIA 149
Cdd:PRK10790 421 QQDPVVLAD-TFLANVTLGR-----------DISEEQVWQALETVQLAElARSLPdgLYTplgeqgnnLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEI---LELVKELNevyglTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGN 221
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIqqaLAAVREHT-----TLVVIAHRLS-TIVEADTILVLHRGQAVEQGT 557
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-229 |
5.42e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTfSYDNvtNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LAVV 80
Cdd:PRK09700 267 EVRNVT-SRDR--KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPA---------DITVEKLISFGRmpYKN---IFSPQTDEDREAIERALVCTNLQSKrDKPIYALSGGERQRVWI 148
Cdd:PRK09700 344 TESRRDNGffpnfsiaqNMAISRSLKDGG--YKGamgLFHEVDEQRTAENQRELLALKCHSV-NQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
.
gi 446325904 229 E 229
Cdd:PRK09700 500 E 500
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1-215 |
6.01e-14 |
|
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: 68.40 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvtnrlksvsSEIEIGK-ITTIIGPNGCGKSTLLS----VMSRNHAPSSGEVILDGKAISEykpkefAR 75
Cdd:cd03240 4 LSIRNIRSFHER---------SEIEFFSpLTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIRE------GE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 76 KLAVVHQ--QNEAPADITVEKLISFgrmpYKN-IFSPQtDEDREAIERalvctnlqskrdkPIYALSGGERQ------RV 146
Cdd:cd03240 69 VRAQVKLafENANGKKYTITRSLAI----LENvIFCHQ-GESNWPLLD-------------MRGRCSGGEKVlasliiRL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 147 WIAMTLAQNTPMLFLDEPTTYLD---IYYQieILELVKELNEVYGLTIVMVLHDiNQAIRYSDHII-VMKDGE 215
Cdd:cd03240 131 ALAETFGSNCGILALDEPTTNLDeenIEES--LAEIIEERKSQKNFQLIVITHD-EELVDAADHIYrVEKDGR 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-169 |
2.42e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 23 EIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkEFARKLAVVHQQNEAPADIT-VEKLISFGRM 101
Cdd:PRK13538 23 TLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELTaLENLRFYQRL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 102 pyknifspQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:PRK13538 102 --------HGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-214 |
2.60e-13 |
|
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: 67.07 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDgkaiSEYKPKEFARklAVVHQ-----QNE------ 85
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDGGWVDLAQ--ASPREilalrRRTigyvsq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 86 -------APA-DITVEKLISFGrmpyknifspqTDEDrEAIERA---LVCTNLQSKrdkpIYAL-----SGGERQRVWIA 149
Cdd:COG4778 101 flrviprVSAlDVVAEPLLERG-----------VDRE-EARARArelLARLNLPER----LWDLppatfSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325904 150 MTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELnEVYGLTIVMVLHDINQAIRYSDHIIVMKDG 214
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-233 |
2.86e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.70 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVT---------NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNH-APSSGEVILDGKAISEYKP- 70
Cdd:TIGR02633 252 EIGDVILEARNLTcwdvinphrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNPa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 71 KEFARKLAVVHQQNEAPA---------DITVEKLISFGRMPYKNIfSPQTDEDREAIERALVCTnlqSKRDKPIYALSGG 141
Cdd:TIGR02633 332 QAIRAGIAMVPEDRKRHGivpilgvgkNITLSVLKSFCFKMRIDA-AAELQIIGSAIQRLKVKT---ASPFLPIGRLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 142 ERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIvtKGN 221
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL--KGD 484
|
250
....*....|...
gi 446325904 222 -PNDVITEEMVKA 233
Cdd:TIGR02633 485 fVNHALTQEQVLA 497
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
3.61e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNvtnRL--KSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILdGKAIseykpkefarKLAV 79
Cdd:PRK11819 326 EAENLSKSFGD---RLliDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEA-PADITVEKLISFGrmpyknifspqTDE----DREAIERALVCT-NLQ-SKRDKPIYALSGGERQRVWIAMTL 152
Cdd:PRK11819 392 VDQSRDAlDPNKTVWEEISGG-----------LDIikvgNREIPSRAYVGRfNFKgGDQQKKVGVLSGGERNRLHLAKTL 460
|
170
....*....|....*...
gi 446325904 153 AQNTPMLFLDEPTTYLDI 170
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDV 478
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-237 |
7.96e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTfsydnVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE-FARKLAV 79
Cdd:COG1129 257 LEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VhqqneaPAD---------------ITV---EKLISFGRMPYKnifspqtdEDREAIERALvcTNLQSK---RDKPIYAL 138
Cdd:COG1129 332 V------PEDrkgeglvldlsirenITLaslDRLSRGGLLDRR--------RERALAEEYI--KRLRIKtpsPEQPVGNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 139 SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVyGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT 218
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
250
....*....|....*....
gi 446325904 219 KGNPNDVITEEMVKAIYGV 237
Cdd:COG1129 475 ELDREEATEEAIMAAATGG 493
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-225 |
1.45e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVIL-DGKAISEYKPKEFARKL 77
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 AVVHQ-----QNEAPADI-----TVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNL-------------------Q 128
Cdd:PTZ00265 463 GVVSQdpllfSNSIKNNIkyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 129 SKRDKPIYA----------------------------LSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELV 180
Cdd:PTZ00265 543 TIKDSEVVDvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446325904 181 KELNEVYGLTIVMVLHDINqAIRYSDHIIVMKDGEivtKGNPNDV 225
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRLS-TIRYANTIFVLSNRE---RGSTVDV 663
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-213 |
1.66e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR----------------------------- 49
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 50 -------------------NHAPS------SGEVILDGKAISEYKPKEFARKLAVVHQQNeapaditveklISFGRMPYK 104
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkegGSGEDstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP-----------MLFNMSIYE 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 105 NIFSPQTDEDREAIERAL-------VCTNLQSKRDKPI----YALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQ 173
Cdd:PTZ00265 1315 NIKFGKEDATREDVKRACkfaaideFIESLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446325904 174 IEILELVKELNEVYGLTIVMVLHDInQAIRYSDHIIVMKD 213
Cdd:PTZ00265 1395 KLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-234 |
1.99e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAI---SEYKPKEFARKLAVVHQQNEAPAD--IT 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYASLDprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 92 V-----EKLISFGRMpyknifspQTDEDREAIERALVCTNLQSKRD-KPIYALSGGERQRVWIAMTLAQNTPMLFLDEPT 165
Cdd:PRK10261 420 VgdsimEPLRVHGLL--------PGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 166 TYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG-------NPNDVITEEMVKAI 234
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGprravfeNPQHPYTRKLMAAV 567
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-228 |
3.00e-12 |
|
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: 65.98 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 19 SVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEV---------------------------------------- 58
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpdgrgrakryigilhqeydlyphrt 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 59 ILDG--KAISEYKPKEFARKLAVVhqqneapaditVEKLISFGRMPYKNIFSPQTDEdreaieralvctnlqskrdkpiy 136
Cdd:TIGR03269 382 VLDNltEAIGLELPDELARMKAVI-----------TLKMVGFDEEKAEEILDKYPDE----------------------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 137 aLSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIE----ILELVKELNEvyglTIVMVLHDINQAIRYSDHIIVMK 212
Cdd:TIGR03269 428 -LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|....*.
gi 446325904 213 DGEIVTKGNPNDVITE 228
Cdd:TIGR03269 503 DGKIVKIGDPEEIVEE 518
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-224 |
3.93e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFArklavvh 81
Cdd:PRK15064 321 EVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHA------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 qqNEAPADITVEKLISFGRMPyknifspqtdEDREAIERALVCTNLQSKRD--KPIYALSGGERQRVWIAMTLAQNTPML 159
Cdd:PRK15064 393 --YDFENDLTLFDWMSQWRQE----------GDDEQAVRGTLGRLLFSQDDikKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 160 FLDEPTTYLDIyyqieilELVKELN---EVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT-KGNPND 224
Cdd:PRK15064 461 VMDEPTNHMDM-------ESIESLNmalEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-210 |
5.77e-12 |
|
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: 62.59 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 23 EIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISeYKPKEFArklavvhqqneapaditveklisfgrmp 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKPQYID---------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 103 yknifspqtdedreaieralvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKE 182
Cdd:cd03222 72 -----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*...
gi 446325904 183 LNEVYGLTIVMVLHDINQAIRYSDHIIV 210
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-217 |
7.30e-12 |
|
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: 64.82 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTN----RLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEykpkefarkl 77
Cdd:COG4615 329 ELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 78 avvhQQNEApaditveklisfgrmpYKNIFS--------------PQTDEDREAIERALVCTNLQSK----------RDk 133
Cdd:COG4615 399 ----DNREA----------------YRQLFSavfsdfhlfdrllgLDGEADPARARELLERLELDHKvsvedgrfstTD- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 134 piyaLSGGERQRVWIAMTLAQNTPMLFLDE------PtTYLDIYYQiEILELVKELnevyGLTIVMVLHDinqaIRY--- 204
Cdd:COG4615 458 ----LSQGQRKRLALLVALLEDRPILVFDEwaadqdP-EFRRVFYT-ELLPELKAR----GKTVIAISHD----DRYfdl 523
|
250
....*....|...
gi 446325904 205 SDHIIVMKDGEIV 217
Cdd:COG4615 524 ADRVLKMDYGKLV 536
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-236 |
1.21e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 11 DNVTNRLKSVSseieigkITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE-FARKLAVVHQQNEAPAD 89
Cdd:PRK10982 15 DNVNLKVRPHS-------IHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 90 ITVEKLISFGRMPYKNIFSPQTD--EDREAIERALvctNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTY 167
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDEL---DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 168 LDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYG 236
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-229 |
1.44e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 32 IIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQqneapADITVEKLISFGRMPykniFSPQT 111
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-----SPVLFSGTVRFNIDP----FSEHN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 112 DEDR-EAIERAlvctNLQSKRDKPIYAL-----------SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILEL 179
Cdd:PLN03232 1338 DADLwEALERA----HIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446325904 180 VKElnEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:PLN03232 1414 IRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
136-227 |
1.62e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 136 YALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
90
....*....|..
gi 446325904 216 IVTKGNPNDVIT 227
Cdd:PRK15093 237 TVETAPSKELVT 248
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-231 |
1.76e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTfSYDnVTN----RLKSVSSEIEIGKITTIIGPNGCGKSTLL-SVMSRNHAPSSGEVILDGKAISEYKPKE-FA 74
Cdd:PRK13549 260 LEVRNLT-AWD-PVNphikRVDDVSFSLRRGEILGIAGLVGAGRTELVqCLFGAYPGRWEGEIFIDGKPVKIRNPQQaIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 75 RKLAVVhqqneaPAD---------------ITVEKLISFGRMPYKNIFSPQTDEDREaIERALVCTnlqSKRDKPIYALS 139
Cdd:PRK13549 338 QGIAMV------PEDrkrdgivpvmgvgknITLAALDRFTGGSRIDDAAELKTILES-IQRLKVKT---ASPELAIARLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 140 GGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIvtK 219
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL--K 484
|
250
....*....|...
gi 446325904 220 GN-PNDVITEEMV 231
Cdd:PRK13549 485 GDlINHNLTQEQV 497
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-215 |
2.19e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF-ARKLAVVHQQNEAPADITV--------EKLIS 97
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqEAGIGIIHQELNLIPQLTIaeniflgrEFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 98 FGRMPYKNIFspqtdedREAiERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTtylDIYYQIEIL 177
Cdd:PRK10762 110 FGRIDWKKMY-------AEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT---DALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446325904 178 ELVKELNEV--YGLTIVMVLHDINQAIRYSDHIIVMKDGE 215
Cdd:PRK10762 179 SLFRVIRELksQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-204 |
2.25e-11 |
|
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: 63.42 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 32 IIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE--FARKLAVVHQQNEAPADItVEKLISFGRMpYKNIFSP 109
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpqLDPTKTVRENVEEGVAEI-KDALDRFNEI-SAKYAEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 110 QTDEDREAIERALVCT--------NLQSK--------R----DKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:TIGR03719 114 DADFDKLAAEQAELQEiidaadawDLDSQleiamdalRcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
170 180 190
....*....|....*....|....*....|....*
gi 446325904 170 IyYQIEILElvKELNEVYGlTIVMVLHDinqaiRY 204
Cdd:TIGR03719 194 A-ESVAWLE--RHLQEYPG-TVVAVTHD-----RY 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-220 |
3.65e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaiseykpkefarkLAVVH 81
Cdd:TIGR00957 639 VHNATFTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAPADiTVEKLISFGRMPYKNIFspqtdedREAIERALVCTNL-------QSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:TIGR00957 706 QQAWIQND-SLRENILFGKALNEKYY-------QQVLEACALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 155 NTPMLFLDEPTTYLDIYYQIEILE-LVKELNEVYGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKG 220
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMG 843
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-220 |
3.74e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 11 DNVTNRLKSvsseieiGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF--ARK-LAVVHQQNEAP 87
Cdd:PRK15079 38 DGVTLRLYE-------GETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSdIQMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 88 -------ADITVEKLISF-GRMPYKNIfspqTDEDREAIERALVCTNLQSKRdkPiYALSGGERQRVWIAMTLAQNTPML 159
Cdd:PRK15079 111 lnprmtiGEIIAEPLRTYhPKLSRQEV----KDRVKAMMLKVGLLPNLINRY--P-HEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 160 FLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKG 220
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-237 |
5.74e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.56 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSrnhAPSSGEVILDGKAISEYKPKE--FARKLAVVHQQNEAPADITV-E 93
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLA---GRKTGGYIEGDIRISGFPKKQetFARISGYCEQNDIHSPQVTVrE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLI--SFGRMPY------KNIFspqTDEDREAIEralvctnLQSKRDK-----PIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:PLN03140 973 SLIysAFLRLPKevskeeKMMF---VDEVMELVE-------LDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 161 LDEPTTYLDIYYQIEILELVKelNEV-YGLTIVMVLH----DINQAIrysDHIIVMKDGEIVTKGNP---NDVITEEMVK 232
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVR--NTVdTGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYSGPlgrNSHKIIEYFE 1117
|
....*
gi 446325904 233 AIYGV 237
Cdd:PLN03140 1118 AIPGV 1122
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-226 |
7.55e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS-RNHAPS-SGEVILDGKAISeykpKEFARKLAVVHQQNEAPADITV-E 93
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPT----KQILKRTGFVTQDDILYPHLTVrE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLI--SFGRMPyKNIFSPQTDEDREAIERALVCTNLQSK--RDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:PLN03211 160 TLVfcSLLRLP-KSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 170 IYYQIEILELVKELNEvYGLTIVMVLHDINQAI-RYSDHIIVMKDGEIVTKGNPNDVI 226
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-225 |
8.59e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 29 ITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEF----ARKLAVVHQQNEAPADITVEKLISFGrmpYK 104
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDARLFPHYKVRGNLRYG---MA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 105 NIFSPQTDEDRE--AIERALvctnlqsKRdKPIyALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEIL----E 178
Cdd:PRK11144 103 KSMVAQFDKIVAllGIEPLL-------DR-YPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLpyleR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446325904 179 LVKELNevygLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDV 225
Cdd:PRK11144 174 LAREIN----IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-221 |
1.07e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPS--SGEVILDGKAISEYKPKEFARKLA 78
Cdd:CHL00131 8 LEIKNLHASVNE-NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNeaPADITVEKLISFGRMPYKNIFSPQTDEDREAIE-RALVCTNLQSKRDKPIY-------ALSGGERQRVWIAM 150
Cdd:CHL00131 87 FLAFQY--PIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEfLEIINEKLKLVGMDPSFlsrnvneGFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 151 TLAQNTPMLFLDEPTTYLDiyyqIEILELV-KELNEVYGLTIVMVLhdINQAIRYSDHII-----VMKDGEIVTKGN 221
Cdd:CHL00131 165 MALLDSELAILDETDSGLD----IDALKIIaEGINKLMTSENSIIL--ITHYQRLLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-220 |
1.85e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 3 IKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAP-SSGEVILDGKAisEYKPkefarklav 79
Cdd:PLN03130 617 IKNGYFSWDSKAERptLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTV--AYVP--------- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 vhqQNEAPADITVEKLISFGrMPYknifspqtdeDREAIERALVCTNLQskRDKPIYA-------------LSGGERQRV 146
Cdd:PLN03130 686 ---QVSWIFNATVRDNILFG-SPF----------DPERYERAIDVTALQ--HDLDLLPggdlteigergvnISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 147 WIAMTLAQNTPMLFLDEPTTYLDIYYQIEILE-LVKElnEVYGLTIVMV---LHDINQAirysDHIIVMKDGEIVTKG 220
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKD--ELRGKTRVLVtnqLHFLSQV----DRIILVHEGMIKEEG 821
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-228 |
1.91e-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: 60.73 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQNeapaditveklI 96
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP-----------V 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFGRMPYKNI--FSPQTDED-REAIERALVCTNLQSKRDKPIYA-------LSGGERQRVWIAMTLAQNTPMLFLDEPTT 166
Cdd:TIGR00957 1371 LFSGSLRMNLdpFSQYSDEEvWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 167 YLDIYYQIEILELVKELNEvyGLTIVMVLHDINQAIRYSdHIIVMKDGEIVTKGNPNDVITE 228
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-224 |
2.92e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILdgkaiseykpkefARKLAVVHQQneapADI---TVE 93
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQ----AWImnaTVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLISFgrmpykniFSPqtdEDREAIERALVCTNLQSK------------RDKPIyALSGGERQRVWIAMTLAQNTPMLFL 161
Cdd:PTZ00243 739 GNILF--------FDE---EDAARLADAVRVSQLEADlaqlgggleteiGEKGV-NLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 162 DEPTTYLDIYYQIEILELVKeLNEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPND 224
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-221 |
7.31e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR--LKSVSSEIEIGKITTIIGPNGCGKSTLLSVM--SRNHAPSSGEVILDGKAISEYKPKEFark 76
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMlgELSHAETSSVVIRGSVAYVPQVSWIF--- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 77 lavvhqqneapaDITVEKLISFGrmpyknifspqTDEDREAIERALVCTNLQSKRDkpIYA-------------LSGGER 143
Cdd:PLN03232 692 ------------NATVRENILFG-----------SDFESERYWRAIDVTALQHDLD--LLPgrdlteigergvnISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 144 QRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILE-LVKElnEVYGLTIVMV---LHDINQAirysDHIIVMKDGEIVTK 219
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKD--ELKGKTRVLVtnqLHFLPLM----DRIILVSEGMIKEE 820
|
..
gi 446325904 220 GN 221
Cdd:PLN03232 821 GT 822
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-216 |
8.85e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 5 NVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAiseykpkefarKLAVVHQQN 84
Cdd:PLN03073 513 DASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 85 EAPADITVEKLISFGR----MPYKNIfspqtdedREAIERALVCTNLQSKrdkPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:PLN03073 582 VDGLDLSSNPLLYMMRcfpgVPEQKL--------RAHLGSFGVTGNLALQ---PMYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 161 LDEPTTYLDiyyqieiLELVKELneVYGLT-----IVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:PLN03073 651 LDEPSNHLD-------LDAVEAL--IQGLVlfqggVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-246 |
8.94e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQqneapADITVEKLISFGRMPykniFSPQTDEDR-EAIERA----LVCTN---LQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:PLN03130 1318 IPQ-----APVLFSGTVRFNLDP----FNEHNDADLwESLERAhlkdVIRRNslgLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 152 LAQNTPMLFLDEPTTYLDIYYQIEILELVKElnEVYGLTIVMVLHDINQAIRySDHIIVMKDGEIVTKGNPNDVITEE-- 229
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEgs 1465
|
250 260
....*....|....*....|....*..
gi 446325904 230 ----MVK------AIYGVDVVVKQDED 246
Cdd:PLN03130 1466 afskMVQstgaanAQYLRSLVFGGDED 1492
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-196 |
1.05e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNhapSSGEVILDGKAISEYKPKE--FARKLAVVHQQNEAPADITV-E 93
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER---VTTGVITGGDRLVNGRPLDssFQRSIGYVQQQDLHLPTSTVrE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLI--SFGRMPyKNIFSPQTDEDREAIERALvctNLQSKRDK----PIYALSGGERQRVWIAMTLAQNTPML-FLDEPTT 166
Cdd:TIGR00956 856 SLRfsAYLRQP-KSVSKSEKMEYVEEVIKLL---EMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLlFLDEPTS 931
|
170 180 190
....*....|....*....|....*....|
gi 446325904 167 YLDIYYQIEILELVKELNEvYGLTIVMVLH 196
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLAD-HGQAILCTIH 960
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-228 |
1.08e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPS---SGEVILDGKAISEYKPkefaRKLAVVHQQNEAPADI-TV 92
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP----RKTSAYISQNDVHVGVmTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 93 EKLISFG------------------RMPYKNIFsPQTDED-------REAIERALVcTNLQSK------------RDKPI 135
Cdd:PLN03140 257 KETLDFSarcqgvgtrydllselarREKDAGIF-PEAEVDlfmkataMEGVKSSLI-TDYTLKilgldickdtivGDEMI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 136 YALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD--IYYQIeilelVKELNEVYGLTIVMVLHDINQ----AIRYSDHII 209
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDssTTYQI-----VKCLQQIVHLTEATVLMSLLQpapeTFDLFDDII 409
|
250
....*....|....*....
gi 446325904 210 VMKDGEIVTKGnPNDVITE 228
Cdd:PLN03140 410 LLSEGQIVYQG-PRDHILE 427
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-220 |
2.33e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRN----HAPSSGEVILDGKAISEYKPkeFARKLAVVHQQNEA--PAdI 90
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGITPEEIKK--HYRGDVVYNAETDVhfPH-L 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 91 TVEKLISFG---RMP---YKNIfspqTDEDREAIERALVCT--NLQSKRDKP-----IYALSGGERQRVWIAMTLAQNTP 157
Cdd:TIGR00956 154 TVGETLDFAarcKTPqnrPDGV----SREEYAKHIADVYMAtyGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 158 MLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDINQ-AIRYSDHIIVMKDGEIVTKG 220
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFG 293
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-211 |
3.16e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.64 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 15 NRLKSVSSEIEIGKITTIIGPNGCGKSTLLSvmsrnhapssgEVIL-DGKAISEYKPKEFARKLAVVHQQNEAPADITVE 93
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYaSGKARLISFLPKFSRNKLIFIDQLQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 94 KLiSFGRmpyknifspqtdedreaieralvctNLQSkrdkpiyaLSGGERQRVWIAMTLAQNT-PMLF-LDEPTTYLDiy 171
Cdd:cd03238 78 YL-TLGQ-------------------------KLST--------LSGGELQRVKLASELFSEPpGTLFiLDEPSTGLH-- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446325904 172 yQIEILELVKELNEVY--GLTIVMVLHDInQAIRYSDHIIVM 211
Cdd:cd03238 122 -QQDINQLLEVIKGLIdlGNTVILIEHNL-DVLSSADWIIDF 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-217 |
3.39e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFaRKLAVVH 81
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER-RRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 -----QQNEAPADITV-EKLI--SFGRMPY-KNIFspqtdEDREAIE---RALV------CTNLQSkrdkPIYALSGGER 143
Cdd:COG3845 338 ipedrLGRGLVPDMSVaENLIlgRYRRPPFsRGGF-----LDRKAIRafaEELIeefdvrTPGPDT----PARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 144 QRVWIAMTLAQNTPMLFLDEPTTYLDI----YYQIEILELVKElnevyGLTIVMVLHDINQAIRYSDHIIVMKDGEIV 217
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLELRDA-----GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-204 |
3.88e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 26 IGkittIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKE----------------FARKLAVVHQQNE---- 85
Cdd:PRK11819 36 IG----VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpqldpektvrenveegVAEVKAALDRFNEiyaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 86 -APADITVEKLISfgRMPyknifspqtdEDREAIErALVCTNLQSK------------RDKPIYALSGGERQRVWIAMTL 152
Cdd:PRK11819 112 yAEPDADFDALAA--EQG----------ELQEIID-AADAWDLDSQleiamdalrcppWDAKVTKLSGGERRRVALCRLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446325904 153 AQNTPMLFLDEPTTYLDiyyqIE-ILELVKELNEVYGlTIVMVLHDinqaiRY 204
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPG-TVVAVTHD-----RY 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-197 |
7.79e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 24 IEIGKITTIIGPNGCGKSTLLSVMSrnhapssGEVILD-GKAIseykpkeFARKLAVVHQQNEAPADI--TV-------- 92
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRII-------YEQDLIVARLQQDPPRNVegTVydfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 93 ----EKLISFGRMPYKnIFSPQTDEDREAIERAL-----------------VCTNLQSKRDKPIYALSGGERQRVWIAMT 151
Cdd:PRK11147 92 eeqaEYLKRYHDISHL-VETDPSEKNLNELAKLQeqldhhnlwqlenrineVLAQLGLDPDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446325904 152 LAQNTPMLFLDEPTTYLDIyYQIEILE-LVKElnevYGLTIVMVLHD 197
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDI-ETIEWLEgFLKT----FQGSIIFISHD 212
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-226 |
1.17e-08 |
|
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: 55.40 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 134 PIYALSGGERQRVWIAMTLAQ--NTPMLF-LDEPTTYL---DIYYQIEILE-LVKElnevyGLTIVMVLHDINqAIRYSD 206
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKrsTGRTLYiLDEPTTGLhfdDIKKLLEVLQrLVDK-----GNTVVVIEHNLD-VIKTAD 899
|
90 100
....*....|....*....|....*.
gi 446325904 207 HIIVM------KDGEIVTKGNPNDVI 226
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGTPEEVA 925
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-228 |
1.19e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEykpkefARklavvH 81
Cdd:NF033858 3 RLEGVSHRYGKTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------AR-----H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 82 QQNEAP--------------ADITVEKLISF-GRMpykniFSpQTDEDREA-IERALVCTNLQSKRDKPIYALSGGERQR 145
Cdd:NF033858 71 RRAVCPriaympqglgknlyPTLSVFENLDFfGRL-----FG-QDAAERRRrIDELLRATGLAPFADRPAGKLSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 146 VWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKEL-NEVYGLTIVMVLHDINQAIRYsDHIIVMKDGEIVTKGNPND 224
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAE 223
|
....
gi 446325904 225 VITE 228
Cdd:NF033858 224 LLAR 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-196 |
1.33e-08 |
|
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: 52.93 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPkefarklavv 80
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLP---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 hQQneapaditveklisfgrmPYkniFSPQTDedREAIeralvctnlqskrdkpIYA----LSGGERQRVWIAMTLAQNT 156
Cdd:cd03223 71 -QR------------------PY---LPLGTL--REQL----------------IYPwddvLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446325904 157 PMLFLDEPTTYLDIYYQIEILELVKELnevyGLTIVMVLH 196
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-197 |
1.41e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSrnhapssGEVILDGKAISeyKPKEFArkLAVVHQQNEAPADITVEKLI 96
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYT--FPGNWQ--LAWVNQETPALPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 sfgrmpyknifspqtDEDRE--AIERALVCTN----------LQSKRD--------------------------KPIYAL 138
Cdd:PRK10636 86 ---------------DGDREyrQLEAQLHDANerndghaiatIHGKLDaidawtirsraasllhglgfsneqleRPVSDF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 139 SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKElnevYGLTIVMVLHD 197
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS----YQGTLILISHD 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-231 |
1.98e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDNVTnRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--RNHAPSSGEVILDGKaiseykPKEF------ 73
Cdd:NF040905 3 EMRGITKTFPGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFDGE------VCRFkdirds 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 74 -ARKLAVVHQQneapaditvEKLIsfgrmPY----KNIF--SPQTDED----REAIERA---LVCTNLQSKRDKPIYALS 139
Cdd:NF040905 76 eALGIVIIHQE---------LALI-----PYlsiaENIFlgNERAKRGvidwNETNRRArelLAKVGLDESPDTLVTDIG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 140 GGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIV-T 218
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIeT 220
|
250
....*....|....*...
gi 446325904 219 KGNPNDVITEE-----MV 231
Cdd:NF040905 221 LDCRADEVTEDriirgMV 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-174 |
2.48e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNR-LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRnHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQqneapaditveKLISFGRMPYKNI--FSPQTDED--REAIERAL--VCTNLQSKRDKPI----YALSGGERQRVWIA 149
Cdd:TIGR01271 1297 IPQ-----------KVFIFSGTFRKNLdpYEQWSDEEiwKVAEEVGLksVIEQFPDKLDFVLvdggYVLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|....*.
gi 446325904 150 MTLAQNTPMLFLDEPTTYLD-IYYQI 174
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDpVTLQI 1391
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-232 |
4.26e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 4 KNVTFSYDNVTNR----LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARK-LA 78
Cdd:PRK10982 247 GEVILEVRNLTSLrqpsIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQNEAPA-----DITVEKLISFGRmPYKNIFSPQTDEDREA-----IERALVCTNLQSKrdkPIYALSGGERQRVWI 148
Cdd:PRK10982 327 LVTEERRSTGiyaylDIGFNSLISNIR-NYKNKVGLLDNSRMKSdtqwvIDSMRVKTPGHRT---QIGSLSGGNQQKVII 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 149 AMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQN 481
|
....
gi 446325904 229 EMVK 232
Cdd:PRK10982 482 EILR 485
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-216 |
4.37e-08 |
|
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: 52.55 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSY-DNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRnHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQqneapaditveKLISFGRMPYKNI--FSPQTDED--REAIERAL--VCTNLQSKRDKPI----YALSGGERQRVWIA 149
Cdd:cd03289 82 IPQ-----------KVFIFSGTFRKNLdpYGKWSDEEiwKVAEEVGLksVIEQFPGQLDFVLvdggCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 150 MTLAQNTPMLFLDEPTTYLD-IYYQIeileLVKELNEVY-GLTIVMVLHDInQAIRYSDHIIVMKDGEI 216
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDpITYQV----IRKTLKQAFaDCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-178 |
6.24e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 13 VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaISeYKPkefarklavvhqQNEAPADITV 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-IS-FSP------------QTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 93 EKLISFG----RMPYKNIFSP-QTDEDreaieralvCTNLQSKRDKPI----YALSGGERQRVWIAMTLAQNTPMLFLDE 163
Cdd:TIGR01271 504 KDNIIFGlsydEYRYTSVIKAcQLEED---------IALFPEKDKTVLgeggITLSGGQRARISLARAVYKDADLYLLDS 574
|
170
....*....|....*
gi 446325904 164 PTTYLDIYYQIEILE 178
Cdd:TIGR01271 575 PFTHLDVVTEKEIFE 589
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-169 |
6.95e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 2 EIKNVTFSYDN--VTNRLksvSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPS-------------SGEVILDGKais 66
Cdd:PRK10938 262 VLNNGVVSYNDrpILHNL---SWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrrgSGETIWDIK--- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 67 eykpkefaRKLAVVHQQ--NEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSK-RDKPIYALSGGER 143
Cdd:PRK10938 336 --------KHIGYVSSSlhLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQ 407
|
170 180
....*....|....*....|....*.
gi 446325904 144 QRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-196 |
1.31e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNVTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSR--NHApsSGEVILdgkaiseykPKefARKLA 78
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwPYG--SGRIAR---------PA--GARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 79 VVHQQneapaditveklisfgrmPY------KNIFS-PQTDE--DREAIERALVCTNLQ------------SKRdkpiya 137
Cdd:COG4178 430 FLPQR------------------PYlplgtlREALLyPATAEafSDAELREALEAVGLGhlaerldeeadwDQV------ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446325904 138 LSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKElnEVYGLTIVMVLH 196
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-222 |
3.57e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 15 NRLKSVSSEIEIGKITTIIGPNGCGKSTLL------SVMSRNHApsSGEVILDGKAISEYkpkEFARKLAVVHQ------ 82
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHL--KKEQPGNHDRIEGL---EHIDKVIVIDQspigrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 QNEAPAdiTVEKLISFGRMPYKNI-----FSPQTDEDR---------------EAIE------------RALVCTNLQS- 129
Cdd:cd03271 84 PRSNPA--TYTGVFDEIRELFCEVckgkrYNRETLEVRykgksiadvldmtveEALEffenipkiarklQTLCDVGLGYi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 130 KRDKPIYALSGGERQRVWIAMTLAQNTP---MLFLDEPTTYL---DIYYQIEIL-ELVKElnevyGLTIVMVLHDINqAI 202
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLqRLVDK-----GNTVVVIEHNLD-VI 235
|
250 260
....*....|....*....|....*.
gi 446325904 203 RYSDHIIVM------KDGEIVTKGNP 222
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-212 |
3.63e-07 |
|
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: 48.51 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMSrnhapssgeVILDGKAISEYKPKEFARklavvhqqneapaditveklisfgrmpykNI 106
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKA-----------------------------GC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 107 FSPQtdedrEAIERALVCTNLqskrdkpiyalSGGERQRVWIAMTLA----QNTPMLFLDEPTTYLDIYYQIEILELVKE 182
Cdd:cd03227 63 IVAA-----VSAELIFTRLQL-----------SGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180 190
....*....|....*....|....*....|
gi 446325904 183 LNeVYGLTIVMVLHDINQAIRySDHIIVMK 212
Cdd:cd03227 127 HL-VKGAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-215 |
4.03e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.86 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaISeykpkeFARKLAVVhqqneAPADITVEKL- 95
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-IS------FSSQFSWI-----MPGTIKENIIf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 96 -ISFGRMPYKNIFSP-QTDEDREAIeralvctnlqSKRDKPIYA-----LSGGERQRVWIAMTLAQNTPMLFLDEPTTYL 168
Cdd:cd03291 121 gVSYDEYRYKSVVKAcQLEEDITKF----------PEKDNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446325904 169 DIYYQIEILE-LVKELneVYGLTIVMVLHDINQaIRYSDHIIVMKDGE 215
Cdd:cd03291 191 DVFTEKEIFEsCVCKL--MANKTRILVTSKMEH-LKKADKILILHEGS 235
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-229 |
1.26e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.37 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDN-VTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd03288 20 IKIHDLCVRYENnLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQneapaDITVEKLISFGRMPYKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYA----LSGGERQRVWIAMTLAQN 155
Cdd:cd03288 100 ILQD-----PILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEggenFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446325904 156 TPMLFLDEPTTYLDIYYQiEILELVKeLNEVYGLTIVMVLHDINqAIRYSDHIIVMKDGEIVTKGNPNDVITEE 229
Cdd:cd03288 175 SSILIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-215 |
1.29e-06 |
|
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: 46.98 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVI-LDGkaiseykpkefarklavvhqqneapaditveklisfgrmpykn 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 106 ifspqtdedrEAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELV----- 180
Cdd:smart00382 39 ----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446325904 181 KELNEVYGLTIVMVLHDINQ-----AIRYSDHIIVMKDGE 215
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-220 |
1.53e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 LSGGERQRVWIAMTLAQN-TPMLF-LDEPTTYL---DIYYQIEILELVKELnevyGLTIVMVLHDiNQAIRYSDHIIVM- 211
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGlTGVLYvLDEPSIGLhprDNDRLIETLKRLRDL----GNTVLVVEHD-EDTIRAADHVIDIg 212
|
90
....*....|....
gi 446325904 212 -----KDGEIVTKG 220
Cdd:cd03270 213 pgagvHGGEIVAQG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-216 |
1.61e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 32 IIGPNGCGKSTLLSVMSRNHAPSSGEVILdGKAIseyKPKEFARKLAVVHQQNEAP-------ADITVEKLISfgrmPYK 104
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI---KLGYFAQHQLEFLRADESPlqhlarlAPQELEQKLR----DYL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 105 NIFSPQTDEDREAIERalvctnlqskrdkpiyaLSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDiyyqieiLELVKELN 184
Cdd:PRK10636 415 GGFGFQGDKVTEETRR-----------------FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQALT 470
|
170 180 190
....*....|....*....|....*....|....*
gi 446325904 185 EV---YGLTIVMVLHDINQAIRYSDHIIVMKDGEI 216
Cdd:PRK10636 471 EAlidFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-170 |
1.64e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 24 IEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEykpKEFARKLAVVHQQNEAPADITVEKLISF----- 98
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLKADLSTLENLHFlcglh 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325904 99 GRMPyknifspqtdedREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDI 170
Cdd:PRK13543 111 GRRA------------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-169 |
3.49e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 29 ITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYkPKEFarkLAVVHQQNEAPADITVEKLISFGRMPYKNIfs 108
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-AKPY---CTYIGHNLGLKLEMTVFENLKFWSEIYNSA-- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325904 109 pqtdedrEAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:PRK13541 102 -------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-225 |
3.64e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 LSGGERQRVWIAMTLAQ----NTpmLF-LDEPTTYL---DIYYQIEIL-ELVKELNevyglTIVMVLH--DInqaIRYSD 206
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKrstgKT--LYiLDEPTTGLhfeDIRKLLEVLhRLVDKGN-----TVVVIEHnlDV---IKTAD 900
|
90 100
....*....|....*....|....*
gi 446325904 207 HIIVM------KDGEIVTKGNPNDV 225
Cdd:PRK00349 901 WIIDLgpeggdGGGEIVATGTPEEV 925
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-226 |
3.76e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 LSGGERQRVWIAMTLA--QNTPMLF-LDEPTTYL---DIYYQIEILE-LVKElnevyGLTIVMVLH--DInqaIRYSDHI 208
Cdd:COG0178 827 LSGGEAQRVKLASELSkrSTGKTLYiLDEPTTGLhfhDIRKLLEVLHrLVDK-----GNTVVVIEHnlDV---IKTADWI 898
|
90 100
....*....|....*....|....
gi 446325904 209 IVM------KDGEIVTKGNPNDVI 226
Cdd:COG0178 899 IDLgpeggdGGGEIVAEGTPEEVA 922
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-225 |
4.81e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 132 DKPIYALSGGERQRVWIAMTL-AQNTPMLF-LDEPTTYL---DIYYQIEILELVKELnevyGLTIVMVLHDiNQAIRYSD 206
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGLhqrDNRRLINTLKRLRDL----GNTLIVVEHD-EDTIRAAD 557
|
90 100
....*....|....*....|....*
gi 446325904 207 HIIVM------KDGEIVTKGNPNDV 225
Cdd:TIGR00630 558 YVIDIgpgageHGGEVVASGTPEEI 582
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-226 |
5.96e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 133 KPIYALSGGERQRVWIAMTL--AQNTPMLF-LDEPTTYL---DIYYQIEILELVKELnevyGLTIVMVLHDINqAIRYSD 206
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlaPSKKPTLYvLDEPTTGLhthDIKALIYVLQSLTHQ----GHTVVIIEHNMH-VVKVAD 879
|
90 100
....*....|....*....|....*.
gi 446325904 207 HIIVM------KDGEIVTKGNPNDVI 226
Cdd:PRK00635 880 YVLELgpeggnLGGYLLASCSPEELI 905
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-231 |
1.16e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFS-YDNVTNRLKSVssEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:PRK10938 4 LQISQGTFRlSDTKTLQLPSL--TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 VHQQNEApaDITVEKLISFGRMPYKNIFSPQTDEDR-EAIERALVCTNLQSKRDKpiYaLSGGERQRVWIAMTLAQNTPM 158
Cdd:PRK10938 82 EWQRNNT--DMLSPGEDDTGRTTAEIIQDEVKDPARcEQLAQQFGITALLDRRFK--Y-LSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325904 159 LFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMV 231
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALV 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-169 |
1.25e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKeFARKLAVV 80
Cdd:PRK13540 2 LDVIELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-YQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 81 HQQNEAPADITVEKlisfgrmpyKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLF 160
Cdd:PRK13540 80 GHRSGINPYLTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
....*....
gi 446325904 161 LDEPTTYLD 169
Cdd:PRK13540 151 LDEPLVALD 159
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-228 |
1.55e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKaiseykpkefARKLAVVHQQNeapaditvEKLI 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLN--------GQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 97 SFGRMPYKNIFSPQTDED-REAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIE 175
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446325904 176 ILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVTKGNPNDVITE 228
Cdd:PRK13545 182 CLDKMNEFKE-QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
27-122 |
1.87e-05 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 44.29 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMS-----------RNHAPSSGEV-ILDGkaisEYKPKEFARKLAVVHQQNEAPADITVEK 94
Cdd:pfam13481 33 GGLGLLAGAPGTGKTTLALDLAaavatgkpwlgGPRVPEQGKVlYVSA----EGPADELRRRLRAAGADLDLPARLLFLS 108
|
90 100
....*....|....*....|....*...
gi 446325904 95 LISFGRMPYKNIFSPQTDEDREAIERAL 122
Cdd:pfam13481 109 LVESLPLFFLDRGGPLLDADVDALEAAL 136
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-74 |
2.35e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 1 MEIKNVTFSYDNvTNRLKSVSSEIEIGKITTIIGPNGCGKSTLLSVMS--RNHAPSSGEVILDGKAISEYKPKEFA 74
Cdd:PRK09580 2 LSIKDLHVSVED-KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRA 76
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-169 |
3.26e-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: 45.00 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 27 GKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAIseykpkefARKLAVVHQQ-NEAPADITVEKLISfGR---MP 102
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTNISDVHQNmGYCPQFDAIDDLLT-GRehlYL 2035
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325904 103 YKNIFSPQTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-197 |
4.17e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 33 IGPNGCGKSTLLSVMSRNHAPSSGEVILD-GKAISEYKPKEFA--------------RKLAVVHQQNEA----P------ 87
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQFAfeeftvldtvimghTELWEVKQERDRiyalPemseed 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 88 ----ADITVEklisFGRMP-YknifspqTDEDReAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQNTPMLFLD 162
Cdd:PRK15064 113 gmkvADLEVK----FAEMDgY-------TAEAR-AGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190
....*....|....*....|....*....|....*
gi 446325904 163 EPTTYLDIyYQIEILElvKELNEvYGLTIVMVLHD 197
Cdd:PRK15064 181 EPTNNLDI-NTIRWLE--DVLNE-RNSTMIIISHD 211
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-239 |
6.12e-05 |
|
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: 43.45 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVTfsydnVTN--RLKSVssEIEIGK-ITTIIGPNGCGKSTLLSVMSR-------------------NHAPSSGEV 58
Cdd:COG3593 1 MKLEKIK-----IKNfrSIKDL--SIELSDdLTVLVGENNSGKSSILEALRLllgpsssrkfdeedfylgdDPDLPEIEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 59 ILD---------GKAISEYKPKEFARKLAVVHQQ-NEAPADIT--VEKLISFGRMPYKNIFSPQTDEDREAIERALVctN 126
Cdd:COG3593 74 ELTfgsllsrllRLLLKEEDKEELEEALEELNEElKEALKALNelLSEYLKELLDGLDLELELSLDELEDLLKSLSL--R 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 127 LQSKRDKPIYALSGGERQRVWIAMTLA-------QNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLH--D 197
Cdd:COG3593 152 IEDGKELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSE-KPNQVIITTHspH 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446325904 198 INQAIRYSDHIIVMKDGEIVTKGNPNDVITEEMVKAIYGVDV 239
Cdd:COG3593 231 LLSEVPLENIRRLRRDSGGTTSTKLIDLDDEDLRKLLRYLGV 272
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
139-228 |
1.05e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 139 SGGERQRVWIAMTLAQNTPMLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDINQAIRYSDHIIVMKDGEIVT 218
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
90
....*....|
gi 446325904 219 KGNPNDVITE 228
Cdd:NF000106 225 DGKVDELKTK 234
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-46 |
1.65e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.23 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|
gi 446325904 18 KSVSS-EIEIGKITTIIGPNGCGKSTLLSV 46
Cdd:COG4637 11 KSLRDlELPLGPLTVLIGANGSGKSNLLDA 40
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-213 |
2.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 LSGGERQ------RVWIAMTLAQN------TPMLFLDEPTTYLDIYYQIEILELVKELNEVYGLTIVMVLHDiNQAIRYS 205
Cdd:PRK02224 782 LSGGERAlfnlslRCAIYRLLAEGiegdapLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHD-DELVGAA 860
|
....*....
gi 446325904 206 DHII-VMKD 213
Cdd:PRK02224 861 DDLVrVEKD 869
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
22-214 |
3.65e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.72 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 22 SEIEIGKITTIIGPNGCGKSTLLSVMSrnhapssgeVILDGKAISEYKpkefARKLAVVHQQNEAPADITVEKLISFGRm 101
Cdd:cd03279 23 TGLDNNGLFLICGPTGAGKSTILDAIT---------YALYGKTPRYGR----QENLRSVFAPGEDTAEVSFTFQLGGKK- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 102 pYKNIFSPQTDEDreAIERALVCTnlQSKRDK----PIYALSGGERQRVWIAMTLA-----QNTP-----MLFLDEPTTY 167
Cdd:cd03279 89 -YRVERSRGLDYD--QFTRIVLLP--QGEFDRflarPVSTLSGGETFLASLSLALAlsevlQNRGgarleALFIDEGFGT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446325904 168 LD---IYYQIEILELVKELNEVygltIVMVLHDINQAIRYSDHIIVMKDG 214
Cdd:cd03279 164 LDpeaLEAVATALELIRTENRM----VGVISHVEELKERIPQRLEVIKTP 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-224 |
5.07e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 132 DKPIYALSGGERQRVWIAMTLAQNTP--MLFLDEPTTYLDIYYQIEILELVKELNEvYGLTIVMVLHDiNQAIRYSDHII 209
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRD-QGNTVLLVEHD-EQMISLADRII 548
|
90 100
....*....|....*....|.
gi 446325904 210 VMK------DGEIVTKGNPND 224
Cdd:PRK00635 549 DIGpgagifGGEVLFNGSPRE 569
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-234 |
6.43e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPSSGEVILDGKAISEYKPKEFARKLAVVHQQneaPA--DITVEk 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQD---PVlfDGTVR- 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 95 lisfgrmpyKNIfSPQTDEDREAIERALVCTNLQSK---RDKPIYA--LSGGER----QRVWIAMT---LAQNTPMLFLD 162
Cdd:PTZ00243 1402 ---------QNV-DPFLEASSAEVWAALELVGLRERvasESEGIDSrvLEGGSNysvgQRQLMCMAralLKKGSGFILMD 1471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446325904 163 EPTTYLDIYYQIEILELVKELNEVYglTIVMVLHDINQAIRYsDHIIVMKDGEIVTKGNPNDV------ITEEMVKAI 234
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELvmnrqsIFHSMVEAL 1546
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-183 |
7.90e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.98 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 1 MEIKNVT----FSYDNVTNRLKSVSseieigKITTIIGPNGCGKSTLLS---------------------VMSRNHAPSS 55
Cdd:COG3950 1 MRIKSLTienfRGFEDLEIDFDNPP------RLTVLVGENGSGKTTLLEaialalsgllsrlddvkfrklLIRNGEFGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 56 GEVIL-----------DGKAISEYKPKEFARKLAVVHQQNEAPADITVEKLISFGRMPYKNIFSPQTDEDREAIERALVC 124
Cdd:COG3950 75 AKLILyygtsrllldgPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 125 -----TNLQSKRDK-------------PIYALSGGERQRV----WIAMTLAQNTPML----------FLDEPTTYLDIYY 172
Cdd:COG3950 155 llpdfKDIRIDRDPgrlvildkngeelPLNQLSDGERSLLalvgDLARRLAELNPALenplegegivLIDEIDLHLHPKW 234
|
250
....*....|.
gi 446325904 173 QIEILELVKEL 183
Cdd:COG3950 235 QRRILPDLRKI 245
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-226 |
2.50e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 138 LSGGERQRVWIAMTL-AQNTPMLF-LDEPTTYL---DIYYQIEILELVKELnevyGLTIVMVLHDiNQAIRYSDHIIvmk 212
Cdd:COG0178 486 LSGGEAQRIRLATQIgSGLVGVLYvLDEPSIGLhqrDNDRLIETLKRLRDL----GNTVIVVEHD-EDTIRAADYII--- 557
|
90 100
....*....|....*....|...
gi 446325904 213 D---------GEIVTKGNPNDVI 226
Cdd:COG0178 558 DigpgagehgGEVVAQGTPEEIL 580
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-169 |
3.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446325904 132 DKPIYALSGGERQ------RVWIAMTLAQNTPMLFLDEPTTYLD 169
Cdd:PRK03918 783 ERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLD 826
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
23-44 |
3.66e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.03 E-value: 3.66e-03
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
23-169 |
4.07e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.44 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 23 EIEIGK-ITTIIGPNGCGKST----LLSVM----SRN-HAPSSGEVILDGKaiSEYKPKEFA----------RKLAVVHQ 82
Cdd:cd03278 17 TIPFPPgLTAIVGPNGSGKSNiidaIRWVLgeqsAKSlRGEKMSDVIFAGS--ETRKPANFAevtltfdnsdGRYSIISQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 83 QneapadiTVEKLISfgrMPyknifspqtdedreaieralvctnlqSKRDKPIYALSGGERQRVWIAMTLA----QNTPM 158
Cdd:cd03278 95 G-------DVSEIIE---AP--------------------------GKKVQRLSLLSGGEKALTALALLFAifrvRPSPF 138
|
170
....*....|.
gi 446325904 159 LFLDEPTTYLD 169
Cdd:cd03278 139 CVLDEVDAALD 149
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-70 |
4.36e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 37.25 E-value: 4.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNH--APSSGEVILDGKAISEYKP 70
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS 101
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
1-44 |
5.58e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 5.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446325904 1 MEIKNVtFSYDNVTnrlksvsseIEIGK-ITTIIGPNGCGKSTLL 44
Cdd:pfam13476 1 LTIENF-RSFRDQT---------IDFSKgLTLITGPNGSGKTTIL 35
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
23-41 |
5.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 37.99 E-value: 5.70e-03
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
31-79 |
7.27e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 36.80 E-value: 7.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446325904 31 TIIGPNGCGKSTLLSVMSRN-HAPSSGEVILDGKAISEYKPKEFARKLAV 79
Cdd:cd04170 3 ALVGHSGSGKTTLAEALLYAtGAIDRLGRVEDGNTVSDYDPEEKKRKMSI 52
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-165 |
8.14e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.41 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 20 VSSEIEIGKITTIIGPNGCGKST-------LLsvmsrnhAPSSGEVILDGKAISeykpkefARKLAV------------- 79
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTtmkmltgLL-------PASEGEAWLFGQPVD-------AGDIATrrrvgymsqafsl 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325904 80 -----VHQQNEAPAditveKLisFgRMPyknifspqTDEDREAIERALVCTNLQSKRDKPIYALSGGERQRVWIAMTLAQ 154
Cdd:NF033858 351 ygeltVRQNLELHA-----RL--F-HLP--------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIH 414
|
170
....*....|.
gi 446325904 155 NTPMLFLDEPT 165
Cdd:NF033858 415 KPELLILDEPT 425
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
17-54 |
8.44e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 36.47 E-value: 8.44e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446325904 17 LKSVSSEIEIGKITTIIGPNGCGKSTLLSVMSRNHAPS 54
Cdd:pfam03215 35 LDAMFLENAKHRILLISGPSGCGKSTVIKELSKELGPK 72
|
|
| |
