|
Name |
Accession |
Description |
Interval |
E-value |
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-288 |
0e+00 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 501.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNL 80
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK13634 81 KPLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2119195095 241 LELGLDVPEVVGLQLKIEEAFNTKFSKISLSEEELAEMVAEFMERGGT 288
Cdd:PRK13634 241 EAIGLDLPETVKFKRALEEKFGISFPKPCLTLEELAHEVVQLLRKGGH 288
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-281 |
1.14e-166 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 463.08 E-value: 1.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeKNLKG 82
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKK-KKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:TIGR04521 80 LRKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEK 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 2119195095 243 LGLDVPEVVGLQLKIEEAfNTKFSKISLSEEELAEMVAE 281
Cdd:TIGR04521 240 IGLDVPEITELARKLKEK-GLPVPKDPLTVEEAADEILK 277
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-242 |
1.77e-118 |
|
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: 339.31 E-value: 1.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:COG1122 1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT----KKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:COG1122 73 LRRKVGLVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-259 |
1.87e-118 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 341.26 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagRKEKNL 80
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLP-EEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:PRK13637 79 SDIRKKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET 238
|
250 260
....*....|....*....|
gi 2119195095 240 LLELGLDVPEVVGLQLKIEE 259
Cdd:PRK13637 239 LESIGLAVPQVTYLVRKLRK 258
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-279 |
8.43e-115 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 331.71 E-value: 8.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNL 80
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFL 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 2119195095 241 LELGLDVPEVVGLQLKIEEAfNTKFSKISLSEEELAEMV 279
Cdd:PRK13649 240 EEKQLGVPKITKFAQRLADR-GISFSSLPITIEEFREVL 277
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-284 |
3.73e-111 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 322.88 E-value: 3.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNL 80
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK13646 81 RPVRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2119195095 241 LELGLDVPEVVGLQLKIEEAFNTKFSKISLSEEELAEMVAEFME 284
Cdd:PRK13646 241 ADWHIGLPEIVQLQYDFEQKYQTKLKDIALTEEEFVSLYKEWQH 284
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-286 |
4.28e-108 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 315.23 E-value: 4.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNL 80
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSlHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2119195095 241 LELGLDVPEVVGLQLKIEEAfNTKFSKISLSEEELAEMVAEFMERG 286
Cdd:PRK13641 240 KKHYLDEPATSRFASKLEKG-GFKFSEMPLTIDELVDGIKNNLKGG 284
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-277 |
9.27e-105 |
|
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: 305.89 E-value: 9.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrKEKNLKG 82
Cdd:TIGR04520 1 IEVENVSFSYPES---EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL---DEENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:TIGR04520 75 IRKKVGMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLKE 232
|
250 260 270
....*....|....*....|....*....|....*
gi 2119195095 243 LGLDVPEVVGLQLKIEEAfNTKFSKISLSEEELAE 277
Cdd:TIGR04520 233 IGLDVPFITELAKALKKR-GIPLPPDILTEEELVD 266
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-287 |
1.84e-94 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 280.47 E-value: 1.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKG 82
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2119195095 243 LGLDVPEVVGLQLKIEEAFNTKFSKISLSEEELAEMVAEFMERGG 287
Cdd:PRK13643 241 HELGVPKATHFADQLQKTGAVTFEKLPITRAELVTLLTSLSVNSG 285
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-284 |
5.75e-94 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 279.66 E-value: 5.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI----RAGRK 76
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 77 E----------------KNLKGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILE 140
Cdd:PRK13651 81 EkvleklviqktrfkkiKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 141 KSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMH 220
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 221 QGEVFTKGTPEQIFSNPKALLELGLDVPEVVGLQLKIEEAfNTKFSKISlSEEELAEMVAEFME 284
Cdd:PRK13651 240 DGKIIKDGDTYDILSDNKFLIENNMEPPKLLNFVNKLEKK-GIDVPKVT-SIEELASEINMYLE 301
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-223 |
1.29e-89 |
|
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: 265.10 E-value: 1.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKGV 83
Cdd:cd03225 1 ELKNLSFSYPDG---ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT----KLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 REKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAME 163
Cdd:cd03225 74 RRKVGLVFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 164 PEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-284 |
1.22e-86 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 260.71 E-value: 1.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAG-RKEKNL 80
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK13645 86 KRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2119195095 241 LELGLDVPEVVGLQLKIEEAFNTKFSKISLSEEELAEMVAEFME 284
Cdd:PRK13645 246 TKIEIDPPKLYQLMYKLKNKGIDLLNKNIRTIEEFAKELAKVLK 289
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-242 |
6.48e-84 |
|
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: 260.99 E-value: 6.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRaGRKEKNLKG 82
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT-KLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFE-ETVEKDIMFGPMNLGV-TEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPrMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP--- 237
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPqhp 499
|
....*..
gi 2119195095 238 --KALLE 242
Cdd:COG1123 500 ytRALLA 506
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-287 |
2.44e-82 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 250.92 E-value: 2.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRA--------- 73
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 74 ---GRKEKNLKGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQ 150
Cdd:PRK13631 102 npySKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSlHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTP 230
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 231 EQIFSNPKALLELGLDVPEVVGLqlkIEE--AFNTKFSKISLSE----EELAEMVAEFMERGG 287
Cdd:PRK13631 261 YEIFTDQHIINSTSIQVPRVIQV---INDliKKDPKYKKLYQKQprtiEQLADAINEFIKGGK 320
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-277 |
4.28e-80 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 243.38 E-value: 4.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:PRK13635 6 IRVEHISFRYPDA---ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL----SEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13635 79 VRRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
250 260 270
....*....|....*....|....*....|....*
gi 2119195095 243 LGLDVPEVVGLQLKIEEAfNTKFSKISLSEEELAE 277
Cdd:PRK13635 237 IGLDVPFSVKLKELLKRN-GILLPNTYLTMESLVD 270
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-281 |
1.14e-79 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 242.69 E-value: 1.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQ-ADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrKEKNLK 81
Cdd:PRK13633 5 IKCKNVSYKYEsNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS---DEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:PRK13633 82 DIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIFSNPKALL 241
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2119195095 242 ELGLDVPEVVglqlkiEEAFNTKFSKISLSEEELA--EMVAE 281
Cdd:PRK13633 240 KIGLDVPQVT------ELAYELKKEGVDIPSDILTidEMVNE 275
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-253 |
1.49e-73 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 226.88 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagRKEKNLKG 82
Cdd:PRK13639 2 LETRDLKYSYPDGT----EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--YDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13639 76 VRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRK 233
|
250
....*....|.
gi 2119195095 243 LGLDVPEVVGL 253
Cdd:PRK13639 234 ANLRLPRVAHL 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-286 |
1.59e-71 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 221.53 E-value: 1.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:PRK13647 5 IEVEDLHFRYKDGTK----ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV----NAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13647 77 VRSKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEqIFSNPKALLE 242
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDIVEQ 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2119195095 243 LGLDVPEVVGLQLKIEEafnTKFSKISLSEEELAEMVAEFMERG 286
Cdd:PRK13647 234 AGLRLPLVAQIFEDLPE---LGQSKLPLTVKEAVQIIRKLLTKG 274
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-277 |
2.19e-70 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 218.32 E-value: 2.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqadSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:PRK13632 8 IKVENVSFSY---PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEK 238
|
250 260 270
....*....|....*....|....*....|....*
gi 2119195095 243 LGLDVPEVVGLQLKIEEAfntkfsKISLSEEELAE 277
Cdd:PRK13632 239 AKIDSPFIYKLSKKLKGI------DPTYNEEELIE 267
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-248 |
1.37e-68 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 214.28 E-value: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:PRK13652 4 IETRDLCYSYSGS----KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI----TKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13652 76 VRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
....*.
gi 2119195095 243 LGLDVP 248
Cdd:PRK13652 235 VHLDLP 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-240 |
1.51e-67 |
|
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: 218.62 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPT---KGSVLIGSREIRagrkEKN 79
Cdd:COG1123 5 LEVRDLSVRYPGG---DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL----ELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 80 LKGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:COG1123 78 EALRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
.
gi 2119195095 240 L 240
Cdd:COG1123 237 L 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-259 |
2.99e-66 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 208.50 E-value: 2.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQaDSpfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSvliGSREIRAGRK--EKNL 80
Cdd:PRK13640 6 VEFKHVSFTYP-DS--KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP---NSKITVDGITltAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK13640 80 WDIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYI-DSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAArYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
250
....*....|....*....
gi 2119195095 241 LELGLDVPEVVGLQLKIEE 259
Cdd:PRK13640 238 KEIGLDIPFVYKLKNKLKE 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-271 |
4.87e-65 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 205.08 E-value: 4.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKekNLKG 82
Cdd:PRK13636 6 LKVEELNYNYSDGTH----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK--GLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRK 238
|
250 260
....*....|....*....|....*....
gi 2119195095 243 LGLDVPEVVGLQLKIEEAFNTKFSKISLS 271
Cdd:PRK13636 239 VNLRLPRIGHLMEILKEKDGFVFDELDLT 267
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-248 |
6.93e-64 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 201.90 E-value: 6.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFerlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKG 82
Cdd:PRK13648 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD----DNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13648 81 LRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERA-DYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
....*.
gi 2119195095 243 LGLDVP 248
Cdd:PRK13648 239 IGLDLP 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-285 |
8.23e-64 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 201.88 E-value: 8.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:PRK13650 5 IEVKNLTFKYKEDQ--EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL----TEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13650 79 IRHKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAArYADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2119195095 243 LGLDVPEVVGLQLKI-EEAFNtkFSKISLSEEELAEMVAEFMER 285
Cdd:PRK13650 237 LGLDIPFTTSLVQSLrQNGYD--LPEGYLTEKELEEQLWELISK 278
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-224 |
5.82e-62 |
|
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: 195.02 E-value: 5.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKG 82
Cdd:cd03255 1 IELKNLSKTYGGGG-EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFpeHQLFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:cd03255 80 RRRHIGFVFQS--FNLLPDlTALENVELPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEdAARYADDIVVMHQGEV 224
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-234 |
8.25e-61 |
|
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: 192.89 E-value: 8.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKG 82
Cdd:COG1127 6 IEVRNLTKSFG-----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI-TGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEE-TVEKDIMFgPM--NLGVTEKEAKTRARAAINLVGLPEeILEKSPFDLSGGQMRRVAIAGV 159
Cdd:COG1127 80 LRRRIGMLFQGG--ALFDSlTVFENVAF-PLreHTDLSEAEIRELVLEKLELVGLPG-AADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-224 |
3.42e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 191.02 E-value: 3.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKG 82
Cdd:COG1136 5 LELRNLTKSYGTGEG-EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VR-EKVGIVFQFpeHQLFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG1136 83 LRrRHIGFVFQF--FNLLPElTALENVALPLLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSmEDAARYADDIVVMHQGEV 224
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-273 |
3.20e-59 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 190.20 E-value: 3.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsREIRAGRKEKnLKG 82
Cdd:PRK13644 2 IRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSK-LQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13644 75 IRKLVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDaARYADDIVVMHQGEVFTKGTPEQIFSNPkALLE 242
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV-SLQT 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 2119195095 243 LGLDVPEVVGL--QLK---IEEAFNTKFSKISLSEE 273
Cdd:PRK13644 231 LGLTPPSLIELaeNLKmhgVVIPWENTSSPSSFAEE 266
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-238 |
4.50e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 188.28 E-value: 4.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIraGRKEKNLKG 82
Cdd:COG1126 2 IEIENLHKSFG-----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL--TDSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPeHQlfeeTVEKDIMFGPMN-LGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIA 157
Cdd:COG1126 75 LRRKVGMVFQqfnlFP-HL----TVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
.
gi 2119195095 238 K 238
Cdd:COG1126 228 Q 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-209 |
6.29e-58 |
|
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: 183.78 E-value: 6.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKekNLKGVREKVGIVFQFPEHQLFEE 101
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRK--GLLERRQRVGLVFQDPDDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVERRVREALTAVGA-SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180 190
....*....|....*....|....*....|
gi 2119195095 182 KEIMDLfysLHKKRNLSTVLV--THSMEDA 209
Cdd:TIGR01166 164 EQMLAI---LRRLRAEGMTVVisTHDVDLA 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-238 |
2.13e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 187.61 E-value: 2.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeknlK 81
Cdd:COG3842 5 ALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV---------T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GV---REKVGIVFQ----FPeHqLfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRV 154
Cdd:COG3842 71 GLppeKRNVGMVFQdyalFP-H-L---TVAENVAFGLRMRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY 224
|
....
gi 2119195095 235 SNPK 238
Cdd:COG3842 225 ERPA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-234 |
1.39e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 181.93 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGrKEKNLKG 82
Cdd:cd03261 1 IELRGLTKSFG-----GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGL-SEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEE-TVEKDIMFgP--MNLGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGV 159
Cdd:cd03261 75 LRRRMGMLFQSG--ALFDSlTVFENVAF-PlrEHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-238 |
1.47e-56 |
|
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: 181.63 E-value: 1.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQaDSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKG 82
Cdd:cd03258 2 IELKNVSKVFG-DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL-TLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpeH-QLFE-ETVEKDIMFgPMNL-GVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:cd03258 80 ARRRIGMIFQ---HfNLLSsRTVFENVAL-PLEIaGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-237 |
3.86e-56 |
|
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: 180.96 E-value: 3.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR----EQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGL-PEEILEKSPFDLSGGQMRRVAIA 157
Cdd:cd03295 73 LRRKIGYVIQqiglFP-HM----TVEENIALVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-233 |
1.47e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkg 82
Cdd:COG1131 1 IEVRGLTKRYG-----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEhqLFEE-TVEKDI-MFGPMNlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG1131 71 VRRRIGYVPQEPA--LYPDlTVRENLrFFARLY-GLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-219 |
1.53e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 179.90 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkeknlkG 82
Cdd:COG1116 8 LELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFE-ETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:COG1116 78 PGPDRGVVFQ--EPALLPwLTVLDNVALGLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVM 219
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-219 |
3.44e-55 |
|
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: 177.66 E-value: 3.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkeknlkG 82
Cdd:cd03293 1 LEVRNVSKTYGGGGG-AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFE-ETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:cd03293 71 PGPDRGYVFQ--QDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVM 219
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-243 |
4.47e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 178.33 E-value: 4.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeKNLKG 82
Cdd:COG3638 3 LELRNLSKRYPGGTP----ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG-RALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFGpmNLGVT----------EKEAKTRARAAINLVGLPEEILEKSpfD-LSGGQ 150
Cdd:COG3638 78 LRRRIGMIFQ--QFNLVPRlSVLTNVLAG--RLGRTstwrsllglfPPEDRERALEALERVGLADKAYQRA--DqLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTP 230
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
250
....*....|...
gi 2119195095 231 EQIfsNPKALLEL 243
Cdd:COG3638 232 AEL--TDAVLREI 242
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-224 |
9.84e-55 |
|
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: 176.93 E-value: 9.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKG 82
Cdd:cd03257 2 LEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL-LKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQL-FEETVEKDIMFGPMNLGVTEKEAKTRARAAINL--VGLPEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:cd03257 80 RRKEIQMVFQDPMSSLnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-247 |
9.98e-55 |
|
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: 177.54 E-value: 9.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRA-GRKEknlk 81
Cdd:COG1120 2 LEAENLSVGYG-----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 gVREKVGIVFQFPEHQlFEETVEKDIMFG--PM--NLGVTEKEAKTRARAAINLVGLPEeiLEKSPFD-LSGGQMRRVAI 156
Cdd:COG1120 73 -LARRIAYVPQEPPAP-FGLTVRELVALGryPHlgLFGRPSAEDREAVEEALERTGLEH--LADRPVDeLSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFsN 236
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-T 227
|
250
....*....|..
gi 2119195095 237 PKALLEL-GLDV 247
Cdd:COG1120 228 PELLEEVyGVEA 239
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-242 |
4.17e-54 |
|
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: 176.15 E-value: 4.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeknlKG 82
Cdd:COG1124 2 LEVRNLSVSYGQGGR-RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR----KA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPE---HQLFeeTVEkDIMFGPMNL-GVTEKEAktRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:COG1124 77 FRRRVQMVFQDPYaslHPRH--TVD-RILAEPLRIhGLPDREE--RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQG---EVFTKGTPEQIFS 235
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGrivEELTVADLLAGPK 231
|
....*....
gi 2119195095 236 NP--KALLE 242
Cdd:COG1124 232 HPytRELLA 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-224 |
1.45e-53 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 173.47 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeKNLKG 82
Cdd:cd03259 1 LELKGLSKTYGSV-----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV------TGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:cd03259 70 ERRNIGMVFQdyalFP-HL----TVAENIAFGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-282 |
5.39e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.04 E-value: 5.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRY-QADSPFErlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLK 81
Cdd:COG1135 2 IELENLSKTFpTKGGPVT--ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpeH-QLFEE-TVEKDIMFgPMNL-GVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAG 158
Cdd:COG1135 79 AARRKIGMIFQ---HfNLLSSrTVAENVAL-PLEIaGVPKAEIRKRVAELLELVGLSDKA-DAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP- 237
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPq 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 238 ----KALLE--LGLDVPEVVGLQLKIEEAFNT----KFSKISLSEEELAEMVAEF 282
Cdd:COG1135 234 seltRRFLPtvLNDELPEELLARLREAAGGGRlvrlTFVGESADEPLLSELARRF 288
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-233 |
1.92e-52 |
|
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: 171.21 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLK-----PTKGSVLIGSREIRAgrKE 77
Cdd:cd03260 1 IELRDLNVYYG-----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYD--LD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 KNLKGVREKVGIVFQFPehQLFEETVEKDIMFGPMNLGV-TEKEAKTRARAAINLVGLPEEILEK-SPFDLSGGQMRRVA 155
Cdd:cd03260 74 VDVLELRRRVGMVFQKP--NPFPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 156 IAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-238 |
5.60e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.41 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkekNL 80
Cdd:COG1118 1 MSIEVRNISKRFGSFT-----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-----NL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KgVRE-KVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEeiLEKS-PFDLSGGQMRRV 154
Cdd:COG1118 71 P-PRErRVGFVFQhyalFP-HM----TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG--LADRyPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
....
gi 2119195095 235 SNPK 238
Cdd:COG1118 223 DRPA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-223 |
9.57e-51 |
|
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: 165.05 E-value: 9.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagRKEKNLKG 82
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--DLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFGpmnlgvtekeaktraraainlvglpeeilekspfdLSGGQMRRVAIAGVLA 161
Cdd:cd03229 74 LRRRIGMVFQ--DFALFPHlTVLENIALG-----------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-233 |
1.88e-50 |
|
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: 166.20 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqadsPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgRKEKNLKG 82
Cdd:cd03256 1 IEVENLSKTY----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINK-LKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFGPMN--------LGVTEKEAKTRARAAINLVGLPEEILEKSPfDLSGGQMRR 153
Cdd:cd03256 76 LRRQIGMIFQ--QFNLIERlSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRAD-QLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-224 |
2.29e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 165.61 E-value: 2.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKG 82
Cdd:COG2884 2 IRFENVSKRYPGG----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL-SRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFgPMN-LGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG2884 77 LRRRIGVVFQ--DFRLLPDrTVYENVAL-PLRvTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLV-THSMEDAARYADDIVVMHQGEV 224
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIaTHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-224 |
5.40e-50 |
|
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: 164.24 E-value: 5.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqadSPFERLaiSDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIraGRKEKNLKG 82
Cdd:cd03262 1 IEIKNLHKSF---GDFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL--TDDKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFGPMN-LGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGVL 160
Cdd:cd03262 74 LRQKVGMVFQ--QFNLFPHlTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-238 |
8.69e-50 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 165.21 E-value: 8.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNAL--LKP---TKGSVLIGSREIRAgrKE 77
Cdd:COG1117 12 IEVRNLNVYYG-----DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYD--PD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 KNLKGVREKVGIVFQFPehQLFEETVEKDIMFGPMNLGVTEK-EAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMRR 153
Cdd:COG1117 85 VDVVELRRRVGMVFQKP--NPFPKSIYDNVAYGLRLHGIKSKsELDEIVEESLRKAALWDEVkdrLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
....*
gi 2119195095 234 FSNPK 238
Cdd:COG1117 241 FTNPK 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-281 |
9.97e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 165.65 E-value: 9.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLaiSDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKG 82
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQL--NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----ENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEeILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13642 79 LRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIFSNPKALLE 242
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 2119195095 243 LGLDVPEVVGLqLKIEEAFNTKFSKISLSEEELAEMVAE 281
Cdd:PRK13642 237 IGLDVPFSSNL-MKDLRKNGFDLPEKYLSEDELVELLAD 274
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-237 |
2.08e-49 |
|
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: 164.74 E-value: 2.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 21 LAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQ----FPeH 96
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQsfalLP-H 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 QlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGL 176
Cdd:cd03294 117 R----TVLENVAFGLEVQGVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 177 DPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-242 |
2.32e-49 |
|
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: 166.00 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKP---TKGSVLIGSREIrAGRKEKNLKGVREK-VGIVFQFP--- 94
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDL-LKLSEKELRKIRGReIQMIFQDPmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 -------EHQLfEETVEKdimfgpmNLGVTEKEAKTRARAAINLVGL--PEEILEKSPFDLSGGQMRRVAIAGVLAMEPE 165
Cdd:COG0444 99 lnpvmtvGDQI-AEPLRI-------HGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 166 VIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP-----KAL 240
Cdd:COG0444 171 LLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPrhpytRAL 250
|
..
gi 2119195095 241 LE 242
Cdd:COG0444 251 LS 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-238 |
2.84e-49 |
|
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: 163.28 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQAdspFErlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeknl 80
Cdd:cd03296 1 MSIEVRNVSKRFGD---FV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREK-VGIVFQfpEHQLFEE-TVEKDIMFG----PMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRV 154
Cdd:cd03296 69 VPVQERnVGFVFQ--HYALFRHmTVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....
gi 2119195095 235 SNPK 238
Cdd:cd03296 226 DHPA 229
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-238 |
4.42e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.18 E-value: 4.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:COG1125 2 IEFENVTKRYPDGTV----AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR----DLDPVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGL-PEEILEKSPFDLSGGQMRRVAIA 157
Cdd:COG1125 74 LRRRIGYVIQqiglFP-HM----TVAENIATVPRLLGWDKERIRARVDELLELVGLdPEEYRDRYPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
.
gi 2119195095 238 K 238
Cdd:COG1125 229 A 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-228 |
6.67e-47 |
|
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: 155.29 E-value: 6.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRA-GRKEknlkg 82
Cdd:cd03214 1 EVENLSVGYG-----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpehqlfeetvekdimfgpmnlgvtekeaktraraAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:cd03214 71 LARKIAYVPQ-----------------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-243 |
1.45e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeknlkg 82
Cdd:COG1121 7 IELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vreKVGIVFQFPEHQL-F----EETVEkdiM--FGPMNL-GVTEKEAKTRARAAINLVGLPEeiLEKSPF-DLSGGQMRR 153
Cdd:COG1121 76 ---RIGYVPQRAEVDWdFpitvRDVVL---MgrYGRRGLfRRPSRADREAVDEALERVGLED--LADRPIgELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTkGTPEQI 233
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEV 225
|
250
....*....|
gi 2119195095 234 FSnPKALLEL 243
Cdd:COG1121 226 LT-PENLSRA 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-238 |
2.31e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 159.08 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-RAGRKEKNl 80
Cdd:COG3839 3 SLELENVSKSYGGVE-----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 kgvrekVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAI 156
Cdd:COG3839 77 ------IAMVFQsyalYP-HM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSN 236
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDR 224
|
..
gi 2119195095 237 PK 238
Cdd:COG3839 225 PA 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-238 |
3.17e-46 |
|
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: 155.29 E-value: 3.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKnlKGVREKVGIVFQFPehQLFEE 101
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPH--EIARLGIGRTFQIP--RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 -TVEKDIM----------FGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:cd03219 90 lTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 171 EPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:cd03219 169 EPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
6.52e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkg 82
Cdd:COG4619 1 LELEGLSFRVG-----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEkDIMFGPMNLGvTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:COG4619 72 WRRQVAYVPQEP--ALWGGTVR-DNLPFPFQLR-ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-230 |
1.52e-45 |
|
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: 153.04 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqadSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkg 82
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFpeHQLFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:cd03263 73 ARQSLGYCPQF--DALFDElTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFysLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTP 230
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-233 |
1.72e-45 |
|
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: 153.61 E-value: 1.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqadsPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnLKG 82
Cdd:TIGR02315 2 LEVENLSKVY----PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKK-LRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFG--------PMNLGVTEKEAKTRARAAINLVGLPEEILEKSPfDLSGGQMRR 153
Cdd:TIGR02315 77 LRRRIGMIFQ--HYNLIERlTVLENVLHGrlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRAD-QLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-223 |
4.11e-45 |
|
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: 150.23 E-value: 4.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:cd03228 1 IEFKNVSFSYPGR---PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR----DLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDImfgpmnlgvtekeaktraraainlvglpeeilekspfdLSGGQMRRVAIAGVLAM 162
Cdd:cd03228 74 LRKNIAYVPQDP--FLFSGTIRENI--------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEdAARYADDIVVMHQGE 223
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-238 |
9.18e-45 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 151.24 E-value: 9.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeKNLKG 82
Cdd:cd03300 1 IELENVSKFYGGF-----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI------TNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:cd03300 70 HKRPVNTVFQnyalFP-HL----TVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-272 |
1.46e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 152.08 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 10 YRYQaDSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKekNLKGVREKVGI 89
Cdd:PRK13638 9 FRYQ-DEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKR--GLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 90 VFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGlpEEILEKSPFD-LSGGQMRRVAIAGVLAMEPEVIV 168
Cdd:PRK13638 82 VFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD--AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 169 LDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLELGLDVP 248
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQP 238
|
250 260 270
....*....|....*....|....*....|.
gi 2119195095 249 EVV------GLQL-KIEEAFNTKFSKISLSE 272
Cdd:PRK13638 239 WLVklhtqlGLPLcKTETEFFHRMQKCAFRE 269
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-243 |
3.29e-44 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 159.23 E-value: 3.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:COG2274 473 DIELENVSFRYPGDSP---PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR----QIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKEaktrARAAINLVGLPEEIlEKSP--FD---------LSGGQ 150
Cdd:COG2274 546 SLRRQIGVVLQ--DVFLFSGTIRENITLG--DPDATDEE----IIEAARLAGLHDFI-EALPmgYDtvvgeggsnLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTP 230
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTH 693
|
250
....*....|...
gi 2119195095 231 EQIFSNPKALLEL 243
Cdd:COG2274 694 EELLARKGLYAEL 706
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-239 |
1.65e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 148.96 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRK---------EKNLKGVREKVGIVFQfpEH 96
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadKNQLRLLRTRLTMVFQ--HF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 QLFEE-TVEKDIMFGPMN-LGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:PRK10619 102 NLWSHmTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 175 GLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-238 |
5.30e-43 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 150.19 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspFERLAisDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeKNLKG 82
Cdd:TIGR03265 5 LSIDNIRKRFGA---FTALK--DISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI------TRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEiLEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:TIGR03265 74 QKRDYGIVFQ--SYALFPNlTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGS-ERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPA 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-224 |
6.12e-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: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkg 82
Cdd:cd03230 1 IEVRNLSKRYG-----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEE-TVEkdimfgpmnlgvtekeaktraraainlvglpeEILekspfDLSGGQMRRVAIAGVLA 161
Cdd:cd03230 71 VKRRIGYLPEEP--SLYENlTVR--------------------------------ENL-----KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-249 |
6.23e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.95 E-value: 6.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgRKEKNLKG 82
Cdd:PRK11153 2 IELKNISKVFPQGGR-TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA-LSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpeH--QLFEETVEKDIMFgPMNL-GVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:PRK11153 80 ARRQIGMIFQ---HfnLLSSRTVFDNVAL-PLELaGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
|
250
....*....|....*..
gi 2119195095 240 LL-------ELGLDVPE 249
Cdd:PRK11153 235 PLtrefiqsTLHLDLPE 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-238 |
3.38e-42 |
|
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: 144.79 E-value: 3.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeKNLKGVREKVGIVFQfpEHQLFEE- 101
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI------TNLPPEKRDISYVPQ--NYALFPHm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 182 KEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
9.08e-42 |
|
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: 151.07 E-value: 9.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlk 81
Cdd:COG4987 333 SLELEDVSFRYPGA---GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKEaktrARAAINLVGLpEEILEKSP--FD---------LSGGQ 150
Cdd:COG4987 406 DLRRRIAVVPQ--RPHLFDTTLRENLRLA--RPDATDEE----LWAALERVGL-GDWLAALPdgLDtwlgeggrrLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTP 230
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTH 553
|
..
gi 2119195095 231 EQ 232
Cdd:COG4987 554 EE 555
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-238 |
1.52e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 143.23 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSRE--IRAGRKEK 78
Cdd:PRK11124 1 MSIQLNGINCFYGAHQ-----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 79 NLKGVREKVGIVFQfpEHQLFEE-TVEKDIMFGPMN-LGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAI 156
Cdd:PRK11124 76 AIRELRRNVGMVFQ--QYNLWPHlTVQQNLIEAPCRvLGLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQiFSN 236
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQ 230
|
..
gi 2119195095 237 PK 238
Cdd:PRK11124 231 PQ 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-248 |
5.05e-41 |
|
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: 148.68 E-value: 5.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQhlnALLK--PTKGSVLIGSREIrAGRKEKNLKGVREKVGIVFQ--F---- 93
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGL---ALLRliPSEGEIRFDGQDL-DGLSRRALRPLRRRMQVVFQdpFgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 94 PEHqlfeeTVEkDIMFGPMNL---GVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:COG4172 377 PRM-----TVG-QIIAEGLRVhgpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 171 EPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMeDAARY-ADDIVVMHQGEVFTKGTPEQIFSNP-----KALLELG 244
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL-AVVRAlAHRVMVMKDGKVVEQGPTEQVFDAPqhpytRALLAAA 529
|
....
gi 2119195095 245 LDVP 248
Cdd:COG4172 530 PLLE 533
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-232 |
5.16e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 149.14 E-value: 5.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYqadsPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:COG4988 336 SIELEDVSFSY----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS----DLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQFPehQLFEETVEKDIMFGpmNLGVTEKEAktraRAAINLVGLpEEILEKSP--FD---------LSGGQ 150
Cdd:COG4988 408 SWRRQIAWVPQNP--YLFAGTIRENLRLG--RPDASDEEL----EAALEAAGL-DEFVAALPdgLDtplgeggrgLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTP 230
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
..
gi 2119195095 231 EQ 232
Cdd:COG4988 556 EE 557
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-233 |
7.07e-41 |
|
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: 141.53 E-value: 7.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkg 82
Cdd:COG4555 2 IEVENLSKKYG-----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDI-MFGPMNlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG4555 72 ARRQIGVLPD--ERGLYDRlTVRENIrYFAELY-GLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-240 |
8.20e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.05 E-value: 8.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQaDSPFErlaisdVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkg 82
Cdd:COG3840 2 LRLDDLTYRYG-DFPLR------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vReKVGIVFQfpEHQLFEE-TVEKDIMFG--P-MNLGVTEKEaktRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:COG3840 71 -R-PVSMLFQ--ENNLFPHlTVAQNIGLGlrPgLKLTAEQRA---QVEQALERVGL-AGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFS--N 236
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDgeP 222
|
....
gi 2119195095 237 PKAL 240
Cdd:COG3840 223 PPAL 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
26-238 |
9.16e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 141.86 E-value: 9.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIR--AGRK-------EKNLKGVREKVGIVFQ-FP- 94
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkPDRDgelvpadRRQLQRIRTRLGMVFQsFNl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 -EHQlfeeTVEKDIMFGPMN-LGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:COG4598 107 wSHM----TVLENVIEAPVHvLGRPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 173 TAGLDPRGRKEImdlfysLHKKRNLST-----VLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:COG4598 182 TSALDPELVGEV------LKVMRDLAEegrtmLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
1.31e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.92 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSRE--IRAGRKEK 78
Cdd:COG4161 1 MSIQLKNINCFYGSHQ-----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 79 NLKGVREKVGIVFQfpEHQLFEE-TVEKDIMFGPMN-LGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAI 156
Cdd:COG4161 76 AIRLLRQKVGMVFQ--QYNLWPHlTVMENLIEAPCKvLGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEqIFSN 236
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQ 230
|
..
gi 2119195095 237 PK 238
Cdd:COG4161 231 PQ 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-259 |
1.76e-40 |
|
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: 143.70 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQfpEHQLFEE-TV 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQ--EARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 104 EKDIMFGpmnlgvtEKEAKTRAR-----AAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:COG4148 95 RGNLLYG-------RKRAPRAERrisfdEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 179 RGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLELGLDVPEVVgLQLKIE 258
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSV-LEATVA 245
|
.
gi 2119195095 259 E 259
Cdd:COG4148 246 A 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-225 |
2.18e-40 |
|
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: 139.59 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeknlkgv 83
Cdd:cd03235 1 EVEDLTVSYG-----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 reKVGIVFQFPE-HQLFEETVEKDIMFGPMN----LGVTEKEAKTRARAAINLVGLPEeiLEKSPFD-LSGGQMRRVAIA 157
Cdd:cd03235 69 --RIGYVPQRRSiDRDFPISVRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSE--LADRQIGeLSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGEVF 225
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-223 |
2.21e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKGV 83
Cdd:cd00267 1 EIENLSFRYG-----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI----AKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 REKVGIVFQfpehqlfeetvekdimfgpmnlgvtekeaktraraainlvglpeeilekspfdLSGGQMRRVAIAGVLAME 163
Cdd:cd00267 72 RRRIGYVPQ-----------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 164 PEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-232 |
3.31e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.85 E-value: 3.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:COG1132 339 EIEFENVSFSYPGDRP----VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR----DLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKEaktrARAAINLVGLpEEILEKSP--FD---------LSGGQ 150
Cdd:COG1132 411 SLRRQIGVVPQ--DTFLFSGTIRENIRYG--RPDATDEE----VEEAAKAAQA-HEFIEALPdgYDtvvgergvnLSGGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTP 230
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRIVEQGTH 558
|
..
gi 2119195095 231 EQ 232
Cdd:COG1132 559 EE 560
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-238 |
4.69e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.89 E-value: 4.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGR---KEKNL-KGVREKVGIVFQ----FPEHQ 97
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsQQKGLiRQLRQHVGFVFQnfnlFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEETVEkdimfGPMNL-GVTEKEAKTRARAAINLVGLPEEilEKS-PFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAG 175
Cdd:PRK11264 102 VLENIIE-----GPVIVkGEPKEEATARARELLAKVGLAGK--ETSyPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 176 LDPRGRKEIMDLFYSL-HKKRNLstVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK11264 175 LDPELVGEVLNTIRQLaQEKRTM--VIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-224 |
1.78e-39 |
|
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: 137.00 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYqadsPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeknlkgv 83
Cdd:cd03226 1 RIENISFSY----KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 REKVGIVFQFPEHQLFEETVEKDIMFGPMNLGvtekEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAME 163
Cdd:cd03226 70 RKSIGYVMQDVDYQLFTDSVREELLLGLKELD----AGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 164 PEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-237 |
2.48e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.53 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLkg 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQ-----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPehQLfeeTVEKDIMFGPMNL-GVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIA 157
Cdd:PRK09493 75 IRQEAGMVFQqfylFP--HL---TALENVMFGPLRVrGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-242 |
3.27e-39 |
|
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: 143.67 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKS----TVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKGVR-EKVGIVFQF 93
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-LGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 94 P----------EHQLFEetvekdimfgPMNL--GVTEKEAKTRARAAINLVGL--PEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:COG4172 101 PmtslnplhtiGKQIAE----------VLRLhrGLSGAAARARALELLERVGIpdPERRLDAYPHQLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP-- 237
Cdd:COG4172 171 LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPqh 250
|
....*...
gi 2119195095 238 ---KALLE 242
Cdd:COG4172 251 pytRKLLA 258
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-241 |
7.39e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 138.71 E-value: 7.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKGVREKVGIVFQFPehqlFE- 100
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI-TGLSGRELRPLRRRMQMVFQDP----YAs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 ----ETVEKDIMFGPMNLGV-TEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAG 175
Cdd:COG4608 108 lnprMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 176 LDPRGRKEIMDLFYSLHKKRNLSTVLVTHsmeDAA--RY-ADDIVVMHQGEVFTKGTPEQIFSNP-----KALL 241
Cdd:COG4608 188 LDVSIQAQVLNLLEDLQDELGLTYLFISH---DLSvvRHiSDRVAVMYLGKIVEIAPRDELYARPlhpytQALL 258
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-233 |
4.95e-38 |
|
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: 133.65 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkeKNLKG 82
Cdd:cd03265 1 IEVENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehqlfeeTVEkDIMFGPMNL-------GVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVA 155
Cdd:cd03265 71 VRRRIGIVFQDL-------SVD-DELTGWENLyiharlyGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 156 IAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-224 |
8.04e-38 |
|
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: 133.33 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadSPFERLAI-SDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLK 81
Cdd:COG4181 9 IELRGLTKTVG--TGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQ-FpeHQLFEETVEKDIMFgPMNLgVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG4181 87 LRARHVGFVFQsF--QLLPTLTALENVML-PLEL-AGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEV 224
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-224 |
1.45e-37 |
|
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: 132.42 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTyLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQfpEHQLFEE-TV 103
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQ--QYALFPHlNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 104 EKDIMFGPMnlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKE 183
Cdd:cd03297 93 RENLAFGLK--RKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119195095 184 IMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-257 |
6.66e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 134.44 E-value: 6.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 18 FERLAI-SDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-RAGRKEKnlkgvreKVGIVFQfpE 95
Cdd:PRK10851 12 FGRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsRLHARDR-------KVGFVFQ--H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 96 HQLFEE-TVEKDIMFG----PMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:PRK10851 83 YALFRHmTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 171 EPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA--LLELGLDVP 248
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATrfVLEFMGEVN 241
|
250
....*....|...
gi 2119195095 249 ----EVVGLQLKI 257
Cdd:PRK10851 242 rlqgTIRGGQFHV 254
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-232 |
7.98e-37 |
|
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: 130.81 E-value: 7.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:cd03253 1 IEFENVTFAYDP----GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR----EVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKEAKTRARAAInlvglPEEILEKSPFD-----------LSGGQM 151
Cdd:cd03253 73 LRRAIGVVPQ--DTVLFNDTIGYNIRYG--RPDATDEEVIEAAKAAQ-----IHDKIMRFPDGydtivgerglkLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPE 231
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHE 220
|
.
gi 2119195095 232 Q 232
Cdd:cd03253 221 E 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-174 |
2.46e-36 |
|
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: 126.99 E-value: 2.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKGVREKVGIVFQFPehQLF-EE 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD----DERKSLRKEIGYVFQDP--QLFpRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 102 TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPE---EILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-237 |
4.33e-36 |
|
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: 132.16 E-value: 4.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQfpEHQLFEE-TV 103
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQ--EARLFPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 104 EKDIMFGPMNlgVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKE 183
Cdd:TIGR02142 93 RGNLRYGMKR--ARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 184 IMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-260 |
5.97e-36 |
|
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: 130.59 E-value: 5.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 21 LAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkEKNLKGVREKVGIVFQFPehqlfe 100
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-----VREPRKVRRSIGIVPQYA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 eTVEKDI-------MFGPMnLGVTEKEAKTRARAAINLVGLPEEILEKSPFdLSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:TIGR01188 76 -SVDEDLtgrenleMMGRL-YGLPKDEAEERAEELLELFELGEAADRPVGT-YSGGMRRRLDIAASLIHQPDVLFLDEPT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 174 AGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSnpkallELGLDVPEVV-- 251
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR------RLGKDTLESRpr 225
|
250
....*....|
gi 2119195095 252 -GLQLKIEEA 260
Cdd:TIGR01188 226 dIQSLKVEVS 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-238 |
1.26e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 128.42 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLK-----PTKGSVLIGSREIRAgrKEKNLKGVREKVGIVFQFPE-- 95
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS--PDVDPIEVRREVGMVFQYPNpf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 96 -HQLFEETVEKDIMFGpmNLGVTEKEAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDE 171
Cdd:PRK14267 98 pHLTIYDNVAIGVKLN--GLVKSKKELDERVEWALKKAALWDEVkdrLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 172 PTAGLDPRGRKEIMDLFYSLhkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-228 |
3.98e-35 |
|
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: 125.77 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYlAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkg 82
Cdd:cd03264 1 LQLENLTKRYG-----KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIV---FQFPEHQLFEETVEkdiMFGPMNlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:cd03264 70 LRRRIGYLpqeFGVYPNFTVREFLD---YIAWLK-GIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
23-238 |
5.27e-35 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 129.04 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNlkgvrekvGIVFQFPEHQLF-EE 101
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKR--------GIAYVYQNYMLFpHK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:NF040840 88 TVFENIAFGLKLRKVPKEEIERKVKEIMELLGI-SHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 182 KEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:NF040840 167 DELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPK 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-241 |
5.34e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.54 E-value: 5.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLI-GSREIRAGRKEknLKGVREKVGIVFQFPEHQLF- 99
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEA--QKLLRQKIQIVFQNPYGSLNp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETVEkDIMFGPM--NLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PRK11308 108 RKKVG-QILEEPLliNTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 178 PRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK-----ALL 241
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRhpytqALL 255
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-235 |
8.03e-35 |
|
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: 125.81 E-value: 8.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:cd03251 1 VEFKNVTFRYPGD---GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR----DYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKEAKTRARAAinlvgLPEEILEKSP--FD---------LSGGQM 151
Cdd:cd03251 74 LRRQIGLVSQ--DVFLFNDTVAENIAYG--RPGATREEVEEAARAA-----NAHEFIMELPegYDtvigergvkLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTPE 231
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLS-TIENADRIVVLEDGKIVERGTHE 221
|
....
gi 2119195095 232 QIFS 235
Cdd:cd03251 222 ELLA 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-235 |
1.40e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 125.51 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeknl 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKR-----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQFPEHQLFEE--TVEKDIMFG--PMN-----LGVTEKEAKTRARAAINLVGLPEEILEkspfDLSGGQM 151
Cdd:PRK11231 69 LSSRQLARRLALLPQHHLTPEgiTVRELVAYGrsPWLslwgrLSAEDNARVNQAMEQTRINHLADRRLT----DLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPE 231
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
....
gi 2119195095 232 QIFS 235
Cdd:PRK11231 224 EVMT 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-224 |
1.66e-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: 124.44 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKG 82
Cdd:cd03292 1 IEFINVTKTYPNGTA----ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEkSPFDLSGGQMRRVAIAGVLAM 162
Cdd:cd03292 76 LRRKIGVVFQ-DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHkKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-235 |
2.18e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.27 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIR--AGRKEKNL 80
Cdd:PRK13548 3 LEARNLSVRLGG-----RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGV-REKVGIVFQFpehqlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEeiLEKSPF-DLSGGQMRRVAIAG 158
Cdd:PRK13548 78 RAVlPQHSSLSFPF--------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAH--LAGRDYpQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLA------MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQ 232
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
...
gi 2119195095 233 IFS 235
Cdd:PRK13548 228 VLT 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-225 |
2.74e-34 |
|
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: 124.00 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQaDSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKG 82
Cdd:TIGR02211 2 LKCENLGKRYQ-EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFpEHQLFEETVEKDIMFgPMNLG-VTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:TIGR02211 81 RNKKLGFIYQF-HHLLPDFTALENVAM-PLLIGkKSVKEAKERAYEMLEKVGLEHRI-NHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVF 225
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLF 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-234 |
1.04e-33 |
|
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: 122.72 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:cd03254 2 EIEFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR----DISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGPMNLGVTE-KEAKTRARAAINLVGLP---EEILEKSPFDLSGGQMRRVAIA 157
Cdd:cd03254 74 SLRSMIGVVLQ--DTFLFSGTIMENIRLGRPNATDEEvIEAAKEAGAHDFIMKLPngyDTVLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRN-------LSTVlvthsmedaaRYADDIVVMHQGEVFTKGTP 230
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTsiiiahrLSTI----------KNADKILVLDDGKIIEEGTH 221
|
....
gi 2119195095 231 EQIF 234
Cdd:cd03254 222 DELL 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-236 |
1.07e-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: 122.65 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqaDSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:cd03249 1 IEFKNVSFRY--PSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR----DLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLV-GLPE----EILEKSpFDLSGGQMRRVAIA 157
Cdd:cd03249 75 LRSQIGLVSQEP--VLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDgydtLVGERG-SQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTPEQIFSN 236
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-230 |
1.09e-33 |
|
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: 130.13 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 17 PFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkEKNLKGVREKVGIVfqfPEH 96
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMC---PQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 Q-LFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPfDLSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:TIGR01257 1012 NiLFHHlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ-DLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 175 GLDPRGRKEIMDLFYSLHKKRNLstVLVTHSMEDAARYADDIVVMHQGEVFTKGTP 230
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTI--IMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-224 |
2.59e-33 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 121.21 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-RAGRKEKNlk 81
Cdd:cd03301 1 VELENVTKRFG-----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPKDRD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 gvrekVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIA 157
Cdd:cd03301 74 -----IAMVFQnyalYP-HM----TVYDNIAFGLKLRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-240 |
3.44e-33 |
|
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: 123.76 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 38 VIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeKNLKGVREKVGIVFQfpEHQLFEE-TVEKDIMFGPMNLGV 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQ--SYALFPHmTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 117 TEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRN 196
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119195095 197 LSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANL 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-237 |
5.86e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.76 E-value: 5.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 21 LAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKGVR-EKVGIVFQ----FPE 95
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDAELREVRrKKIAMVFQsfalMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 96 HQLFEETVekdimFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAG 175
Cdd:PRK10070 121 MTVLDNTA-----FGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 176 LDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-225 |
5.88e-33 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 120.51 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRaGRKEKNLKG 82
Cdd:TIGR02982 2 ISIRNLNHYYGHGS-LRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELH-GASKKQLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDI-MFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:TIGR02982 80 LRRRIGYIFQ--AHNLLGFlTARQNVqMALELQPNLSYQEARERARAMLEAVGL-GDHLNYYPHNLSGGQKQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHS--MEDAaryADDIVVMHQGEVF 225
Cdd:TIGR02982 157 VHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDnrILDV---ADRILQMEDGKLL 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-219 |
6.24e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 126.25 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqadsPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGrkekNLKG 82
Cdd:TIGR02857 322 LEFSGVSVAY----PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA----DADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFGPMNLGVTE-KEAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMRRVAIAG 158
Cdd:TIGR02857 394 WRDQIAWVPQHP--FLFAGTIAENIRLARPDASDAEiREALERAGLDEFVAALPQGLdtpIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEDAARyADDIVVM 219
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-238 |
7.79e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 121.04 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNAL--LKP---TKGSVLIGSREIRAGRKEKnlKGVREKVGIVFQFPEH 96
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDT--VDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 qlFEETVEKDIMFGPMNLGVTEK----EAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:PRK14239 98 --FPMSIYENVVYGLRLKGIKDKqvldEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 173 TAGLDPRGRKEIMDLFYSLHKKRNLstVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-228 |
3.49e-32 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 117.98 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQaDSPFerlaisDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeknLKG 82
Cdd:cd03298 1 VRLDKIRFSYG-EQPM------HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA------APP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFG--PmNLGVTEkEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:cd03298 68 ADRPVSMLFQ--ENNLFAHlTVEQNVGLGlsP-GLKLTA-EDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-238 |
5.50e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.86 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLK-----PTKGSVLIGSREIRagrkEKNLKGVREKVGIVFQFPeHQ 97
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIF----KMDVIELRRRVQMVFQIP-NP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEETVEKDIMFGP-MN-LGVTEKEAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:PRK14247 94 IPNLSIFENVALGLkLNrLVKSKKELQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 173 TAGLDPRGRKEIMDLFYSLhkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-224 |
7.13e-32 |
|
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: 116.16 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKG 82
Cdd:cd03246 1 LEVENVSFRYPGA---EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ----WDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKDImfgpmnlgvtekeaktraraainlvglpeeilekspfdLSGGQMRRVAIAGVLAM 162
Cdd:cd03246 74 LGDHVGYLPQ--DDELFSGSIAENI--------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARyADDIVVMHQGEV 224
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-224 |
7.16e-32 |
|
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: 118.75 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPF---ERLAI-SDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEK 78
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakQRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL-YQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 79 NLKGVREKVGIVFQFPEHQLFEETVEKDIMFGPMN--LGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAI 156
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRhlTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-238 |
1.00e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 118.66 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKG-----SVLIGSREIRAGRkekNLKGVREKVGIVFQFP 94
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR---DVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 EHqlFEETVEKDIMFG-PMNLGVTEKEAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:PRK14271 111 NP--FPMSIMDNVLAGvRAHKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 171 EPTAGLDPRGRKEIMDLFYSLHKKrnLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-238 |
1.82e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 117.81 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGS----VLIGSREIRAGRKEKNLKGVREKVGIVFQfpEHQ 97
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiELLGRTVQREGRLARDIRKSRANTGYIFQ--QFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEE-TVEKDIMFGPmnLGVT----------EKEAKTRARAAINLVGLPEEILEKSPfDLSGGQMRRVAIAGVLAMEPEV 166
Cdd:PRK09984 97 LVNRlSVLENVLIGA--LGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVS-TLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 167 IVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQiFSNPK 238
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDNER 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-240 |
2.41e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkeKNLKG 82
Cdd:PRK09452 15 VELRGISKSFD-----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------THVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPEHQLFEetvekDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:PRK09452 84 ENRHVNTVFQsyalFPHMTVFE-----NVAFGLRMQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
..
gi 2119195095 239 AL 240
Cdd:PRK09452 238 NL 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-241 |
2.45e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.48 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLA----ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEK 78
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 79 nLKGVREKVGIVFQFPEHQLFEETVEKDIMFGPMN--LGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAI 156
Cdd:PRK10419 84 -RKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRhlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVF--TKGTPEQIF 234
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVetQPVGDKLTF 242
|
....*..
gi 2119195095 235 SNPKALL 241
Cdd:PRK10419 243 SSPAGRV 249
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
2.67e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.27 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIR---AGRke 77
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 knlkgvrekvGIVFQfpEHQLFE-ETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAI 156
Cdd:COG4525 79 ----------GVVFQ--KDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVM 219
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-248 |
6.59e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.95 E-value: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKE---KN 79
Cdd:COG4604 2 IEIKNVSKRYG-----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelaKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 80 LKGVREKVGIVFQFpehqlfeeTVEKDIMFG--PMNLGVTEKEAKTRARAAINLVGLPEeiLEKSPFD-LSGGQMRRVAI 156
Cdd:COG4604 77 LAILRQENHINSRL--------TVRELVAFGrfPYSKGRLTAEDREIIDEAIAYLDLED--LADRYLDeLSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFsN 236
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII-T 225
|
250
....*....|...
gi 2119195095 237 PKALLEL-GLDVP 248
Cdd:COG4604 226 PEVLSDIyDTDIE 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-273 |
1.49e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.13 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 5 LKNVEYRYQADSpferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNlkgvR 84
Cdd:PRK11432 9 LKNITKRFGSNT-----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQ----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 85 EkVGIVFQ----FPEHQLFEetvekDIMFGPMNLGVTEKEAKTRARAAINLVGLpeEILEKSPFD-LSGGQMRRVAIAGV 159
Cdd:PRK11432 79 D-ICMVFQsyalFPHMSLGE-----NVGYGLKMLGVPKEERKQRVKEALELVDL--AGFEDRYVDqISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 240 LL-------------ELGLDVPEVVGLQLKIEEAFNTKFSK-----------ISLSEE 273
Cdd:PRK11432 231 RFmasfmgdanifpaTLSGDYVDIYGYRLPRPAAFAFNLPDgectvgvrpeaITLSEQ 288
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-237 |
1.50e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.13 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFErlaisDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLK-----PTKGSVLIGSREIRAGRKe 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILE-----GVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 kNLKGVREKVGIVFqfPEHQLFEETVEKDIMFGPMNLGVTEK-EAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMRR 153
Cdd:PRK14258 82 -NLNRLRRQVSMVH--PKPNLFPMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIkhkIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQ-----GEVFTKG 228
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG 238
|
....*....
gi 2119195095 229 TPEQIFSNP 237
Cdd:PRK14258 239 LTKKIFNSP 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-238 |
1.71e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 115.26 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 21 LAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNAL--LKPT---KGSVLIGSREIRAGRKEKnlKGVREKVGIVFQFPE 95
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDVDP--VEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 96 HqlFEETVEKDIMFGPMNLG----VTEKEAKTRARAAinlvgLPEEI---LEKSPFDLSGGQMRRVAIAGVLAMEPEVIV 168
Cdd:PRK14243 102 P--FPKSIYDNIAYGARINGykgdMDELVERSLRQAA-----LWDEVkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 169 LDEPTAGLDPRGRKEIMDLFYSLhkKRNLSTVLVTHSMEDAARYADDIVVMH---------QGEVFTKGTPEQIFSNPK 238
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQ 251
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-247 |
4.13e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 113.14 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfeRLAISdVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsreirAGRKEKNLKG 82
Cdd:PRK10771 2 LKLTDITWLYH------HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL------NGQDHTTTPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFGpMNLGVTEKEAKTRARAAI-NLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:PRK10771 69 SRRPVSMLFQ--ENNLFSHlTVAQNIGLG-LNPGLKLNAAQREKLHAIaRQMGI-EDLLARLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSN--PK 238
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGkaSA 224
|
....*....
gi 2119195095 239 ALLeLGLDV 247
Cdd:PRK10771 225 SAL-LGIKS 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-234 |
5.64e-30 |
|
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: 113.26 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSV--LIGSReiragRKEKNL 80
Cdd:COG1119 4 LELRNVTVRRG-----GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGER-----RGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIV-----FQFPEHqlfeETVEKDIM---FGpmNLGVTEK---EAKTRARAAINLVGLpEEILEKSPFDLSGG 149
Cdd:COG1119 74 WELRKRIGLVspalqLRFPRD----ETVLDVVLsgfFD--SIGLYREptdEQRERARELLELLGL-AHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 150 QMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGT 229
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
....*
gi 2119195095 230 PEQIF 234
Cdd:COG1119 227 KEEVL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-241 |
1.80e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 112.01 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 21 LAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKgvreKVGIVFQFPEHQLFE 100
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPGHQIA----RMGVVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 E-TVEKDIMFGP---MNLGV------------TEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEP 164
Cdd:PRK11300 94 EmTVIENLLVAQhqqLKTGLfsgllktpafrrAESEALDRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 165 EVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP---KALL 241
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPdviKAYL 252
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-235 |
3.12e-29 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 116.89 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:TIGR03375 463 EIEFRNVSFAYPGQ---ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR----QIDPA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEkeakTRARAAINLVGLpEEILEKSP--FD---------LSGGQ 150
Cdd:TIGR03375 536 DLRRNIGYVPQ--DPRLFYGTLRDNIALG--APYADD----EEILRAAELAGV-TEFVRRHPdgLDmqigergrsLSGGQ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLstVLVTHSMEdAARYADDIVVMHQGEVFTKGTP 230
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTS-LLDLVDRIIVMDNGRIVADGPK 683
|
....*
gi 2119195095 231 EQIFS 235
Cdd:TIGR03375 684 DQVLE 688
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-238 |
4.95e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 112.88 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRaGRKEKNLKGVREKVGIVFQFPEHQLFEE 101
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL-GMKDDEWRAVRSDIQMIFQDPLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNL---GVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:PRK15079 115 MTIGEIIAEPLRTyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 179 RGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
6.31e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.95 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLqhlNAL---LKPTKGSVLIGSREI-------R 72
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLL---NAIagsLPPDSGSILIDGKDVtklpeykR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 73 AGRkeknlkgvrekVGIVFQFP---------------------------------EHQLFEETVEKdimfgpMNLGVtEK 119
Cdd:COG1101 79 AKY-----------IGRVFQDPmmgtapsmtieenlalayrrgkrrglrrgltkkRRELFRELLAT------LGLGL-EN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 120 EAKTRaraainlVGLpeeilekspfdLSGGQmrRVAIAgvLAM----EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKR 195
Cdd:COG1101 141 RLDTK-------VGL-----------LSGGQ--RQALS--LLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEN 198
|
250 260
....*....|....*....|....*....
gi 2119195095 196 NLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:COG1101 199 NLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-204 |
1.02e-28 |
|
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: 108.72 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknl 80
Cdd:COG4133 1 MMLEAENLSCRRG-----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 kgVREKVGIVFQFPEhqLFEE-TVEKDIMFGPMNLGVTEKEAktRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:COG4133 73 --YRRRLAYLGHADG--LKPElTVRENLRFWAALYGLRADRE--AIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFySLHKKRNLSTVLVTH 204
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELI-AAHLARGGAVLLTTH 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-237 |
1.46e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.24 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGsreiraGRKEKNLKGVREKVGIVFQfpEHQLFEE 101
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD------GVDLSHVPPYQRPINMMFQ--SYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 -TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRG 180
Cdd:PRK11607 106 mTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 181 RK----EIMDLFyslhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK11607 185 RDrmqlEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-224 |
3.21e-28 |
|
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: 108.06 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:cd03245 2 RIEFRNVSFSYPNQ---EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR----QLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKeaktRARAAINLVGLpEEILEKSP-----------FDLSGGQ 150
Cdd:cd03245 75 DLRRNIGYVPQ--DVTLFYGTLRDNITLG--APLADDE----RILRAAELAGV-TDFVNKHPngldlqigergRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLstVLVTH--SMEDaarYADDIVVMHQGEV 224
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-210 |
3.50e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.57 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKP---TKGSVLIGSREIRAGRKEknlkgvREKVGIVFQfpEHQLF 99
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE------QRRIGILFQ--DDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EE-TVEKDIMFGpMNLGVTEKEAKTRARAAINLVGLPEeILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:COG4136 89 PHlSVGENLAFA-LPPTIGRAQRRARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190
....*....|....*....|....*....|..
gi 2119195095 179 RGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAA 210
Cdd:COG4136 167 ALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
3-224 |
4.21e-28 |
|
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: 107.64 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADsPFErlaisdVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGsreiraGRKEKNLKG 82
Cdd:TIGR01277 1 LALDKVRYEYEHL-PME------FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVN------DQSHTGLAP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEE-TVEKDIMFG---PMNLGVTEKEaktRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:TIGR01277 68 YQRPVSMLFQ--ENNLFAHlTVRQNIGLGlhpGLKLNAEQQE---KVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:TIGR01277 142 CLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-233 |
5.30e-28 |
|
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: 107.52 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkgvREKVGIVFQFPEHQLFEE 101
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-----RARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 -TVEKDIMFGpmnlGVTEKEAKTRARaainlvglPEEILEKSP----------FDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:cd03224 90 lTVEENLLLG----AYARRRAKRKAR--------LERVYELFPrlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 171 EPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-235 |
1.12e-27 |
|
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: 107.19 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkg 82
Cdd:cd03252 1 ITFEHVRFRYKPDGP---VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKDIMFGPMNLGVTEKEAKTR-ARAAINLVGLPE---EILEKSPFDLSGGQMRRVAIAG 158
Cdd:cd03252 74 LRRQVGVVLQ--ENVLFNRSIRDNIALADPGMSMERVIEAAKlAGAHDFISELPEgydTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlsTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFS 235
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR---TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-238 |
1.60e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.06 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGV--REKVGIVFQFPeH 96
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIklRKEVGMVFQQP-N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 QLFEETVEKDIMFGPMNLGVTEK-EAKTRARAAINLVGLPEEILEK--SPFD-LSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRlnSPASqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 173 TAGLDPRGRKEIMDLFYSLhkKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-233 |
4.25e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 105.30 E-value: 4.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNlkgVREKVGIVFQ----FPehQ 97
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER---ARAGIAYVPQgreiFP--R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LfeeTVEKDIMFGPMNLGVTEKEaktraraainlvgLPEEILEKSPF----------DLSGGQMRRVAIAGVLAMEPEVI 167
Cdd:TIGR03410 90 L---TVEENLLTGLAALPRRSRK-------------IPDEIYELFPVlkemlgrrggDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 168 VLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-239 |
4.49e-27 |
|
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: 105.32 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-------RAGRkeknlkgvrekvGIVFQ 92
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhkRARL------------GIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 93 FPEHQLFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDE 171
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 172 PTAGLDPRGRKEIMDLFYSLhKKRNLStVLVT-HSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-239 |
6.39e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLkPTKGSVLIGSREIRaGRKEKNLKGVREKVGIVFQFPEHQL 98
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLH-NLNRRQLLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 99 -----FEETVEKDIMFGPMNLGVTEKEAktRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:PRK15134 376 nprlnVLQIIEEGLRVHQPTLSAAQREQ--QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 174 AGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
7.13e-27 |
|
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: 109.37 E-value: 7.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlk 81
Cdd:TIGR02868 334 TLELRDLSAGYPGAPP----VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE--- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 gVREKVGIVFQFPeHqLFEETVEKDIMFGpmNLGVTEKEAKT---RARAAINLVGLPE----EILEKSPFdLSGGQMRRV 154
Cdd:TIGR02868 407 -VRRRVSVCAQDA-H-LFDTTVRENLRLA--RPDATDEELWAaleRVGLADWLRALPDgldtVLGEGGAR-LSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIM-DLFYSLHKKRnlsTVLVTHS 205
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSGRT---VVLITHH 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-244 |
8.22e-27 |
|
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: 109.52 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:COG5265 358 VRFENVSFGYDPERP----ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR----DVTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKDIMFGpmNLGVTEKEAKTRARAA-----INlvGLPE----EILE---KspfdLSGGQ 150
Cdd:COG5265 430 LRAAIGIVPQ--DTVLFNDTIAYNIAYG--RPDASEEEVEAAARAAqihdfIE--SLPDgydtRVGErglK----LSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRN-------LSTVlvthsmedaaRYADDIVVMHQGE 223
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTtlviahrLSTI----------VDADEILVLEAGR 569
|
250 260
....*....|....*....|.
gi 2119195095 224 VFTKGTPEQifsnpkaLLELG 244
Cdd:COG5265 570 IVERGTHAE-------LLAQG 583
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-237 |
9.87e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.88 E-value: 9.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQfpEHQLFEE-TV 103
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQ--DARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 104 EKDIMFGpMNlgvtekeAKTRAR--AAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD-PRG 180
Cdd:PRK11144 94 RGNLRYG-MA-------KSMVAQfdKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 181 RkEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK11144 165 R-ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-286 |
1.03e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.96 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGrkeknlkg 82
Cdd:COG4152 2 LELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIvfqfpehqLFEE-------TVEKDIMFgpmnL----GVTEKEAKTRARAAINLVGLPEEI---LEkspfDLSG 148
Cdd:COG4152 69 DRRRIGY--------LPEErglypkmKVGEQLVY----LarlkGLSKAEAKRRADEWLERLGLGDRAnkkVE----ELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 149 GQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhkKRNLSTVLV-THSMEDAARYADDIVVMHQGEVFTK 227
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL--AAKGTTVIFsSHQMELVEELCDRIVIINKGRKVLS 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 228 GTPEQI---FSNPKALLELGLDVPEVVGLQLKIEEAFNTKFSKISLSEEELAEMV-AEFMERG 286
Cdd:COG4152 211 GSVDEIrrqFGRNTLRLEADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELlRALLARG 273
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-281 |
1.10e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.17 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKE----- 77
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 ----KNLKGVR-EKVGIVFQFPEHQL-----FEETVEKDIMfgpMNLGVTEKEAKTRARAAINLVGLPE--EILEKSPFD 145
Cdd:PRK10261 92 eqsaAQMRHVRgADMAMIFQEPMTSLnpvftVGEQIAESIR---LHQGASREEAMVEAKRMLDQVRIPEaqTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 146 LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVF 225
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 226 TKGTPEQIFSNP-----KALLELgldVPEVVGLQlkiEEAFNTKFSKISLSEEELAEMVAE 281
Cdd:PRK10261 249 ETGSVEQIFHAPqhpytRALLAA---VPQLGAMK---GLDYPRRFPLISLEHPAKQEPPIE 303
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-219 |
1.88e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVligsrEIRAGRKeknLKGVREKVGIVFQFPEhqlf 99
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGGAR---VAYVPQRSEVPDSLPL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 eeTVEKDIMFG----PMNLGVTEKEAKTRARAAINLVGLPEeiLEKSPFD-LSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:NF040873 73 --TVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLAD--LAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2119195095 175 GLDPRGRKEIMDLFYSLHkKRNLSTVLVTHSMEDAARyADDIVVM 219
Cdd:NF040873 149 GLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-224 |
2.90e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.60 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREiragrkeknLKG 82
Cdd:PRK11247 13 LLLNAVSKRYG-----ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP---------LAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKDimfgpmNLGVTEK-EAKTRARAAINLVGLPEEILEkSPFDLSGGQMRRVAIAGVLA 161
Cdd:PRK11247 79 AREDTRLMFQ--DARLLPWKKVID------NVGLGLKgQWRDAALQALAAVGLADRANE-WPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
20-239 |
4.20e-26 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 103.37 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSR-----EIRAGRKEKNLKGVREKVGIVFQFP 94
Cdd:TIGR02323 16 GKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAERRRLMRTEWGFVHQNP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 EHQL-FEETVEKDIMFGPMNLGVtEKEAKTRARAAINL--VGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDE 171
Cdd:TIGR02323 96 RDGLrMRVSAGANIGERLMAIGA-RHYGNIRATAQDWLeeVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 172 PTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKA 239
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-237 |
4.26e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.72 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVRekvgIVFQFPEHQLFEE 101
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIR----MIFQDPSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNLGvTEKEAKTRAR---AAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:PRK15112 104 QRISQILDFPLRLN-TDLEPEQREKqiiETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 179 RGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-235 |
4.98e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.53 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-RAGRKEknlkgVREKVGIVFQ----------- 92
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKE-----VARRIGLLAQnattpgditvq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 93 -------FPEHQLFEETVEKDimfgpmnlgvteKEAKTRARAAINLVGLPEEILEKspfdLSGGQMRRVAIAGVLAMEPE 165
Cdd:PRK10253 100 elvargrYPHQPLFTRWRKED------------EEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 166 VIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFS 235
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-238 |
5.27e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 102.86 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 11 RYQADSPFerlaISDVSIDVPSGTYLAVIGHTGSGKS----TVLQHLNALLKPTKGSVLIGSREIRAGrkekNLKGvrEK 86
Cdd:PRK10418 11 ALQAAQPL----VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPC----ALRG--RK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 87 VGIVFQFPEHQlfeetvekdimFGPMN------------LGVTEKEAktRARAAINLVGL--PEEILEKSPFDLSGGQMR 152
Cdd:PRK10418 81 IATIMQNPRSA-----------FNPLHtmhtharetclaLGKPADDA--TLTAALEAVGLenAARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 153 RVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQ 232
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
....*.
gi 2119195095 233 IFSNPK 238
Cdd:PRK10418 228 LFNAPK 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-228 |
5.27e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 100.85 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadsPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkg 82
Cdd:cd03247 1 LSINNVSFSYP---EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKdimfgpmNLGvtekeakTRaraainlvglpeeilekspfdLSGGQMRRVAIAGVLAM 162
Cdd:cd03247 73 LSSLISVLNQRP--YLFDTTLRN-------NLG-------RR---------------------FSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLstVLVTHSMEdAARYADDIVVMHQGEVFTKG 228
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-222 |
8.45e-26 |
|
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: 101.77 E-value: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNlkgvrekvgIVFQfpEHQLFE-E 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQ--NYSLLPwL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFG--PMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPR 179
Cdd:TIGR01184 70 TVRENIALAvdRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2119195095 180 GRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQG 222
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-233 |
8.91e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 8.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLkgV 83
Cdd:PRK10575 13 ALRNVSFRVPG-----RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-ESWSSKAF--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 REKVGIVFQFPEHQLFeeTVEKDIMFG--PMN--LGVTEKEAKTRARAAINLVGLpeeilekSPF------DLSGGQMRR 153
Cdd:PRK10575 85 RKVAYLPQQLPAAEGM--TVRELVAIGryPWHgaLGRFGAADREKVEEAISLVGL-------KPLahrlvdSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-235 |
1.41e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 105.95 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:TIGR02203 330 DVEFRNVTFRYPGR---DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA----DYTLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGPMNlGVTEKEAKTRARAAiNLV--------GLPEEILEKSPfDLSGGQMRR 153
Cdd:TIGR02203 403 SLRRQVALVSQ--DVVLFNDTIANNIAYGRTE-QADRAEIERALAAA-YAQdfvdklplGLDTPIGENGV-LLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNEL 554
|
..
gi 2119195095 234 FS 235
Cdd:TIGR02203 555 LA 556
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-238 |
1.52e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 103.28 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 15 DSPFErlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALL----KPTKGSVLIGSREIRAGRKEKNLKGVREKVGIV 90
Cdd:PRK11022 17 SAPFR--AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 91 FQFPEHQLFE-ETVEKDIMFG-PMNLGVTEKEAKTRARAAINLVGLPEEI--LEKSPFDLSGGQMRRVAIAGVLAMEPEV 166
Cdd:PRK11022 95 FQDPMTSLNPcYTVGFQIMEAiKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 167 IVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-224 |
1.62e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIR-AGRKEKNLK 81
Cdd:cd03216 1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVrekvGIVFQfpehqlfeetvekdimfgpmnlgvtekeaktraraainlvglpeeilekspfdLSGGQMRRVAIAGVLA 161
Cdd:cd03216 76 GI----AMVYQ-----------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-224 |
3.78e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.81 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 5 LKNVEYRYQA-DSPFERLaiSDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGV 83
Cdd:PRK10535 7 LKDIRRSYPSgEEQVEVL--KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 REKVGIVFQfPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGVLAME 163
Cdd:PRK10535 85 REHFGFIFQ-RYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 164 PEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARyADDIVVMHQGEV 224
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-228 |
4.85e-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: 99.28 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeknlkGVREKVGIVfqfPEHQ-LFE 100
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--------AARNRIGYL---PEERgLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 ETVEKDIM--FGPMNlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:cd03269 84 KMKVIDQLvyLAQLK-GLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119195095 179 RGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:cd03269 162 VNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-252 |
7.23e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.04 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI--RAGRkeknl 80
Cdd:PRK13537 8 IDFRNVEKRYG-----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsRARH----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 kgVREKVGIVFQF----PEHqlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAI 156
Cdd:PRK13537 78 --ARQRVGVVPQFdnldPDF-----TVRENLLVFGRYFGLSAAAARALVPPLLEFAKL-ENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSN 236
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
250
....*....|....*.
gi 2119195095 237 pkallELGLDVPEVVG 252
Cdd:PRK13537 229 -----EIGCDVIEIYG 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-238 |
7.84e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 7.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVeyrYQAdspFERLAIS-DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGsrEIRAGRKEKNL 80
Cdd:PRK11000 3 SVTLRNV---TKA---YGDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVrekvGIVFQ----FPEHQLFEetvekDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAI 156
Cdd:PRK11000 75 RGV----GMVFQsyalYPHLSVAE-----NMSFGLKLAGAKKEEINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSN 236
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHY 224
|
..
gi 2119195095 237 PK 238
Cdd:PRK11000 225 PA 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-228 |
1.86e-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: 97.67 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsreirAGRKEKNLKG 82
Cdd:cd03268 1 LKTNDLTKTYG-----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF------DGKSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEhqLFEE-TVEKDIMFGPMNLGVTEKEAKTraraAINLVGLPEEilEKSPF-DLSGGQMRRVAIAGVL 160
Cdd:cd03268 70 ALRRIGALIEAPG--FYPNlTARENLRLLARLLGIRKKRIDE----VLDVVGLKDS--AKKKVkGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhkKRNLSTVLV-THSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSL--RDQGITVLIsSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-238 |
2.05e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.13 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNlkgVREKVGIVfqfPE-HQLFE 100
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI---ARLGIGYV---PEgRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 E-TVEKDIMFGPMNLGVTEKEAKTraraainlvglPEEILEKSP----------FDLSGGQMRRVAIAGVLAMEPEVIVL 169
Cdd:COG0410 92 SlTVEENLLLGAYARRDRAEVRAD-----------LERVYELFPrlkerrrqraGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 170 DEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-232 |
2.34e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRkEKNLk 81
Cdd:PRK11160 338 SLTLNNVSFTYPDQ---PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAAL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 gvREKVGIVFQFPeHqLFEETVeKDimfgpmNLGVTEKEAK-TRARAAINLVGLpEEILE-KSPFD---------LSGGQ 150
Cdd:PRK11160 413 --RQAISVVSQRV-H-LFSATL-RD------NLLLAAPNASdEALIEVLQQVGL-EKLLEdDKGLNawlgeggrqLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLstVLVTHSMEDAARYaDDIVVMHQGEVFTKGTP 230
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGLEQF-DRICVMDNGQIIEQGTH 557
|
..
gi 2119195095 231 EQ 232
Cdd:PRK11160 558 QE 559
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-211 |
3.36e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.58 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 7 NVEYRYQaDSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREK 86
Cdd:PRK11629 10 NLCKRYQ-EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 87 VGIVFQFpeHQLFE-----ETVEKDIMFGpmnlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLA 161
Cdd:PRK11629 89 LGFIYQF--HHLLPdftalENVAMPLLIG----KKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAAR 211
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-239 |
4.65e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-------RA 73
Cdd:COG1137 2 MTLEAENLVKSYGK-----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 74 grkeknlkgvreKVGIVF--QfpEHQLFEE-TVEKDIMfgpMNLGVTEKEAKTRARAAinlvglpEEILE--------KS 142
Cdd:COG1137 77 ------------RLGIGYlpQ--EASIFRKlTVEDNIL---AVLELRKLSKKEREERL-------EELLEefgithlrKS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 143 P-FDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLStVLVT-HSMEDAARYADDIVVMH 220
Cdd:COG1137 133 KaYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIG-VLITdHNVRETLGICDRAYIIS 210
|
250
....*....|....*....
gi 2119195095 221 QGEVFTKGTPEQIFSNPKA 239
Cdd:COG1137 211 EGKVLAEGTPEEILNNPLV 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-255 |
8.09e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.53 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRA------GRKeknLKGVREKVGIVFQFPEH 96
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsaraaSRR---VASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 QLFEetvekdiM--------FGPMNlgvtekEAKTRA-RAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVI 167
Cdd:PRK09536 96 QVVE-------MgrtphrsrFDTWT------ETDRAAvERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 168 VLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKalLELGLDV 247
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT--LRAAFDA 238
|
....*...
gi 2119195095 248 PEVVGLQL 255
Cdd:PRK09536 239 RTAVGTDP 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-235 |
8.19e-24 |
|
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: 100.65 E-value: 8.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGS--VLIGSREIRAGRKEKNL 80
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KG-VREKVGIVFQfpEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEE----ILEKSPFDLSGGQMRRVA 155
Cdd:TIGR03269 360 RGrAKRYIGILHQ--EYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEkaeeILDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 156 IAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDlfySLHKKR---NLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQ 232
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTH---SILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
...
gi 2119195095 233 IFS 235
Cdd:TIGR03269 515 IVE 517
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-228 |
9.47e-24 |
|
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: 95.90 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsreirAG-RKEKNLK 81
Cdd:cd03266 2 ITADALTKRFRDVKK-TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV------DGfDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEE-TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:cd03266 75 EARRRLGFVSD--STGLYDRlTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDlfYSLHKKRNLSTVLV-THSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFsTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-222 |
1.20e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkgvrekvGIVFQfPEHQLFEE 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQ-NEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119195095 182 KEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQG 222
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-230 |
1.65e-23 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 95.25 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLK 81
Cdd:cd03244 2 DIEFKNVSLRYRPNLP---PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI----SKIGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQFPehQLFEETVEKdimfgpmNLGVTEKEAKTRARAAINLVGLPEEI----------LEKSPFDLSGGQM 151
Cdd:cd03244 75 DLRSRISIIPQDP--VLFSGTIRS-------NLDPFGEYSDEELWQALERVGLKEFVeslpggldtvVEEGGENLSVGQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlsTVL-VTHSMEDAARYaDDIVVMHQGEVFTKGTP 230
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC---TVLtIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-223 |
2.08e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.17 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 5 LKNVEYryQADSpfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkgVR 84
Cdd:PRK10247 10 LQNVGY--LAGD---AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI----YR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 85 EKVGIVFQFPehQLFEETVEKDIMFgPMNLgvtEKEAKTRARAAINLV--GLPEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK10247 81 QQVSYCAQTP--TLFGDTVYDNLIF-PWQI---RNQQPDPAIFLDDLErfALPDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSmEDAARYADDIVVM--HQGE 223
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD-KDEINHADKVITLqpHAGE 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-224 |
2.87e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkeknLKGVRE----KVGIVFQfpEHQ 97
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-------FRSPRDaqaaGIAIIHQ--ELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEE-TVEKDIMFG--PMNLGVT-EKEAKTRARAAINLVGL---PEEILEkspfDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:COG1129 90 LVPNlSVAENIFLGrePRRGGLIdWRAMRRRARELLARLGLdidPDTPVG----DLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 171 EPTAGLDPRgrkEIMDLFYSLH--KKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:COG1129 166 EPTASLTER---EVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-243 |
3.14e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTVLqhlNALLK--PTKGSVLIGSREIRagrkEKNLKGVREKVGIVFQFPehQLFEETV 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIELR----ELDPESWRKHLSWVGQNP--QLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 104 EKDIMFGPMNLGVTE-KEAKTRARAAINLVGLPE----EILEKSPfDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:PRK11174 440 RDNVLLGNPDASDEQlQQALENAWVSEFLPLLPQgldtPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 179 RGRKEIMDlfySLHK-KRNLSTVLVTHSMEDAARYaDDIVVMHQGEVFTKGTPEQIFSNPKALLEL 243
Cdd:PRK11174 519 HSEQLVMQ---ALNAaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-224 |
3.24e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 94.85 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKeknlKG 82
Cdd:cd03248 12 VKFQNVTFAYPTRP--DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH----KY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFGPMNLGVTE-KEAKTRARAAINLVGLP----EEILEKSPfDLSGGQMRRVAIA 157
Cdd:cd03248 86 LHSKVSLVGQEP--VLFARSLQDNIAYGLQSCSFECvKEAAQKAHAHSFISELAsgydTEVGEKGS-QLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLStvLVTHSMEDAARyADDIVVMHQGEV 224
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVL--VIAHRLSTVER-ADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-243 |
5.86e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSpfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:TIGR00958 479 IEFQDVSFSYPNRP--DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV----QYDHHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFGpmnLGVTEKEAKTRARAAIN----LVGLPE----EILEKSPFdLSGGQMRRV 154
Cdd:TIGR00958 553 LHRQVALVGQEP--VLFSGSVRENIAYG---LTDTPDEEIMAAAKAANahdfIMEFPNgydtEVGEKGSQ-LSGGQKQRI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDprgrKEIMDLFYSLHKKRNLSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVVEMGTHKQLM 701
|
....*....
gi 2119195095 235 SNPKALLEL 243
Cdd:TIGR00958 702 EDQGCYKHL 710
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-237 |
1.12e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.22 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSRE------IRAGRKE 77
Cdd:PRK11701 8 SVRGLTKLYGP-----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 KNLKgVREKVGIVFQFPEHQLfEETVEKDIMFGPMNLGVTEKE-AKTRARAAINL--VGLPEEILEKSPFDLSGGQMRRV 154
Cdd:PRK11701 83 RRRL-LRTEWGFVHQHPRDGL-RMQVSAGGNIGERLMAVGARHyGDIRATAGDWLerVEIDAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
...
gi 2119195095 235 SNP 237
Cdd:PRK11701 241 DDP 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-237 |
1.35e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKS-TVLQHLNALLKP----TKGSVLI-GSREIRAgrKEKNLKGVR-EKVGIVF 91
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFhGESLLHA--SEQTLRGVRgNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 92 QFP----------EHQLFEETVekdimfgpMNLGVTEKEAKTRARAAINLVGL--PEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:PRK15134 99 QEPmvslnplhtlEKQLYEVLS--------LHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-224 |
1.58e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.17 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSrEIRAGRKEKNLKgvreKVGIVF--------QF 93
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLR----RIGVVFgqktqlwwDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 94 PEHQLFEetVEKDIMfgpmnlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:cd03267 111 PVIDSFY--LLAAIY------DLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 174 AGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-238 |
2.55e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.46 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnLKGVREKVGIVFQFPEHQLF-E 100
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDPYASLDpR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 ETVEKDIMFGPMNLGVTE-KEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPR 179
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 180 GRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPK 238
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-234 |
2.60e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 96.33 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLK 81
Cdd:PRK10790 340 RIDIDNVSFAYRDD----NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----SSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQFPehqlfeeTVEKDIMFGPMNLGVTEKEAKT-RARAAINLV----GLPEEI---LEKSPFDLSGGQMRR 153
Cdd:PRK10790 412 VLRQGVAMVQQDP-------VVLADTFLANVTLGRDISEEQVwQALETVQLAelarSLPDGLytpLGEQGNNLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLstVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQI 233
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
.
gi 2119195095 234 F 234
Cdd:PRK10790 562 L 562
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-229 |
2.85e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.24 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:PRK11176 341 DIEFRNVTFTYPGK---EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR----DYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFgPMNLGVTEKEAKTRARAA-----INLV--GLPEEILEKSPFdLSGGQMRRV 154
Cdd:PRK11176 414 SLRNQVALVSQ--NVHLFNDTIANNIAY-ARTEQYSREQIEEAARMAyamdfINKMdnGLDTVIGENGVL-LSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlsTVLVTHSMEDAARYADDIVVMHQGEVFTKGT 229
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR---TSLVIAHRLSTIEKADEILVVEDGEIVERGT 561
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-223 |
5.56e-22 |
|
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: 90.99 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQhlnALL---KPTKGSVLIGSReiragrkekn 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLS---ALLgelEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 80 lkgvrekVGIVFQFPehQLFEETVEKDIMFG-PMNlgvtekeaKTRARAAINLVGL-------PE----EILEKSpFDLS 147
Cdd:cd03250 68 -------IAYVSQEP--WIQNGTIRENILFGkPFD--------EERYEKVIKACALepdleilPDgdltEIGEKG-INLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 148 GGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMD-LFysLHKKRNLSTV-LVTHSMEdAARYADDIVVMHQGE 223
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCI--LGLLLNNKTRiLVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-224 |
1.39e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIrAGRKEKNLKGVREKVGIVFQfPEHQLF 99
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-TRLKNREVPFLRRQIGMIFQ-DHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpeeiLEKS---PFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGL 176
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGL----LDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2119195095 177 DPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:PRK10908 169 DDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-252 |
1.79e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSV-LIGSREIRAGRKekn 79
Cdd:PRK13536 40 VAIDLAGVSKSYG-----DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 80 lkgVREKVGIVFQFPEHQLfEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:PRK13536 112 ---ARARIGVVPQFDNLDL-EFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARL-ESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNpka 239
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE--- 262
|
250
....*....|...
gi 2119195095 240 llELGLDVPEVVG 252
Cdd:PRK13536 263 --HIGCQVIEIYG 273
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-245 |
2.08e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.09 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKP---TKGSVLIGSREIrAGRKEKNLKGVR-EKVGIVFQFP--- 94
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREI-LNLPEKELNKLRaEQISMIFQDPmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 -------EHQLFEEtvekdIMfgpMNLGVTEKEAKTRARAAINLVGLPE--EILEKSPFDLSGGQMRRVAIAGVLAMEPE 165
Cdd:PRK09473 110 lnpymrvGEQLMEV-----LM---LHKGMSKAEAFEESVRMLDAVKMPEarKRMKMYPHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 166 VIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKALLELGL 245
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGL 261
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-219 |
2.35e-21 |
|
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: 89.80 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGS------------REIRAGRkeknlkgvREKVGI 89
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdlaqaspREILALR--------RRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 90 VFQF----PEhqlfeeTVEKDIMFGPM-NLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEP 164
Cdd:COG4778 98 VSQFlrviPR------VSALDVVAEPLlERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 165 EVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVM 219
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-229 |
2.82e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.49 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLK 81
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQ----GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR----TVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQfpEHQLFEETVEKDIMFGPMNlgVTEKEAKTRARAAINLvglpeEILEKSP--FD---------LSGGQ 150
Cdd:PRK13657 406 SLRRNIAVVFQ--DAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAH-----DFIERKPdgYDtvvgergrqLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRN-------LSTVlvthsmedaaRYADDIVVMHQGE 223
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTtfiiahrLSTV----------RNADRILVFDNGR 546
|
....*.
gi 2119195095 224 VFTKGT 229
Cdd:PRK13657 547 VVESGS 552
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-233 |
2.98e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSR-----EIRAGrkek 78
Cdd:COG1134 23 SLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELGAG---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 79 nlkgvrekvgivFQfPEHqlfeeTVEKDIMFGPMNLGVTEKEAKTRAraainlvglpEEILEKSP----FDL------SG 148
Cdd:COG1134 99 ------------FH-PEL-----TGRENIYLNGRLLGLSRKEIDEKF----------DEIVEFAElgdfIDQpvktysSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 149 gqMR-RVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTK 227
Cdd:COG1134 151 --MRaRLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*.
gi 2119195095 228 GTPEQI 233
Cdd:COG1134 228 GDPEEV 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-246 |
3.25e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.21 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 8 VEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnLKGVREKV 87
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR-LYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 88 GIVFQ---------------FP--EH-QLFEETVEKDIMfgpMNLgvtekEAkTRARAAINLVglpeeileksPFDLSGG 149
Cdd:PRK11831 87 SMLFQsgalftdmnvfdnvaYPlrEHtQLPAPLLHSTVM---MKL-----EA-VGLRGAAKLM----------PSELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 150 QMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGT 229
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|....*..
gi 2119195095 230 PEQIFSNPKALLELGLD 246
Cdd:PRK11831 228 AQALQANPDPRVRQFLD 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-224 |
3.84e-21 |
|
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: 88.38 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEY-RYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKP--TKGSVLIGSREIRagrke 77
Cdd:cd03213 2 VTLSFRNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 78 knLKGVREKVGIVFQfpEHQLFEE-TVEKDIMFgpmnlgvtekeaktraraAINLVGLpeeilekspfdlSGGQMRRVAI 156
Cdd:cd03213 77 --KRSFRKIIGYVPQ--DDILHPTlTVRETLMF------------------AAKLRGL------------SGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSmedaARY-----ADDIVVMHQGEV 224
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQ----PSSeifelFDKLLLLSQGRV 190
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-224 |
6.66e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 88.61 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 6 KNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKgvre 85
Cdd:TIGR03740 4 KNLSKRFG-----KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW----TRKDLH---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 86 KVGIVFQFPEhqLFEE-TVEKDIMFGPMNLGVTEkeakTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEP 164
Cdd:TIGR03740 71 KIGSLIESPP--LYENlTARENLKVHTTLLGLPD----SRIDEVLNIVDL-TNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 165 EVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-237 |
1.16e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.29 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGsreiraGRKEKNLKG 82
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ----VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIG------GRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQ----FPeHQlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAG 158
Cdd:PRK11650 74 ADRDIAMVFQnyalYP-HM----SVRENMAYGLKIRGMPKAEIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPR----GRKEIMDlfysLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIF 234
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKlrvqMRLEIQR----LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVY 223
|
...
gi 2119195095 235 SNP 237
Cdd:PRK11650 224 EKP 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-224 |
1.34e-20 |
|
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: 87.71 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALL---KPTKGSVLIGSREIRAGRkeknlkgVREKVGIVFQFpE 95
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQ-------FQKCVAYVRQD-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 96 HQLFEETVEKDIMFGPMN-LGVTEKEAKTRARAAINLVG-LPEEILEKSPFD-LSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:cd03234 91 ILLPGLTVRETLTYTAILrLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 173 TAGLDPRGRKEIMdLFYSLHKKRNlSTVLVT-HS-MEDAARYADDIVVMHQGEV 224
Cdd:cd03234 171 TSGLDSFTALNLV-STLSQLARRN-RIVILTiHQpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-211 |
3.21e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQ----FPEHQLFEe 101
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQsfmlIPTLNALE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 tvekDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEiLEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:PRK10584 108 ----NVELPALLRGESSRQSRNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190
....*....|....*....|....*....|
gi 2119195095 182 KEIMDLFYSLHKKRNLSTVLVTHSMEDAAR 211
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-224 |
1.31e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 21 LAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSRE---------IRAGrkeknlkgvrekVGIVF 91
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrirsprdaIALG------------IGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 92 QfpeH-QLFEE-TVEKDIMFG---PMNLGVTEKEAKTRARAAINLVGL---PEEILEkspfDLSGGQMRRVAIAGVLAME 163
Cdd:COG3845 87 Q---HfMLVPNlTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLdvdPDAKVE----DLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 164 PEVIVLDEPTAGLDPrgrKEIMDLFYSLH--KKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:COG3845 160 ARILILDEPTAVLTP---QEADELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-230 |
3.86e-19 |
|
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: 83.23 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLK 81
Cdd:cd03369 6 EIEVENLSVRYAPDLP---PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQFPehQLFEETVEkdimfgpMNLGVTEKEAKTRARAAINLVGlpeeilekSPFDLSGGQMRRVAIAGVLA 161
Cdd:cd03369 79 DLRSSLTIIPQDP--TLFSGTIR-------SNLDPFDEYSDEEIYGALRVSE--------GGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDlfySLHKKRNLSTVL-VTHSMEDAARYaDDIVVMHQGEVFTKGTP 230
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQK---TIREEFTNSTILtIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-235 |
4.40e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 87.02 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkgVREKVGIVFQfpEHQLFEETVE 104
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRET----FGKHIGYLPQ--DVELFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 105 KDImfGPMNLGVTEKEAKTRARAAinlvGLPEEILeKSP--FD---------LSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:TIGR01842 410 ENI--ARFGENADPEKIIEAAKLA----GVHELIL-RLPdgYDtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 174 AGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTPEQIFS 235
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-224 |
1.06e-18 |
|
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: 81.32 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLK-GV------REKVGIVfqfp 94
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRaGIayvpedRKREGLV---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 ehqlfeetvekdimfgpMNLGVTEkeaktraraaiNLVglpeeilekSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:cd03215 91 -----------------LDLSVAE-----------NIA---------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119195095 175 GLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03215 134 GVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-224 |
1.90e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.81 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSR-----EIRAGrkek 78
Cdd:cd03220 19 SLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllGLGGG---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 79 nlkgvrekvgivFQfPEHqlfeeTVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEksPF-DLSGGQMRRVAIA 157
Cdd:cd03220 95 ------------FN-PEL-----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL--PVkTYSSGMKARLAFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 158 GVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-235 |
4.09e-18 |
|
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: 84.08 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNAL--LKPTKGSVLIG----------SREIRAGRK------------- 76
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSKVGEPcpvcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 77 ------EKNLKGVREKVGIVFQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTRARAAINLVGLPEEILEKSPfDLSGGQ 150
Cdd:TIGR03269 95 dfwnlsDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIAR-DLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTP 230
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTP 253
|
....*
gi 2119195095 231 EQIFS 235
Cdd:TIGR03269 254 DEVVA 258
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-233 |
6.92e-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: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLK 81
Cdd:TIGR01193 473 DIVINDVSYSYGYGSN----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL----KDIDRH 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVREKVGIVFQFPehQLFEETVEKDIMFGPmNLGVTEKEAKtrarAAINLVGLPEEI----------LEKSPFDLSGGQM 151
Cdd:TIGR01193 545 TLRQFINYLPQEP--YIFSGSILENLLLGA-KENVSQDEIW----AACEIAEIKDDIenmplgyqteLSEEGSSISGGQK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrnlSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPE 231
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHD 693
|
..
gi 2119195095 232 QI 233
Cdd:TIGR01193 694 EL 695
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-237 |
7.78e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.16 E-value: 7.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRyQADSPFErlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQhlnALLKPTKGSVLIGSREIR-------- 72
Cdd:PRK15093 4 LDIRNLTIEFK-TSDGWVK--AVDRVSMTLTEGEIRGLVGESGSGKSLIAK---AICGVTKDNWRVTADRMRfddidllr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 73 -AGRKEKNLkgVREKVGIVFQFPEHQLF-EETVEKDIMF---GPMNLGVTEKEAKTRARAAINL---VGL--PEEILEKS 142
Cdd:PRK15093 78 lSPRERRKL--VGHNVSMIFQEPQSCLDpSERVGRQLMQnipGWTYKGRWWQRFGWRKRRAIELlhrVGIkdHKDAMRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 143 PFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQG 222
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250
....*....|....*
gi 2119195095 223 EVFTKGTPEQIFSNP 237
Cdd:PRK15093 236 QTVETAPSKELVTTP 250
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-237 |
7.79e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.22 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 9 EYRY-QADSPferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRkeknLKGVREKV 87
Cdd:PRK10789 320 QFTYpQTDHP----ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ----LDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 88 GIVFQFPehQLFEETVEKDIMFGpmNLGVTEKEAKTRARAAI---NLVGLPE----EILEKSPFdLSGGQMRRVAIAGVL 160
Cdd:PRK10789 392 AVVSQTP--FLFSDTVANNIALG--RPDATQQEIEHVARLASvhdDILRLPQgydtEVGERGVM-LSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMdlfYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQIL---HNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-205 |
1.15e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeknlkgvrEKVGIVFQFPEHQL 98
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD-----------PDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 99 F---EETVEKDIMFGPMNLGVTEkeakTRARAAINLVGLPEeiLEKSPF-DLSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:PRK13539 83 AmkpALTVAENLEFWAAFLGGEE----LDIAAALEAVGLAP--LAHLPFgYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|.
gi 2119195095 175 GLDPRGRKEIMDLFySLHKKRNLSTVLVTHS 205
Cdd:PRK13539 157 ALDAAAVALFAELI-RAHLAQGGIVIAATHI 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-222 |
1.25e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkeknLKGVREK----VGIVFQfpEHQ 97
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-------FASTTAAlaagVAIIYQ--ELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEE-TVEKDIMFG--PMNLGVTEKEAkTRARAAINLVGLPEEILEKSPF-DLSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:PRK11288 90 LVPEmTVAENLYLGqlPHKGGIVNRRL-LNYEAREQLEHLGVDIDPDTPLkYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 174 AGLDPRgrkEIMDLFYSLHKKRNLSTVL--VTHSMEDAARYADDIVVMHQG 222
Cdd:PRK11288 169 SSLSAR---EIEQLFRVIRELRAEGRVIlyVSHRMEEIFALCDAITVFKDG 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-204 |
1.64e-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: 78.55 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKE--------------KNLKGVR 84
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphenilylghlpglKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 85 EKvgIVFQFPEHQLFEETVEKdimfgpmnlgvtekeaktrARAAINLVGLpeeilEKSPF-DLSGGQMRRVAIAGVLAME 163
Cdd:TIGR01189 92 EN--LHFWAAIHGGAQRTIED-------------------ALAAVGLTGF-----EDLPAaQLSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119195095 164 PEVIVLDEPTAGLDPRGRKEIMDLFYSlHKKRNLSTVLVTH 204
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRA-HLARGGIVLLTTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-285 |
1.64e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.90 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgRKEKNLKgvreKVGIVF-QfpEHQLF- 99
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFAR----RIGVVFgQ--RSQLWw 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 ----EETVE--KDIMfgpmnlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:COG4586 110 dlpaIDSFRllKAIY------RIPDAEYKKRLDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 174 AGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI---FSNPKAL-LELGLDVPE 249
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELkerFGPYKTIvLELAEPVPP 262
|
250 260 270
....*....|....*....|....*....|....*....
gi 2119195095 250 VV---GLQLKIEEAFNTKFSKIslSEEELAEMVAEFMER 285
Cdd:COG4586 263 LElprGGEVIEREGNRVRLEVD--PRESLAEVLARLLAR 299
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-237 |
1.20e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFErlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREiraGRKEKNLKG 82
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVE--IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH---NLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFGPMNLGVTE------------------KEAKTRARAAINL------------- 131
Cdd:PTZ00265 458 WRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknKRNSCRAKCAGDLndmsnttdsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 132 ---------------------------VGLP---EEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:PTZ00265 536 emrknyqtikdsevvdvskkvlihdfvSALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 182 KEIMDLFYSLHKKRNLSTVLVTHSMEdAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-235 |
2.04e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQFPehQLFEE 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFP--VLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVekdIM--FGPMN-LGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:PRK15056 100 VV---MMgrYGHMGwLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 179 RGRKEIMDLFYSLHKKRnlSTVLV-THSMEDAARYAdDIVVMHQGEVFTKGTPEQIFS 235
Cdd:PRK15056 176 KTEARIISLLRELRDEG--KTMLVsTHNLGSVTEFC-DYTVMVKGTVLASGPTETTFT 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-177 |
2.64e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 5 LKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgSREIRAGRKEKN----- 79
Cdd:COG0488 1 LENLSKSFGG-----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLRIGYLPQEppldd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 80 --------LKGVREKVGIVFQFPEHQLFEETVEKDIM--------FGPMNlgvtEKEAKTRARAAINLVGLPEEILEKSP 143
Cdd:COG0488 75 dltvldtvLDGDAELRALEAELEELEAKLAEPDEDLErlaelqeeFEALG----GWEAEARAEEILSGLGFPEEDLDRPV 150
|
170 180 190
....*....|....*....|....*....|....
gi 2119195095 144 FDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-238 |
3.68e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGsVLIGSREIRAGRkeknlkg 82
Cdd:PRK09544 5 VSLENVSVSFG-----QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGKLRIGY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPEhqlfeeTVEKDIMFGPmnlGVTEKE---AKTRARAAiNLVGLPeeiLEKspfdLSGGQMRRVAIAGV 159
Cdd:PRK09544 72 VPQKLYLDTTLPL------TVNRFLRLRP---GTKKEDilpALKRVQAG-HLIDAP---MQK----LSGGETQRVLLARA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQgEVFTKGTPEQIFSNPK 238
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-233 |
5.57e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEknlkgVREKVGIVFQ-FpehQLFE 100
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA-----TRRRVGYMSQaF---SLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 E-TVEKdimfgpmNL-------GVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAgvLAM--EPEVIVLD 170
Cdd:NF033858 353 ElTVRQ-------NLelharlfHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLA--VAVihKPELLILD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 171 EPTAGLDPRGRkeimDLFYSLHKKrnLS-----TVLV-THSMEDAARyADDIVVMHQGEVFTKGTPEQI 233
Cdd:NF033858 423 EPTSGVDPVAR----DMFWRLLIE--LSredgvTIFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-222 |
2.29e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVFQFPehQLFEET 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP--WLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 103 VEKDIMFG-PMNlgvtekeaKTRARAAINLVGLPEEIlEKSPF-----------DLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:cd03290 95 VEENITFGsPFN--------KQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 171 EPTAGLDPRGRKEIMD---LFYSLHKKRNLstVLVTHSMEdAARYADDIVVMHQG 222
Cdd:cd03290 166 DPFSALDIHLSDHLMQegiLKFLQDDKRTL--VLVTHKLQ-YLPHADWIIAMKDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-224 |
3.94e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 24 SDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgRKEKNlkgvREKVGIVFqFPE----HQLF 99
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA-LSTAQ----RLARGLVY-LPEdrqsSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETVEK----DIMFGPMNLGV-TEKEAKT--RARAAInlvGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:PRK15439 354 LDAPLAwnvcALTHNRRGFWIkPARENAVleRYRRAL---NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 173 TAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-236 |
4.71e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqaDSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsreiragrkeknlkg 82
Cdd:PLN03130 615 ISIKNGYFSW--DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFG-PMNlgvtekeaKTRARAAINLVGLPE-----------EILEKSpFDLSGGQ 150
Cdd:PLN03130 677 IRGTVAYVPQVS--WIFNATVRDNILFGsPFD--------PERYERAIDVTALQHdldllpggdltEIGERG-VNISGGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 151 MRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMD--LFYSLHKKrnlSTVLVTHSMEDAArYADDIVVMHQGEVFTKG 228
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLS-QVDRIILVHEGMIKEEG 821
|
....*...
gi 2119195095 229 TPEQIFSN 236
Cdd:PLN03130 822 TYEELSNN 829
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-233 |
4.77e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspfeRLAISDVSIDVPSGTYLAVIGHTGSGKSTVLqhlnallkptkgSVLIGSREIRAGRKE---KN 79
Cdd:NF033858 2 ARLEGVSHRYGK-----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLL------------SLIAGARKIQQGRVEvlgGD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 80 L--KGVREKVG--IVFqFPE---HQLFEE-TVEKDI-----MFGpmnLGVTEKEAK----TRAraainlVGLpeeilekS 142
Cdd:NF033858 65 MadARHRRAVCprIAY-MPQglgKNLYPTlSVFENLdffgrLFG---QDAAERRRRidelLRA------TGL-------A 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 143 PF------DLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLV-THSMEDAARYaDD 215
Cdd:NF033858 128 PFadrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEAERF-DW 206
|
250
....*....|....*...
gi 2119195095 216 IVVMHQGEVFTKGTPEQI 233
Cdd:NF033858 207 LVAMDAGRVLATGTPAEL 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-233 |
1.44e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.85 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSG--KSTVLQHLNAllkPTKGSvligsREIRAGRKEKNLKGVREKVGIvfQFPEHQLF 99
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR-----RPWRF*TWCANRRALRRTIG*--HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETV---EKDIMFGpMNLGVTEKEAKTRARAAINLVGLPEEIlEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGL 176
Cdd:NF000106 98 RESFsgrENLYMIG-R*LDLSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 177 DPRGRKEIMDLFYSLhkKRNLSTVLV-THSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:NF000106 176 DPRTRNEVWDEVRSM--VRDGATVLLtTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-236 |
3.48e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKnlkgvREKVGIVFQFPEHQLF 99
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-----RARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETVEKDIMFGPMNL--GVTEKEAKTRAraainlvglpEEILEKSPFD---------LSGGQMRRVAIAGVLAMEPEVIV 168
Cdd:PRK10895 91 RRLSVYDNLMAVLQIrdDLSAEQREDRA----------NELMEEFHIEhlrdsmgqsLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 169 LDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSN 236
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-224 |
4.14e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkeknLKGVRE--KVGIVFqFPE---H 96
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-------IRSPRDaiRAGIAY-VPEdrkG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 Q-LF-EETVEKDIMFGPM----NLG-VTEKEAKTRARAAINLVGL----PEEILEkspfDLSGGQMRRVAIAGVLAMEPE 165
Cdd:COG1129 339 EgLVlDLSIRENITLASLdrlsRGGlLDRRRERALAEEYIKRLRIktpsPEQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 166 VIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-204 |
4.90e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.06 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKE--------------KNLKGVR 84
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiargllylghapgiKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 85 EKvgIVFQFPEHQlfEETVEKdimfgpmnlgvtekeaktrARAAINLVGLpeeilEKSPFD-LSGGQMRRVAIAGVLAME 163
Cdd:cd03231 92 EN--LRFWHADHS--DEQVEE-------------------ALARVGLNGF-----EDRPVAqLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2119195095 164 PEVIVLDEPTAGLDPRGRKEIMDLFYSlHKKRNLSTVLVTH 204
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAG-HCARGGMVVLTTH 183
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-223 |
9.08e-14 |
|
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: 67.09 E-value: 9.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSreiragrkeknlkg 82
Cdd:cd03221 1 IELENLSKTYG-----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vREKVGIVFQfpehqlfeetvekdimfgpmnlgvtekeaktraraainlvglpeeilekspfdLSGGQMRRVAIAGVLAM 162
Cdd:cd03221 62 -TVKIGYFEQ-----------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFysLHKKRNLstVLVTHSmedaaRY-----ADDIVVMHQGE 223
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEAL--KEYPGTV--ILVSHD-----RYfldqvATKIIELEDGK 144
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-224 |
1.23e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLigsreiragrKEKNLKGVREKVGIVfqfpehqlfEETVE 104
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------AERSIAYVPQQAWIM---------NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 105 KDIMF----GPMNLG----VTEKEAKTRARAAinlvGLPEEILEKSpFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGL 176
Cdd:PTZ00243 739 GNILFfdeeDAARLAdavrVSQLEADLAQLGG----GLETEIGEKG-VNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119195095 177 DPR-GRKEIMDLFY-SLHKKrnlSTVLVTHSMEDAARyADDIVVMHQGEV 224
Cdd:PTZ00243 814 DAHvGERVVEECFLgALAGK---TRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-236 |
1.34e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYqaDSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsreiragrkeknlkg 82
Cdd:PLN03232 615 ISIKNGYFSW--DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV---------------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDIMFGpmnlgvtEKEAKTRARAAINLVGLPE-----------EILEKSpFDLSGGQM 151
Cdd:PLN03232 677 IRGSVAYVPQVS--WIFNATVRENILFG-------SDFESERYWRAIDVTALQHdldllpgrdltEIGERG-VNISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSlHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPE 231
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFA 824
|
....*
gi 2119195095 232 QIFSN 236
Cdd:PLN03232 825 ELSKS 829
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-222 |
1.77e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-RAGRKEKNLKGvrekVGIVFQfpEHQLFE 100
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDHKLAAQLG----IGIIYQ--ELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 E-TVEKDIMFGPMN----LGVTEKE-AKTRARAAINL--VGLPEEILEKSPfDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:PRK09700 94 ElTVLENLYIGRHLtkkvCGVNIIDwREMRVRAAMMLlrVGLKVDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 173 TAGLDprgRKEIMDLFYSLH--KKRNLSTVLVTHSMEDAARYADDIVVMHQG 222
Cdd:PRK09700 173 TSSLT---NKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-240 |
1.83e-13 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 70.43 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 119 KEAKTRARAAINlVGLPEEILEKSPFDLSGGQMRRVAIA--------GVLamepevIVLDEPTAGLDPRGRKEIMDLFYS 190
Cdd:TIGR00630 463 KEIRERLGFLID-VGLDYLSLSRAAGTLSGGEAQRIRLAtqigsgltGVL------YVLDEPSIGLHQRDNRRLINTLKR 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 191 LHKKRNlsTVLVTHSMEDAARYADDIVVM------HQGEVFTKGTPEQIFSNPKAL 240
Cdd:TIGR00630 536 LRDLGN--TLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILANPDSL 589
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-251 |
2.43e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPT--------KGSVLIGSREIRA--GRKEKNLKGVREKVGi 89
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAidAPRLARLRAVLPQAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 90 vfqfpeHQLFEETVEKDIMFG----PMNLGVTEKEAKTRARAAINLVGlPEEILEKSPFDLSGGQMRRVAIAGVLAM--- 162
Cdd:PRK13547 93 ------QPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAG-ATALVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 ------EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTP------ 230
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPadvltp 245
|
250 260
....*....|....*....|....
gi 2119195095 231 ---EQIFSNPKALLELGLDVPEVV 251
Cdd:PRK13547 246 ahiARCYGFAVRLVDAGDGVPPVI 269
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-225 |
3.09e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLK--PTKGSVLIGSREIRagrkeknl 80
Cdd:COG2401 31 LEAFGVELRVV-----ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 kgvREKVGIvfqfpehqlfeETVEKDimfGPMNLGVtekeaktrarAAINLVGLPEEILEKSPFD-LSGGQMRRVAIAGV 159
Cdd:COG2401 98 ---REASLI-----------DAIGRK---GDFKDAV----------ELLNAVGLSDAVLWLRRFKeLSTGQKFRFRLALL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVM-HQGEVF 225
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvGYGGVP 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-249 |
3.50e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRYQADSPFERLaISDVSIDVPSGTYLAVIGHTGSGKSTVLqhlNALL-KPTKGSVLIGSREIRaGRKeKNL 80
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAfRSPKGVKGSGSVLLN-GMP-IDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 81 KGVREKVGIVFQfpeHQLF--EETVEKDIMFGP---MNLGVTEKEAKTRARAAINLVGLPE--------EILEKSpfdLS 147
Cdd:TIGR00955 95 KEMRAISAYVQQ---DDLFipTLTVREHLMFQAhlrMPRRVTKKEKRERVDEVLQALGLRKcantrigvPGRVKG---LS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 148 GGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHSMEDAARYA--DDIVVMHQGEVF 225
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG--KTIICTIHQPSSELFElfDKIILMAEGRVA 246
|
250 260
....*....|....*....|....
gi 2119195095 226 TKGTPEQIfsnPKALLELGLDVPE 249
Cdd:TIGR00955 247 YLGSPDQA---VPFFSDLGHPCPE 267
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-235 |
6.10e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRY--QADSPFERlaisDVSIDVPSGTYLAVIGHTGSGKSTVLQHL--------------------------- 53
Cdd:PTZ00265 1166 IEIMDVNFRYisRPNVPIYK----DLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 54 ---------------------------NALLKPTKGSVLIGSREIragrKEKNLKGVREKVGIVFQFPehQLFEETVEKD 106
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgeDSTVFKNSGKILLDGVDI----CDYNLKDLRNLFSIVSQEP--MLFNMSIYEN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 107 IMFGPMNlgVTEKEAKTRAR-AAInlvglpEEILEKSP--FD---------LSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:PTZ00265 1316 IKFGKED--ATREDVKRACKfAAI------DEFIESLPnkYDtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119195095 175 GLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGE-----VFTKGTPEQIFS 235
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDrtgsfVQAHGTHEELLS 1452
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
146-224 |
8.38e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 8.38e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 146 LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-236 |
1.11e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLkgvREKVGIVfqfPE-HQLFE 100
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM---REAVAIV---PEgRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 101 E-TVEKDIMFGpmNLGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPR 179
Cdd:PRK11614 94 RmTVEENLAMG--GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 180 GRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSN 236
Cdd:PRK11614 172 IIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-223 |
4.34e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLK--PTKGSVLIGSREIRAgrkeknlKGVR--EKVGIVFQFPEHQ 97
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKA-------SNIRdtERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEE-TVEKDIMFG---PMNLGVTEKEAKT-RARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:TIGR02633 89 LVPElSVAENIFLGneiTLPGGRMAYNAMYlRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 173 TAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-233 |
6.10e-12 |
|
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: 66.19 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkekNLKGVREKVGIVFQFPEHQLFEE 101
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----NISDVHQNMGYCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGR 181
Cdd:TIGR01257 2029 GREHLYLYARLR-GVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 182 KEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQI 233
Cdd:TIGR01257 2107 RMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-236 |
6.93e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRagrkEKNLKG 82
Cdd:PLN03130 1238 IKFEDVVLRYRPELP---PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS----KFGLMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDImfGPMNlgvtEK------EAKTRA--RAAI--NLVGLPEEILEKSPfDLSGGQMR 152
Cdd:PLN03130 1311 LRKVLGIIPQAP--VLFSGTVRFNL--DPFN----EHndadlwESLERAhlKDVIrrNSLGLDAEVSEAGE-NFSVGQRQ 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 153 RVAIAGVLAMEPEVIVLDEPTAGLDPRG----RKEIMDLFYSlhkkrnlSTVLVTHSMEDAARYADDIVVMHQGEVFTKG 228
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTdaliQKTIREEFKS-------CTMLIIAHRLNTIIDCDRILVLDAGRVVEFD 1454
|
....*...
gi 2119195095 229 TPEQIFSN 236
Cdd:PLN03130 1455 TPENLLSN 1462
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-229 |
9.10e-12 |
|
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: 65.32 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLigsreiRAGRkeknlkgvrekVGIVFQFPehQLFEET 102
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGR-----------ISFSPQTS--WIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 103 VEKDIMFgpmnlGVTEKEakTRARAAINLVGLPEEIL-----EKSPF-----DLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:TIGR01271 503 IKDNIIF-----GLSYDE--YRYTSVIKACQLEEDIAlfpekDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 173 TAGLDPRGRKEImdlFYSLHKK--RNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGT 229
Cdd:TIGR01271 576 FTHLDVVTEKEI---FESCLCKlmSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGT 630
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-204 |
1.20e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 7 NVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRK--EKNLKGVR 84
Cdd:PRK13540 6 ELDFDYH-----DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 85 EKVGIvfqfPEHQLFEETVEKDIMFGPMNLGVTEkeaktraraAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEP 164
Cdd:PRK13540 81 HRSGI----NPYLTLRENCLYDIHFSPGAVGITE---------LCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2119195095 165 EVIVLDEPTAGLDPRGRKEIMDLFYSlHKKRNLSTVLVTH 204
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-223 |
1.44e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQAdspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKG 82
Cdd:PRK10522 323 LELRNVTFAYQD----NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA----EQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEETVEKdimfgpmnlgvtEKEAKTRARAAINLVGLpeEILEKSPFD--------LSGGQMRRV 154
Cdd:PRK10522 395 YRKLFSAVFT--DFHLFDQLLGP------------EGKPANPALVEKWLERL--KMAHKLELEdgrisnlkLSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHsmEDAarY---ADDIVVMHQGE 223
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH--DDH--YfihADRLLEMRNGQ 526
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-231 |
2.12e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.39 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLqhlNALL-----KPTKGSVLIGSREI-------RAgrkeknlkgvREKVGIVFQ 92
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLA---KVLMghpkyEVTSGSILLDGEDIlelspdeRA----------RAGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 93 FPEH------QLFEETVEKDIMFGPMNLgvteKEAKTRARAAINLVGLPEEILEKSPFD-LSGGQMRRVAIAGVLAMEPE 165
Cdd:COG0396 85 YPVEipgvsvSNFLRTALNARRGEELSA----REFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 166 VIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSmedaAR-----YADDIVVMHQGEVFTKGTPE 231
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHY----QRildyiKPDFVHVLVDGRIVKSGGKE 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-228 |
2.17e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLqhlNALLKPTKGSVLIGSREIRAGrkeKNLKGVREKVGIVFQ----FP 94
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNR---KPTKQILKRTGFVTQddilYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 EHQLFEETVEKDIMFGPMNLgvtEKEAKTR-ARAAINLVGLP--EEILEKSPF--DLSGGQMRRVAIAGVLAMEPEVIVL 169
Cdd:PLN03211 154 HLTVRETLVFCSLLRLPKSL---TKQEKILvAESVISELGLTkcENTIIGNSFirGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 170 DEPTAGLDPRGRKEIMDLFYSLHKKrnlSTVLVTHSMEDAARYA---DDIVVMHQGEV--FTKG 228
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQK---GKTIVTSMHQPSSRVYqmfDSVLVLSEGRClfFGKG 291
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-243 |
2.29e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVligsreiragrkekNLKG 82
Cdd:TIGR00957 637 ITVHNATFTWARDLP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------HMKG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vreKVGIVFQfpEHQLFEETVEKDIMFG-PMNlgvtEKEAKTRARAAI---NLVGLPE----EILEKSpFDLSGGQMRRV 154
Cdd:TIGR00957 700 ---SVAYVPQ--QAWIQNDSLRENILFGkALN----EKYYQQVLEACAllpDLEILPSgdrtEIGEKG-VNLSGGQKQRV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMD-LFYSLHKKRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQI 233
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQEL 848
|
250
....*....|
gi 2119195095 234 FSNPKALLEL 243
Cdd:TIGR00957 849 LQRDGAFAEF 858
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-236 |
5.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:PLN03232 1235 IKFEDVHLRYRPGLP---PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV----AKFGLTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEKDI-MFGPMN-LGVTEKEAKTRARAAI--NLVGLPEEILEKSPfDLSGGQMRRVAIAG 158
Cdd:PLN03232 1308 LRRVLSIIPQSP--VLFSGTVRFNIdPFSEHNdADLWEALERAHIKDVIdrNPFGLDAEVSEGGE-NFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 159 VLAMEPEVIVLDEPTAGLDPRG----RKEIMDLFyslhkkRNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGTPEQIF 234
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTdsliQRTIREEF------KSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
..
gi 2119195095 235 SN 236
Cdd:PLN03232 1458 SR 1459
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-229 |
5.97e-11 |
|
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: 61.80 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLigsreiRAGRkeknlkgvrekvgIVFQFPEHQLFEET 102
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK------HSGR-------------ISFSSQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 103 VEKDIMFGpmnlgVTEKEakTRARAAINLVGLPEEILEKSPFD----------LSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:cd03291 114 IKENIIFG-----VSYDE--YRYKSVVKACQLEEDITKFPEKDntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 173 TAGLDPRGRKEImdlFYSLHKK--RNLSTVLVTHSMEDAARyADDIVVMHQGEVFTKGT 229
Cdd:cd03291 187 FGYLDVFTEKEI---FESCVCKlmANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGT 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-224 |
6.07e-11 |
|
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: 62.53 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHL-NALLKPTKGSVLIGSREIRAgrkEKNLKGVREKVGIVfqfPEHQLFEE 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDI---RNPAQAIRAGIAMV---PEDRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 TVEKDIMFGPMNLGVTEKEA-KTRARAAINLVGLPEEILE-----KSPF----DLSGGQMRRVAIAGVLAMEPEVIVLDE 171
Cdd:TIGR02633 350 IVPILGVGKNITLSVLKSFCfKMRIDAAAELQIIGSAIQRlkvktASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 172 PTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-224 |
8.55e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQadspfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGsreiragrkeknlkg 82
Cdd:COG0488 316 LELEGLSKSYG-----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG--------------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vrEKVGIVFqFPEHQLF---EETVEKDIMfgpmnlGVTEKEAKTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGV 159
Cdd:COG0488 376 --ETVKIGY-FDQHQEEldpDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 160 LAMEPEVIVLDEPTAGLDPRGRKEIMDLfyslhkkrnLST-----VLVTHsmeDaaRY-----ADDIVVMHQGEV 224
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEA---------LDDfpgtvLLVSH---D--RYfldrvATRILEFEDGGV 507
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-224 |
1.72e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 4 SLKNVEYRyqadSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREI-RAGRKEKNLKG 82
Cdd:COG3845 259 EVENLSVR----DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 V------REKVGIVFQFPehqLFEETVEKDIMFGPMNLGVTEKEAKTRARAainlvglpEEILEKspFD----------- 145
Cdd:COG3845 335 VayipedRLGRGLVPDMS---VAENLILGRYRRPPFSRGGFLDRKAIRAFA--------EELIEE--FDvrtpgpdtpar 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 146 -LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRG----RKEIMDLfyslhKKRNLSTVLVTHSMEDAARYADDIVVMH 220
Cdd:COG3845 402 sLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiefiHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMY 476
|
....
gi 2119195095 221 QGEV 224
Cdd:COG3845 477 EGRI 480
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-205 |
1.79e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 58.32 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRyqadSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVligsreiragrkeknlkg 82
Cdd:cd03223 1 IELENLSLA----TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vrekvgivfQFPEHqlfeetveKDIMFGP----MNLGvtekeaktRARAAINLvglpeeileksPFD--LSGGQMRRVAI 156
Cdd:cd03223 59 ---------GMPEG--------EDLLFLPqrpyLPLG--------TLREQLIY-----------PWDdvLSGGEQQRLAF 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2119195095 157 AGVLAMEPEVIVLDEPTAGLDPrgrkEIMDLFYSLHKKRnLSTVL-VTHS 205
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKEL-GITVIsVGHR 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-177 |
5.32e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 36 LAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSR------EIRA---GRKEKNLKGVREKVGivfqfpEHQLFEETVEkd 106
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYIKPdydGTVEDLLRSITDDLG------SSYYKSEIIK-- 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 107 imfgPMNLgvtekeaktraraainlvglpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PRK13409 440 ----PLQL---------------------ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
122-249 |
5.37e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 60.23 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 122 KTRARAAINLvGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVI--VLDEPTAGLDPRGRKEIMDLFYSLHKKRNlST 199
Cdd:PRK00635 454 KSRLSILIDL-GLPYLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGN-TV 531
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 200 VLVTHSmEDAARYADDIV------VMHQGEVFTKGTPEQIFSNPKALL------ELGLDVPE 249
Cdd:PRK00635 532 LLVEHD-EQMISLADRIIdigpgaGIFGGEVLFNGSPREFLAKSDSLTakylrqELTIPIPE 592
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-222 |
6.01e-10 |
|
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: 57.64 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVeyRYQADSPFERLAI-SDVSIDVPSGTYLAVIGHTGSGKSTVLqhlNALLKPTKGSVLIGSREIRAGRKEKNLk 81
Cdd:cd03232 4 LTWKNL--NYTVPVKGGKRQLlNNISGYVKPGTLTALMGESGAGKTTLL---DVLAGRKTAGVITGEILINGRPLDKNF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 gvREKVGIVFQFPEHqLFEETVEKDIMFgpmnlgvtekEAKTRAraainlvglpeeilekspfdLSGGQMRRVAIAGVLA 161
Cdd:cd03232 78 --QRSTGYVEQQDVH-SPNLTVREALRF----------SALLRG--------------------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 162 MEPEVIVLDEPTAGLDPRGRKEIMDLFyslhkkRNLS----TVLVTHSMEDAA--RYADDIVVMHQG 222
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFL------KKLAdsgqAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-240 |
1.02e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 8 VEYRYQADSPferLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKGVREKV 87
Cdd:PTZ00243 1314 VQMRYREGLP---LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA----YGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 88 GIVFQFPehQLFEETVEKDImfGPMnLGVTEKEaktrARAAINLVGLPEEILEKSP----------FDLSGGQMRRVAIA 157
Cdd:PTZ00243 1387 SMIPQDP--VLFDGTVRQNV--DPF-LEASSAE----VWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 158 -GVLAMEPEVIVLDEPTAGLDPRGRKEI----MDLFyslhkkRNLSTVLVTHSMEDAARYaDDIVVMHQGEVFTKGTPEQ 232
Cdd:PTZ00243 1458 rALLKKGSGFILMDEATANIDPALDRQIqatvMSAF------SAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRE 1530
|
....*...
gi 2119195095 233 IFSNPKAL 240
Cdd:PTZ00243 1531 LVMNRQSI 1538
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-223 |
1.07e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLkPT---KGSVLIGSREIRAgrkeknlKGVR--EKVGIVFQFPEH 96
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA-------SNIRdtERAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 97 QLFEE-TVEKDIMFG--PMNLGVTEKEAKT-RARAAINLVGLPEEILEKSpFDLSGGQMRRVAIAGVLAMEPEVIVLDEP 172
Cdd:PRK13549 92 ALVKElSVLENIFLGneITPGGIMDYDAMYlRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 173 TAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:PRK13549 171 TASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
132-228 |
1.15e-09 |
|
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: 57.27 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 132 VGLPEEILEKSPFDLSGGQMRRVAIAGVLAME-PEVI-VLDEPTAGLDPRGRKEIMDlfySLHKKRNL-STVLVTHSMED 208
Cdd:cd03270 124 VGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIE---TLKRLRDLgNTVLVVEHDED 200
|
90 100
....*....|....*....|....*.
gi 2119195095 209 AARYADDIVVM------HQGEVFTKG 228
Cdd:cd03270 201 TIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-188 |
1.69e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 2 DISLKNVEYRyqadSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVligsreiragrkeknlk 81
Cdd:COG4178 362 ALALEDLTLR----TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 gvrekvgivfQFPEHQlfeetvekDIMFGP----MNLGvTEKEA-----------KTRARAAINLVGLP---EEILEKSP 143
Cdd:COG4178 421 ----------ARPAGA--------RVLFLPqrpyLPLG-TLREAllypataeafsDAELREALEAVGLGhlaERLDEEAD 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119195095 144 FD--LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLF 188
Cdd:COG4178 482 WDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-177 |
1.73e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREiragrkeknlkgvreKVGIVFQFPEHQL 98
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------------KLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 99 FEETVEKDIMFGPMNLGVTEKEAKTRAR-AAINLVGLPEEileKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRAYvGRFNFKGSDQQ---KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-231 |
2.01e-09 |
|
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: 56.00 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLQHL--NALLKPTKGSVLigsreiragrkeknLKGvrekvgivfqfpehqlfeet 102
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEIL--------------FKG-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 103 veKDIMfgpmNLGVTEkeaktRARAAINLV-GLPEEILEKSPFDL--------SGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:cd03217 64 --EDIT----DLPPEE-----RARLGIFLAfQYPPEIPGVKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 174 AGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHsMEDAARY--ADDIVVMHQGEVFTKGTPE 231
Cdd:cd03217 133 SGLDIDALRLVAEVINKL-REEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-245 |
4.01e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 24 SDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSRE---------IRAG-------RKEKnlkgvrekv 87
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPidirsprdaIRAGimlcpedRKAE--------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 88 GIVfqfPEHqlfeeTVEKDI---------MFGPMNLGVTEKEAKTRARAAINLvglpeeileKSP------FDLSGGQMR 152
Cdd:PRK11288 341 GII---PVH-----SVADNInisarrhhlRAGCLINNRWEAENADRFIRSLNI---------KTPsreqliMNLSGGNQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 153 RVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQ 232
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
250
....*....|...
gi 2119195095 233 ifSNPKALLELGL 245
Cdd:PRK11288 483 --ATERQALSLAL 493
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-177 |
5.83e-09 |
|
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: 56.72 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 33 GTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSR------EIRA---GRKEKNLKGVREKvgivfQFPEHQLFEETV 103
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqYISPdydGTVEEFLRSANTD-----DFGSSYYKTEII 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119195095 104 EkdimfgPMNLgvtekeaktraraainlvglpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:COG1245 441 K------PLGL---------------------EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-232 |
7.31e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.11 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTY-----LAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgsreiragrkeknlkgVREKVGIVFQFPEHQlF 99
Cdd:cd03237 12 EFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI----------------ELDTVSYKPQYIKAD-Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETVEkDIMFGPMNLGVTEKEAKTRAraaINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPR 179
Cdd:cd03237 75 EGTVR-DLLSSITKDFYTHPYFKTEI---AKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 180 GR----KEIMDlfYSLHKKrnlSTVLVTHSMEDAARYADDIVVMHQGE--VFTKGTPEQ 232
Cdd:cd03237 150 QRlmasKVIRR--FAENNE---KTAFVVEHDIIMIDYLADRLIVFEGEpsVNGVANPPQ 203
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
146-240 |
7.73e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 56.23 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 146 LSGGQMRRVAIA--------GVLamepevIVLDEPTAGLDPRgrkeimD---LFYSLHKKRNL-STVLVTHSMEDAARYA 213
Cdd:PRK00349 490 LSGGEAQRIRLAtqigsgltGVL------YVLDEPSIGLHQR------DndrLIETLKHLRDLgNTLIVVEHDEDTIRAA 557
|
90 100 110
....*....|....*....|....*....|...
gi 2119195095 214 DDIVVM------HQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK00349 558 DYIVDIgpgagvHGGEVVASGTPEEIMKNPNSL 590
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-223 |
8.10e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrkekNLKGVREK----VGIVFQfPEHQ 97
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-------DFKSSKEAlengISMVHQ-ELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEETVEKDIMFG--PMN-LGVTEKEAKTRARAAINLVGLPEEILEKSPfDLSGGQMRRVAIAGVLAMEPEVIVLDEPTA 174
Cdd:PRK10982 85 VLQRSVMDNMWLGryPTKgMFVDQDKMYRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2119195095 175 GLDprgRKEIMDLFYSLHK--KRNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:PRK10982 164 SLT---EKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-224 |
1.11e-08 |
|
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: 55.57 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkeKNLKG 82
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA----DNREA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQfpEHQLFEEtvekdimfgpmNLGVTEKEAKTRARAAINLVglpeEILEK--------SPFDLSGGQMRRV 154
Cdd:COG4615 404 YRQLFSAVFS--DFHLFDR-----------LLGLDGEADPARARELLERL----ELDHKvsvedgrfSTTDLSQGQRKRL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 155 AIAGVLAMEPEVIVLDEPTAGLDPRGRKeimdLFY-----SLhKKRNLSTVLVTHsmEDaaRY---ADDIVVMHQGEV 224
Cdd:COG4615 467 ALLVALLEDRPILVFDEWAADQDPEFRR----VFYtellpEL-KARGKTVIAISH--DD--RYfdlADRVLKMDYGKL 535
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-242 |
1.48e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 23 ISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAgrkEKNLKGVREKVGIV------------ 90
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP---RSPLDAVKKGMAYItesrrdngffpn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 91 FQFPEHQLFEETVEKDIMFGPMNLGVTEKEAKTrARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLD 170
Cdd:PRK09700 356 FSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRT-AENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 171 EPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVftkgtpEQIFSNPKALLE 242
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRDDMSE 499
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-177 |
4.17e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 1 MDISLKNVEYRYQADSPFER-----LAISDVSIDVPSG--------------TYLAVIGHTGSGKSTVLQHLNALLKPTK 61
Cdd:PLN03073 484 VDAVVNDPDYKFEFPTPDDRpgppiISFSDASFGYPGGpllfknlnfgidldSRIAMVGPNGIGKSTILKLISGELQPSS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 62 GSVLigsreiragRKEKnlkgVREKVgivfqFPEHQLFEETVEKDIMFGPMNL--GVTEKeaktRARAAINLVGLPEEIL 139
Cdd:PLN03073 564 GTVF---------RSAK----VRMAV-----FSQHHVDGLDLSSNPLLYMMRCfpGVPEQ----KLRAHLGSFGVTGNLA 621
|
170 180 190
....*....|....*....|....*....|....*...
gi 2119195095 140 EKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PLN03073 622 LQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-237 |
9.30e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLkPTKGSVLIGSREIRAGRKEKnLKGVR----EKVGIVFQFPEHQLFEe 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAE-LARHRaylsQQQTPPFAMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 tvekdiMFGPMnlGVTEKEAKTRARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL-----AMEPE--VIVLDEPTA 174
Cdd:PRK03695 92 ------LHQPD--KTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 175 GLDPrGRKEIMDLFYSLHKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNP 237
Cdd:PRK03695 163 SLDV-AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-222 |
1.18e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTvlqhlnaLLKptkgsVLIG-------SREIRAGRKEKNLKGVR--EKVGIVFQ 92
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKST-------LMK-----VLSGvyphgsyEGEILFDGEVCRFKDIRdsEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 93 FPEHQLFEE-TVEKDIMFG--PMNLGVTE-KEAKTRARAAINLVGLPEeilekSPF----DLSGGQMRRVAIAGVLAMEP 164
Cdd:NF040905 84 HQELALIPYlSIAENIFLGneRAKRGVIDwNETNRRARELLAKVGLDE-----SPDtlvtDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119195095 165 EVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQG 222
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-177 |
1.94e-07 |
|
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: 51.86 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 17 PFERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIgSREIRAGR-------------KEKNLKGV 83
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIKVGYlpqepqldptktvRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 84 REKVGIVFQFPE--HQLFEETVEKDIMFGPMnlgvTEKEAKTRARAAINL---VGLPEEILEKSPFD-----LSGGQMRR 153
Cdd:TIGR03719 94 AEIKDALDRFNEisAKYAEPDADFDKLAAEQ----AELQEIIDAADAWDLdsqLEIAMDALRCPPWDadvtkLSGGERRR 169
|
170 180
....*....|....*....|....
gi 2119195095 154 VAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
146-233 |
2.27e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 146 LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVf 225
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL- 483
|
90
....*....|....*
gi 2119195095 226 tKG-------TPEQI 233
Cdd:PRK13549 484 -KGdlinhnlTQEQV 497
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-238 |
2.52e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 33 GTYLAVIGHTGSGKSTVLQHLNALLKPT-----------------KGSVL------IGSREIRAGRK-------EKNLKG 82
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELqnyfkkLYNGEIKVVHKpqyvdliPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 vreKVGivfqfpehQLFEETVEKDIMfgpmnlgvtekeaktraRAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVLAM 162
Cdd:PRK13409 179 ---KVR--------ELLKKVDERGKL-----------------DEVVERLGL-ENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 163 EPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRnlSTVLVTHsmeDAA---RYADDIVVMHqgevftkGTPEQ--IFSNP 237
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEH---DLAvldYLADNVHIAY-------GEPGAygVVSKP 297
|
.
gi 2119195095 238 K 238
Cdd:PRK13409 298 K 298
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-177 |
3.49e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSReiragrkeknlkgVreKVGIVFQFPEHQL 98
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET-------------V--KLAYVDQSRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 99 FEETVEKDIMFGPMNLGVTEKEAKTRAR-AAINLVGlPEEilEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PRK11819 401 PNKTVWEEISGGLDIIKVGNREIPSRAYvGRFNFKG-GDQ--QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-235 |
3.77e-07 |
|
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: 51.48 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 3 ISLKNVEYRYQADSPFerlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIragrKEKNLKG 82
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDL---VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----AKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 83 VREKVGIVFQFPehQLFEETVEkdimfgpMNLGVTEKEAKTRARAAINLV-----------GLPEEILEKSPfDLSGGQM 151
Cdd:TIGR00957 1358 LRFKITIIPQDP--VLFSGSLR-------MNLDPFSQYSDEEVWWALELAhlktfvsalpdKLDHECAEGGE-NLSVGQR 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 152 RRVAIAGVLAMEPEVIVLDEPTAGLDprgrKEIMDLFYS-LHKKRNLSTVL-VTHSMEDAARYAdDIVVMHQGEVFTKGT 229
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVD----LETDNLIQStIRTQFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
....*.
gi 2119195095 230 PEQIFS 235
Cdd:TIGR00957 1503 PSNLLQ 1508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-235 |
4.46e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 27 SIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSREIRAGRKEKNLKGVREKvgivFQFPEHQLFEETvEKD 106
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNNTDMLSPG-EDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 107 imFGPMNLGVTEKEAKTRARAA--INLVGLpEEILEKsPFD-LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKE 183
Cdd:PRK10938 98 --TGRTTAEIIQDEVKDPARCEqlAQQFGI-TALLDR-RFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119195095 184 IMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFS 235
Cdd:PRK10938 174 LAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-219 |
5.36e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQhlnallkptkgsvligsrEIRAGRKEKNLKGVREKvgivfqFPEHQLfee 101
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------EGLYASGKARLISFLPK------FSRNKL--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 102 tvekdIMFGpmnlgvtekeaKTRARAAINLVGLPeeiLEKSPFDLSGGQMRRVAIAGVLAMEPE--VIVLDEPTAGLDPR 179
Cdd:cd03238 63 -----IFID-----------QLQFLIDVGLGYLT---LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2119195095 180 GRKEIMDLFYSLHKKRNlSTVLVTHSmEDAARYADDIVVM 219
Cdd:cd03238 124 DINQLLEVIKGLIDLGN-TVILIEHN-LDVLSSADWIIDF 161
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-224 |
6.54e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 6.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 146 LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
129-209 |
6.69e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 129 INLVGLPEEiLEKSPF-DLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSME 207
Cdd:PRK10938 385 LDILGIDKR-TADAPFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAE 463
|
..
gi 2119195095 208 DA 209
Cdd:PRK10938 464 DA 465
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-242 |
1.01e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 145 DLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLSTVLVTHSMEdAARYADDIVVMHQGEV 224
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLA-VLDYLSDRIHVFEGEP 149
|
90
....*....|....*...
gi 2119195095 225 FTKGTpeqiFSNPKALLE 242
Cdd:cd03222 150 GVYGI----ASQPKGTRE 163
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
146-240 |
1.44e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 49.25 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 146 LSGGQMRRVAIA--------GVLamepevIVLDEPTAGLDPR--GRkeimdLFYSLHKKRNL-STVLVT-HSmEDAARYA 213
Cdd:COG0178 486 LSGGEAQRIRLAtqigsglvGVL------YVLDEPSIGLHQRdnDR-----LIETLKRLRDLgNTVIVVeHD-EDTIRAA 553
|
90 100 110
....*....|....*....|....*....|...
gi 2119195095 214 DDIVVM------HQGEVFTKGTPEQIFSNPKAL 240
Cdd:COG0178 554 DYIIDIgpgageHGGEVVAQGTPEEILKNPDSL 586
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-238 |
1.94e-06 |
|
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: 48.13 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 30 VP-SGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVligsreiragRKEKNLKGVREKvgivFQFPEHQ-LFEETVEKDI 107
Cdd:cd03236 22 VPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF----------DDPPDWDEILDE----FRGSELQnYFTKLLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 108 --MFGPMNLGVTEKEAKTRARAAINLV---GLPEEI---------LEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPT 173
Cdd:cd03236 88 kvIVKPQYVDLIPKAVKGKVGELLKKKderGKLDELvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119195095 174 AGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMEDAARYADDIVVMHqgevftkGTPEQ--IFSNPK 238
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY-------GEPGAygVVTLPK 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-244 |
2.49e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 26 VSIDVPSGTYLAVIGHTGSGKSTvlqhLNALL------KPTKGSVLIGSREIRAGRKEKNlkgVREKVGIVFQFP----- 94
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKST----LSATLagredyEVTGGTVEFKGKDLLELSPEDR---AGEGIFMAFQYPveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 -EHQLFEETVEKDIMfgpmnlGVTEKEAKTR------ARAAINLVGLPEEILEKS-PFDLSGGQMRRVAIAGVLAMEPEV 166
Cdd:PRK09580 93 vSNQFFLQTALNAVR------SYRGQEPLDRfdfqdlMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 167 IVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIV-VMHQGEVFTKGTpeqiFSNPKALLELG 244
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD----FTLVKQLEEQG 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-223 |
3.12e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 22 AISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSvligsreIRAGRKEKNLKGVREK----VGIVFQfpEHQ 97
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS-------ILYLGKEVTFNGPKSSqeagIGIIHQ--ELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 98 LFEE-TVEKDIM--------FGPMNLGVTEKEA-KTRARAAIN-----LVGlpeeilekspfDLSGGQMRRVAIAGVLAM 162
Cdd:PRK10762 90 LIPQlTIAENIFlgrefvnrFGRIDWKKMYAEAdKLLARLNLRfssdkLVG-----------ELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119195095 163 EPEVIVLDEPTAGLDPRgrkEIMDLFYSLH--KKRNLSTVLVTHSMEDAARYADDIVVMHQGE 223
Cdd:PRK10762 159 ESKVIIMDEPTDALTDT---ETESLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
142-207 |
3.23e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.77 E-value: 3.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 142 SPFDLSGGQMRRVAIAGVL---AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKrNLSTVLVTHSME 207
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRN-GAQLILTTHSPL 300
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-181 |
4.09e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 32 SGTYLAVIGHTGSGKSTVLQHLNALLKPT-----------------KGSVL------IGSREIRAGRK-------EKNLK 81
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELqdyfkkLANGEIKVAHKpqyvdliPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 G-VREkvgivfqfpehqLFEETVEKDImfgpmnlgvtekeaktrARAAINLVGLpEEILEKSPFDLSGGQMRRVAIAGVL 160
Cdd:COG1245 178 GtVRE------------LLEKVDERGK-----------------LDELAEKLGL-ENILDRDISELSGGELQRVAIAAAL 227
|
170 180
....*....|....*....|.
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGR 181
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQR 248
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-233 |
7.95e-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: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 132 VGLPEEILEKSPFDLSGGQMRRVAIAGVL---AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMeD 208
Cdd:TIGR00630 816 VGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNL-D 893
|
90 100 110
....*....|....*....|....*....|.
gi 2119195095 209 AARYADDIVVM------HQGEVFTKGTPEQI 233
Cdd:TIGR00630 894 VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-224 |
1.98e-05 |
|
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: 44.56 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLkPTKGSVligSREIRAGRKEKNlkgvrekvGIVFQFPEHQL 98
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT-EGNVSV---EGDIHYNGIPYK--------EFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 99 FeeTVEKDIMFGPMNLGVTEKEAkTRARAAINLVGLpeeilekspfdlSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDP 178
Cdd:cd03233 87 Y--VSEEDVHFPTLTVRETLDFA-LRCKGNEFVRGI------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119195095 179 RGRKEIMDLFYSLHKKRNLSTVL-VTHSMEDAARYADDIVVMHQGEV 224
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-187 |
2.93e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 6 KNVEYRYQADSPfERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLqhlNALLKPTKGSVLIGSREIRAGRKEKnlKGVRE 85
Cdd:TIGR00956 763 RNLTYEVKIKKE-KRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLVNGRPLD--SSFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 86 KVGIVFQFPEHqLFEETVEKDIMFG-----PMNLGVTEK-----------EAKTRARAainLVGLPEEilekspfDLSGG 149
Cdd:TIGR00956 837 SIGYVQQQDLH-LPTSTVRESLRFSaylrqPKSVSKSEKmeyveevikllEMESYADA---VVGVPGE-------GLNVE 905
|
170 180 190
....*....|....*....|....*....|....*....
gi 2119195095 150 QMRRVAIAGVLAMEPEVIV-LDEPTAGLDPRGRKEIMDL 187
Cdd:TIGR00956 906 QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
18-217 |
3.04e-05 |
|
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: 44.14 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 18 FERLAI-------SDVSIDVPSGTYLaVIGHTGSGKSTVLQHLNALLKPTKgsvligSREIRAGRKEKNLKGVREKVGIV 90
Cdd:cd03240 1 IDKLSIrnirsfhERSEIEFFSPLTL-IVGQNGAGKTTIIEALKYALTGEL------PPNSKGGAHDPKLIREGEVRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 91 fqfpeHQLFEETVEKDIMFgpmnlgvtekeakTRARAAI-NLVGLPEE----ILEKSPFDLSGGQ------MRRVAIAGV 159
Cdd:cd03240 74 -----KLAFENANGKKYTI-------------TRSLAILeNVIFCHQGesnwPLLDMRGRCSGGEkvlaslIIRLALAET 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119195095 160 LAMEPEVIVLDEPTAGLDP-RGRKEIMDLFYSLHKKRNLSTVLVTHSmEDAARYADDIV 217
Cdd:cd03240 136 FGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-224 |
3.33e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 37 AVIGHTGSGKSTVLQHLNALLKPTKGSVLIGsreiraGRKEKNLKGVR-EKVGIVFQFPEHQLF-EETVEKDIMFGpmnl 114
Cdd:PRK15439 41 ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG------GNPCARLTPAKaHQLGIYLVPQEPLLFpNLSVKENILFG---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 115 gvTEKEAKTRARAAINLVGLPEEI---LEKSPFDLSGGQMrrVAIAGVLAMEPEVIVLDEPTAGLDPrgrKEIMDLFYSL 191
Cdd:PRK15439 111 --LPKRQASMQKMKQLLAALGCQLdldSSAGSLEVADRQI--VEILRGLMRDSRILILDEPTASLTP---AETERLFSRI 183
|
170 180 190
....*....|....*....|....*....|....*
gi 2119195095 192 HKKRNLST--VLVTHSMEDAARYADDIVVMHQGEV 224
Cdd:PRK15439 184 RELLAQGVgiVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-223 |
3.93e-05 |
|
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: 42.75 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 36 LAVIGHTGSGKSTVLQHLNALLKPTKGSVLIGSreiragrkeknlkgvrekvgivfqfpehqlfeetvekdimfgpmnlg 115
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIYID----------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 116 vtekeakTRARAAINLVGLPEEILEKSPFDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDL-----FYS 190
Cdd:smart00382 38 -------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLL 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 2119195095 191 LHKKRNLSTVLVTHSMED-----AARYADDIVVMHQGE 223
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-204 |
5.73e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 28 IDVPSGTYLaVIGHTGSGKSTVLQHLN-ALLKPTKGSVLIGSREIRAGRKEKNLKGVREKVGIVF-------QFPEHQLF 99
Cdd:COG0419 19 IDFDDGLNL-IVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYrierrqgEFAEFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 100 EETVEKDIMFGPMNLGVTEK----------EAKTRARAAINLVGLPEEILEK-----SPFDLSGGQMRRVAIAGVLAMep 164
Cdd:COG0419 98 KPSERKEALKRLLGLEIYEElkerlkeleeALESALEELAELQKLKQEILAQlsgldPIETLSGGERLRLALADLLSL-- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2119195095 165 eviVLDepTAGLDPRGRKEIMDLFYSLHkkrnlstvLVTH 204
Cdd:COG0419 176 ---ILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-231 |
5.82e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 19 ERLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNA--LLKPTKGSVLIGSREIRAGRKEKnlkgvREKVGI--VFQFP 94
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEE-----RAHLGIflAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 95 -----------------EHQLFEETVEKD-IMFGPMnlgVTEKeaktraraaINLVGLPEEILEKSPFD-LSGGQMRRVA 155
Cdd:CHL00131 94 ieipgvsnadflrlaynSKRKFQGLPELDpLEFLEI---INEK---------LKLVGMDPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 156 IAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlSTVLVTHSMedaaRYADDIV-----VMHQGEVFTKGTP 230
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQ----RLLDYIKpdyvhVMQNGKIIKTGDA 236
|
.
gi 2119195095 231 E 231
Cdd:CHL00131 237 E 237
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
145-177 |
6.62e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 6.62e-05
10 20 30
....*....|....*....|....*....|...
gi 2119195095 145 DLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-230 |
7.09e-05 |
|
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: 43.37 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 25 DVSIDVPSGTYLAVIGHTGSGKSTVLqhlNALLKPTkgsvlIGSREIRAGRKEKNLKGVR-----EKVGIVFQFPE---- 95
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLI---NDTLYPA-----LARRLHLKKEQPGNHDRIEglehiDKVIVIDQSPIgrtp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 96 --------------HQLF----------EETVEkdIMFGPMN----LGVTEKEAKT------RARAAINL---VGLPEEI 138
Cdd:cd03271 85 rsnpatytgvfdeiRELFcevckgkrynRETLE--VRYKGKSiadvLDMTVEEALEffenipKIARKLQTlcdVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 139 LEKSPFDLSGGQMRRVAIAGVLAME---PEVIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNlsTVLVT-HSMeDAARYAD 214
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN--TVVVIeHNL-DVIKCAD 239
|
250 260
....*....|....*....|..
gi 2119195095 215 DIVVM------HQGEVFTKGTP 230
Cdd:cd03271 240 WIIDLgpeggdGGGQVVASGTP 261
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-177 |
7.61e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 20 RLAISDVSIDVPSGTYLAVIGHTGSGKSTVLQH--LNALLK-PTKGSVLIGSREIrAGRKEKNLKGV-----------RE 85
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYmaMHAIDGiPKNCQILHVEQEV-VGDDTTALQCVlntdiertqllEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 86 KVGIVFQFPEHQLFEETVEKDimfGPMNLGVTEKEAKTR-----------------ARAAINLVGLP--EEILEKSPFDL 146
Cdd:PLN03073 269 EAQLVAQQRELEFETETGKGK---GANKDGVDKDAVSQRleeiykrlelidaytaeARAASILAGLSftPEMQVKATKTF 345
|
170 180 190
....*....|....*....|....*....|.
gi 2119195095 147 SGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
146-177 |
4.01e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 4.01e-04
10 20 30
....*....|....*....|....*....|..
gi 2119195095 146 LSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLD 177
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
131-185 |
7.33e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 7.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2119195095 131 LVGLPEEIlekspfDLSGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIM 185
Cdd:PLN03140 1011 IVGLPGVT------GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
6-242 |
1.17e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 6 KNVEYRYqadspferlAISDVSIDVPSGTYLAVIGHTGSGKSTVLQHLNALLKPTKGSVLI-GSRE---IRAGRKEKnLK 81
Cdd:PRK13545 32 KDGEYHY---------ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAAliaISSGLNGQ-LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 82 GVrekvgivfqfpehqlfeETVE-KDIMfgpmnLGVTEKEAKTRARAAINLVGLPEEILEKSPfDLSGGQMRRVAIAGVL 160
Cdd:PRK13545 102 GI-----------------ENIElKGLM-----MGLTKEKIKEIIPEIIEFADIGKFIYQPVK-TYSSGMKSRLGFAISV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 161 AMEPEVIVLDEPTAGLDPRGRKEIMDLFYSLhKKRNLSTVLVTHSMEDAARYADDIVVMHQGEVFTKGTPEQIFSNPKAL 240
Cdd:PRK13545 159 HINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
..
gi 2119195095 241 LE 242
Cdd:PRK13545 238 LK 239
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-229 |
1.60e-03 |
|
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: 38.49 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 146 LSGGQMRRVAIAGVLAMEPE----VIVLDEPTAGLDPRGRKEIMDLFYSLHKKRNLsTVLVTHSMEDAARYAddiVVMHQ 221
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELAELAD---KLIHI 153
|
....*...
gi 2119195095 222 GEVFTKGT 229
Cdd:cd03227 154 KKVITGVY 161
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-61 |
4.13e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 4.13e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2119195095 25 DVSIDvPSGTYLaVIGHTGSGKSTVLQHLNALLKPTK 61
Cdd:pfam13555 16 TIPID-PRGNTL-LTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
147-222 |
4.78e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.55 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119195095 147 SGGQMRRVAIAGVLAMEPEVIVLDEPTAGLDPRGRKEIMDlfySLHKKRNL--STVLVT--HSMEDAARYADDIVVMHQG 222
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIR---ALKTSANIldTTPLVAiyQCSQDAYELFDKVIVLYEG 287
|
|
| |
