|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-502 |
1.63e-77 |
|
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: 259.07 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGR-WAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFVHIVDADGTERPVDGDR 98
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 VTFVGQDPSTQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVM 178
Cdd:COG1123 85 IGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 179 IFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGIAVKGIATSAAPAG 257
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMD-DGRIVEDGPPEEILAAPQALAAVPRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 258 APDASTPGTGAPDRPdleseadavPLLALTGTHV-----ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQ 332
Cdd:COG1123 244 GAARGRAAPAAAAAE---------PLLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 333 MKAGA-NFRIDGASARRVPDAFASWA-------FQNPEHQF-TRATVAAEIDSALagtDPHGPLGADELR-KLREA---- 398
Cdd:COG1123 315 LRPTSgSILFDGKDLTKLSRRSLRELrrrvqmvFQDPYSSLnPRMTVGDIIAEPL---RLHGLLSRAERReRVAELlerv 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 399 -LCPRALDpVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVART 476
Cdd:COG1123 392 gLPPDLAD-RYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGlTYLFISHDLAVVRY 470
|
490 500
....*....|....*....|....*.
gi 1080238652 477 WADRASIVAEGKVAWSGPAADLPASP 502
Cdd:COG1123 471 IADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-244 |
6.63e-44 |
|
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: 158.26 E-value: 6.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDG-- 96
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPT------SGEVLVDGKDITKKNLRElr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 DRVTFVGQDPSTQVLTLRVVDDVSmaleFSLVEAGI----VAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVA 172
Cdd:COG1122 75 RKVGLVFQNPDDQLFAPTVEEDVA----FGPENLGLpreeIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 173 RAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLD-DGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
40-230 |
4.95e-43 |
|
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: 154.93 E-value: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIpshIPIDhaGFVHIVDADGTERPVD--GDRVTFVGQDPSTQVLTLRV 115
Cdd:cd03225 19 DISLTIkkGEFVLIVGPNGSGKSTLLRLLNGLL---GPTS--GEVLVDGKDLTKLSLKelRRKVGLVFQNPDDQFFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:cd03225 94 EEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRREL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1080238652 196 FAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILD 230
Cdd:cd03225 174 LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
289-498 |
6.04e-38 |
|
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: 141.32 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 289 THVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRvpDAFASWA------FQNP 361
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSgEVLVDGKDITK--KNLRELRrkvglvFQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EHQFTRATVAAEIdsALagtdphGP----LGADELRK-LREALcpRALD-----PVSPFVLSGGQKRRLGIFLAVAANRR 431
Cdd:COG1122 85 DDQLFAPTVEEDV--AF------GPenlgLPREEIRErVEEAL--ELVGlehlaDRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
293-488 |
7.61e-35 |
|
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: 131.82 E-value: 7.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFASW----AFQNPEHQFTR 367
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSgEVLVDGKDLTKLSLKELRRkvglVFQNPDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAEIDSAL--AGTDPhgplgADELRKLREALCPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHL 442
Cdd:cd03225 91 PTVEEEVAFGLenLGLPE-----EEIEERVEEALELVGLEGLrdrSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 443 DSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGK 488
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
40-235 |
8.65e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 131.61 E-value: 8.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVhIVDADGTERPVDGDRVTFVGQDPSTQVLTlrvvD 117
Cdd:cd03226 18 DLSLDLyaGEIIALTGKNGAGKTTLAKILAGLIKES-----SGSI-LLNGKPIKAKERRKSIGYVMQDVDYQLFT----D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 118 DVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFA 197
Cdd:cd03226 88 SVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080238652 198 AIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDADGSV 235
Cdd:cd03226 168 LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
293-489 |
2.02e-33 |
|
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: 127.37 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDG---ASARRVPDAFasWAFQNPEHQFTRA 368
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKESSGSILLNGkpiKAKERRKSIG--YVMQDVDYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAAEidsaLAGTDPHGPLGADELRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSR 448
Cdd:cd03226 88 SVREE----LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 449 IVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
294-498 |
2.97e-32 |
|
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: 125.36 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARR-----------VPDAFASWAFQNP 361
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSgSILIDGEDVRKeprearrqigvLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 E---------HQFTRATVAAEIDSALAGTDphgpLGADELRKLREalcpraldpvspfvLSGGQKRRLGIFLAVAANRRL 432
Cdd:COG4555 92 ReniryfaelYGLFDEELKKRIEELIELLG----LEEFLDRRVGE--------------LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHD-RRVARTwADRASIVAEGKVAWSGPAADL 498
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEAL-CDRVVILHKGKVVAQGSLDEL 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
294-498 |
4.51e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.79 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--------AGANFRIDGASARR----VPDAFASWAFQNP 361
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsgevrvLGEDVARDPAEVRRrigyVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 E---------HQFTRATVAAEIDSALAGTDphgpLGADELRKLREalcpraldpvspfvLSGGQKRRLGIFLAVAANRRL 432
Cdd:COG1131 91 RenlrffarlYGLPRKEARERIDELLELFG----LTDAADRKVGT--------------LSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
283-498 |
7.87e-32 |
|
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: 124.39 E-value: 7.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGAS---------ARRVpda 352
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSgEVLLDGRDlaslsrrelARRI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 faSWAFQNPEHQFtRATVAaeiDSALAGTDPH----GPLGADELRKLREALcpRALDpVSPFV------LSGGQKRRLGI 422
Cdd:COG1120 78 --AYVPQEPPAPF-GLTVR---ELVALGRYPHlglfGRPSAEDREAVEEAL--ERTG-LEHLAdrpvdeLSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 423 FLAVAANRRLLLLDEPLAHLDsPSSRI-VLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLD-LAHQLeVLELLRRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
282-470 |
8.18e-32 |
|
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: 122.97 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFAS---WA 357
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAgEVLWNGEPIRDAREDYRRrlaYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNPEhQFTRATVAAEID--SALAGTDPHGPLGADELRKLreALCPRALDPVSpfVLSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:COG4133 81 GHADG-LKPELTVRENLRfwAALYGLRADREAIDEALEAV--GLAGLADLPVR--QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHD 470
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
294-489 |
2.60e-31 |
|
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: 120.20 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFA---SWAFQNPEhQFTRAT 369
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSgEIKVLGKDIKKEPEEVKrriGYLPEEPS-LYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VaaeidsalagtdphgplgadelrklREALcpraldpvspfVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRI 449
Cdd:cd03230 90 V-------------------------RENL-----------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 450 VLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
282-497 |
5.05e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGaNFRIDGASARR-------VPDA 352
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPptSG-TVRLFGKPPRRarrrigyVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 FAS-WAFqnPehqftrATVAaeiDSALAGTDPH----GPLGADELRKLREALcpRALD-------PVSpfVLSGGQKRRl 420
Cdd:COG1121 84 AEVdWDF--P------ITVR---DVVLMGRYGRrglfRRPSRADREAVDEAL--ERVGledladrPIG--ELSGGQQQR- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 421 gIFLA--VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWsGPAAD 497
Cdd:COG1121 148 -VLLAraLAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-242 |
1.05e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 15 TAPARLRVSGAGVRHaDGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIvdaDGTERPV 94
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-----PTSGTVRL---FGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 DGDRVTFVGQ----DPSTQVltlRVVDDVSMALefsLVEAGIVAKQSA-------EALSELGLSELAEKDPWALSGGQRQ 163
Cdd:COG1121 73 ARRRIGYVPQraevDWDFPI---TVRDVVLMGR---YGRRGLFRRPSRadreavdEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 164 RMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdaDGSVAAHGAPE 242
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL--NRGLVAHGPPE 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
282-526 |
2.27e-30 |
|
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: 126.17 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVA--RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANF----RIDGASARRVPDAF-- 353
Cdd:COG1123 3 PLLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevLLDGRDLLELSEALrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 --ASWAFQNPEHQFTRATVAAEIDSAL-AGTDPHGPLGADELRKLREALCPRALDpVSPFVLSGGQKRRLGIFLAVAANR 430
Cdd:COG1123 83 rrIGMVFQDPMTQLNPVTVGDQIAEALeNLGLSRAEARARVLELLEAVGLERRLD-RYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 431 RLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSRRDR 509
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVP 241
|
250
....*....|....*..
gi 1080238652 510 PLPAAGARTSLDESPGT 526
Cdd:COG1123 242 RLGAARGRAAPAAAAAE 258
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
35-216 |
2.07e-29 |
|
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: 116.46 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDGDRVTFVGQDPStqvL-- 111
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPD------SGEILIDGRDVTGVPPERRNIGMVFQDYA---Lfp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:cd03259 86 HLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180
....*....|....*....|....*.
gi 1080238652 192 RRSLFAAIRDL-RAPGRVILLIEHDL 216
Cdd:cd03259 166 REELREELKELqRELGITTIYVTHDQ 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-239 |
2.68e-29 |
|
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: 116.09 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDGTERPVDGDRVTFVGQdpSTQVLT---LRV 115
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-----SGSIRV---FGKPLEKERKRIGYVPQ--RRSIDRdfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDDVSMALEFSLVEAGIVAKQSA----EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:cd03235 88 RDVVLMGLYGHKGLFRRLSKADKakvdEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1080238652 192 RRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDADgsVAAHG 239
Cdd:cd03235 168 QEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT--VVASG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-491 |
8.92e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 121.33 E-value: 8.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDFG----------TIN-----AITGPVGCGKTSLAHLIAGLIpshipidhagfvhivDADGTERPVDGD-RVTFVG 103
Cdd:COG0488 3 NLSKSFGgrpllddvslSINpgdriGLVGRNGAGKSTLLKILAGEL---------------EPDSGEVSIPKGlRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 104 QDPST--------QVLT--------LRVVDDVSMALEFSLVEAGIVAK---------------QSAEALSELGLSELAEK 152
Cdd:COG0488 68 QEPPLdddltvldTVLDgdaelralEAELEELEAKLAEPDEDLERLAElqeefealggweaeaRAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 153 DPWA-LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPgrvILLIEHD---------------- 215
Cdd:COG0488 148 RPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGT---VLVVSHDryfldrvatrileldr 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 216 --LRPFDG----WVDTVTILDADGSVAAHGAPEGIA--------VKGIATSAAPA------------GAPDASTpgtgap 269
Cdd:COG0488 225 gkLTLYPGnysaYLEQRAERLEQEAAAYAKQQKKIAkeeefirrFRAKARKAKQAqsrikaleklerEEPPRRD------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 270 DRPDLESEADAV---PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKAGANF 339
Cdd:COG0488 299 KTVEIRFPPPERlgkKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLagelepdSGTVKLGETV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 340 RIdgasarrvpdA-FAswafQNPEHQFTRATVAAEIDSALAGTDPHgplgadELRKLREALC---PRALDPVSpfVLSGG 415
Cdd:COG0488 379 KI----------GyFD----QHQEELDPDKTVLDELRDGAPGGTEQ------EVRGYLGRFLfsgDDAFKPVG--VLSGG 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 416 QKRRL---GIFLAvAANrrLLLLDEPLAHLDSPSSRIVLDALAEYAgagGTVVFTCHDRRVARTWADRASIVAEGKVAW 491
Cdd:COG0488 437 EKARLalaKLLLS-PPN--VLLLDEPTNHLDIETLEALEEALDDFP---GTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-253 |
2.94e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 28 RHADGRWAPDMVDLSFDFGTINAITGPVGCGKTS-LAHLIAGLIPSHIPIDHAGfvhIVDADGTERPVDGdRVTFVGQDP 106
Cdd:PRK13647 13 RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTlLLHLNGIYLPQRGRVKVMG---REVNAENEKWVRS-KVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 107 STQVLTLRVVDDVSmaleFSLVEAGI----VAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDE 182
Cdd:PRK13647 89 DDQVFSSTVWDDVA----FGPVNMGLdkdeVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 183 PAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGIAVKGIATSA 253
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLK-EGRVLAEGDKSLLTDEDIVEQA 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
286-488 |
1.62e-26 |
|
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: 106.18 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 286 LTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGAsarrvpdafaswafqnpehq 364
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGK-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 ftratvaaeidsalagtdphgPLGADELRKLRE--ALCPRaldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHL 442
Cdd:cd00267 62 ---------------------DIAKLPLEELRRriGYVPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 443 DSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGK 488
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
39-216 |
2.02e-26 |
|
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: 107.94 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIvdaDGTERPVDGDRVTFVGQDPStqVLT-LRVV 116
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPT------SGEVLV---DGEPVTGPGPDRGYVFQQDA--LLPwLTVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLF 196
Cdd:cd03293 92 DNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQ 171
|
170 180
....*....|....*....|.
gi 1080238652 197 AAIRDL-RAPGRVILLIEHDL 216
Cdd:cd03293 172 EELLDIwRETGKTVLLVTHDI 192
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
282-498 |
2.69e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 108.22 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTG-THVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA------NFRIDGASARRVPDAFA 354
Cdd:COG3638 1 PMLELRNlSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSgeilvdGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 SWA--FQNPeHQFTRATVaaeIDSALAGTDPH--------GPLGADELRKLREALC-----PRALDPVSPfvLSGGQKRR 419
Cdd:COG3638 81 RIGmiFQQF-NLVPRLSV---LTNVLAGRLGRtstwrsllGLFPPEDRERALEALErvglaDKAYQRADQ--LSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 420 LGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGiTVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
291-491 |
3.65e-26 |
|
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: 106.85 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 291 VARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVPDAFAsWAFQNPEHQFT-RA 368
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKPLEKERKRIG-YVPQRRSIDRDfPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAaeiDSALAGTDPH----GPLGADELRKLREAL--------CPRALDPvspfvLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:cd03235 86 SVR---DVVLMGLYGHkglfRRLSKADKAKVDEALervglselADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 437 EPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAW 491
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
39-244 |
6.51e-26 |
|
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: 107.92 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDAD-GTERPVDGD----RVTFVGQDPSTQVLT 112
Cdd:TIGR04521 24 VSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkPT------SGTVTIDGRDiTAKKKKKLKdlrkKVGLVFQFPEHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRVVDDVS---MALEFSLVEAGIVAKqsaEALSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:TIGR04521 98 ETVYKDIAfgpKNLGLSEEEAEERVK---EALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 189 EDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:TIGR04521 175 PKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMH-KGKIVLDGTPREV 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
284-503 |
9.66e-26 |
|
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: 106.37 E-value: 9.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA---NFR---IDGASARRVPDAFASWA 357
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSgsvLFDgedITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNPEhQFTRATVAAEIDSALAGTDPHGPLGADELRKLREA------------LCPRALDPVSpfVLSGGQKRRLGIFLA 425
Cdd:cd03219 81 FQIPR-LFPELTVLENVMVAAQARTGSGLLLARARREEREAreraeellervgLADLADRPAG--ELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
290-497 |
1.34e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.74 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGAsarrvpdAFASWAFQN-------- 360
Cdd:COG4559 8 SVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSgEVRLNGR-------PLAAWSPWElarrravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 361 PEHQ-----FTratvAAEIdsALAGTDPHGPLGADELRKLREALcpRALDpVSPFV------LSGGQKRR--LGIFLA-- 425
Cdd:COG4559 81 PQHSslafpFT----VEEV--VALGRAPHGSSAAQDRQIVREAL--ALVG-LAHLAgrsyqtLSGGEQQRvqLARVLAql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 426 ---VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAAD 497
Cdd:COG4559 152 wepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-244 |
1.65e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.02 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDGDR--VTFVGQDPSTQV 110
Cdd:PRK13635 20 TYALKDVSFSVyeGEWVAIVGHNGSGKSTLAKLLNGLLLPE-----AGTITVGGMVLSEETVWDVRrqVGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:PRK13635 95 VGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 191 GRRSLFAAIRDLRAPGRV-ILLIEHDLRPfDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK13635 175 GRREVLETVRQLKEQKGItVLSITHDLDE-AAQADRVIVMN-KGEILEEGTPEEI 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
36-244 |
2.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 36 PDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIpshIPIDHAGFVHIVDadGTERPVDG-----DRVTFVGQDPST 108
Cdd:PRK13640 21 PALNDISFSIprGSWTALIGHNGSGKSTISKLINGLL---LPDDNPNSKITVD--GITLTAKTvwdirEKVGIVFQNPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:PRK13640 96 QFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 189 EDGRRSLFAAIRDLRAP-GRVILLIEHDLRPFDGwVDTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLD-DGKLLAQGSPVEI 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
40-244 |
4.63e-25 |
|
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: 104.55 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshipIDHaGFVHIVDADGTERPVDGDR-VTFVGQD-PSTQVLTLRv 115
Cdd:COG4555 19 DVSFTAkdGEITGLLGPNGAGKTTLLRMLAGLLK----PDS-GSILIDGEDVRKEPREARRqIGVLPDErGLYDRLTVR- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 vDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKdPWA-LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:COG4555 93 -ENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDR-RVGeLSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 195 LFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:COG4555 171 LREILRALKKEGKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQGSLDEL 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-244 |
5.92e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 38 MVDLSFDF--GTINAITGPVGCGKTSL-AHLIAGLIPSHIPIDHAGFvHIVDADGTERPVD-GDRVTFVGQDPSTQVLTL 113
Cdd:PRK13641 23 LDNISFELeeGSFVALVGHTGSGKSTLmQHFNALLKPSSGTITIAGY-HITPETGNKNLKKlRKKVSLVFQFPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDDVSMA---LEFSLVEAGIVAKQsaeALSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDE 189
Cdd:PRK13641 102 TVLKDVEFGpknFGFSEDEAKEKALK---WLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 190 DGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLE-HGKLIKHASPKEI 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
39-217 |
7.93e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.58 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIvdaDGTE------------RpvdGDRVTFVGQD 105
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDrPT------SGEVLI---DGQDisslserelarlR---RRHIGFVFQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 106 PstQVL-TLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPA 184
Cdd:COG1136 95 F--NLLpELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPT 172
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 185 AHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:COG1136 173 GNLDSKTGEEVLELLRELnRELGTTIVMVTHDPE 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
290-493 |
1.07e-24 |
|
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: 101.74 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGAS-ARRVPDAFASWafqnpehqftR 367
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSgEILLDGKDlASLSPKELARK----------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAEIDSalagtdphgpLGADEL--RKLREalcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP 445
Cdd:cd03214 76 AYVPQALEL----------LGLAHLadRPFNE--------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 446 SSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03214 132 HQIELLELLRRLARERGkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
284-498 |
1.72e-24 |
|
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: 102.51 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVP-DAFASW--AFQ 359
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGRDITGLPpHERARAgiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 nPEHQ--FTRATVAAEID-SALAGTDPHGPLGADELRKLREALCPRALDPVSpfVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:cd03224 81 -PEGRriFPELTVEENLLlGAYARRRAKRKARLERVYELFPRLKERRKQLAG--TLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 437 EPLAHLdSPS-SRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:cd03224 158 EPSEGL-APKiVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
39-217 |
4.06e-24 |
|
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: 101.03 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIvdaDGTE--RPVDGDR-------VTFVGQDPst 108
Cdd:cd03255 23 VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDrPT------SGEVRV---DGTDisKLSEKELaafrrrhIGFVFQSF-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVL-TLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:cd03255 92 NLLpDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180 190
....*....|....*....|....*....|.
gi 1080238652 188 DEDGRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:cd03255 172 DSETGKEVMELLRELnKEAGTTIVVVTHDPE 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
293-480 |
5.10e-24 |
|
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: 101.04 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDG-------ASARRVPDAFASWAFQNPEHQ 364
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGkdllklsRRLRKIRRKEIQMVFQDPMSS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 FT-RATVAAEIDSALAgtdPHGPLGADELRKLREALCPRALDPVS------PFVLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:cd03257 95 LNpRMTIGEQIAEPLR---IHGKLSKKEARKEAVLLLLVGVGLPEevlnryPHELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080238652 438 PLAHLDSPSSRIVLDALAE-YAGAGGTVVFTCHDRRVARTWADR 480
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIADR 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
284-480 |
5.72e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.28 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGANF----RIDGASA----RRVpdaf 353
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADldPPTSGEIYldgkPLSAMPPpewrRQV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 aSWAFQNPehQFTRATVAAEIdsALAGTDPHGPLGADELRKLREALC--PRALD-PVSPfvLSGGQKRRLGIFLAVAANR 430
Cdd:COG4619 77 -AYVPQEP--ALWGGTVRDNL--PFPFQLRERKFDRERALELLERLGlpPDILDkPVER--LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 431 RLLLLDEPLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADR 480
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADR 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
15-217 |
6.36e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 101.70 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 15 TAPARLRVSGAGVRHA---DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIvdaDGT 90
Cdd:COG1116 3 AAAPALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPT------SGEVLV---DGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 91 ERPVDGDRVTFVGQDPStqvLT--LRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIA 168
Cdd:COG1116 74 PVTGPGPDRGVVFQEPA---LLpwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 169 GAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVD 200
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
40-244 |
7.14e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.91 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDG-DRVTFVGQDPSTQvLTLRV 115
Cdd:COG1131 18 GVSLTVepGEIFGLLGPNGAGKTTTIRMLLGLLrPT------SGEVRVLGEDVARDPAEVrRRIGYVPQEPALY-PDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 196 FAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:COG1131 171 WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIID-KGRIVADGTPDEL 218
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
20-269 |
9.21e-24 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 101.43 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVrHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGfvhiVDADGTERPVDGDR 98
Cdd:TIGR03873 2 LRLSRVSW-SAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALrPDAGTVDLAG----VDLHGLSRRARARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 VTFVGQDPSTQVlTLRVVDDVSM---------ALEfSLVEAGIVAkqsaEALSELGLSELAEKDPWALSGGQRQRMAIAG 169
Cdd:TIGR03873 77 VALVEQDSDTAV-PLTVRDVVALgriphrslwAGD-SPHDAAVVD----RALARTELSHLADRDMSTLSGGERQRVHVAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 170 AVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPEGIAVKGI 249
Cdd:TIGR03873 151 ALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDG-GRVVAAGPPREVLTPAL 229
|
250 260
....*....|....*....|
gi 1080238652 250 ATSAAPAGAPDASTPGTGAP 269
Cdd:TIGR03873 230 IRAVYGVDATVLTHPDTGRP 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-244 |
1.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.74 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLipsHIPIDhaGFVHIVDADGTERPVDGD------RVTFVGQDPSTQVLT 112
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL---HVPTQ--GSVRVDDTLITSTSKNKDikqirkKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRVVDDVSmaleFSLVEAGiVAKQSAEALSE-----LGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAH 186
Cdd:PRK13649 101 ETVLKDVA----FGPQNFG-VSQEEAEALAReklalVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 187 VDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPEGI 244
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEK-GKLVLSGKPKDI 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
282-503 |
1.54e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 100.50 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GAnfRIDGASARRVPDAF 353
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPtsgrilfdGR--DITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 ASWAFQNPeHQFTRATVA--------AEIDSALAGTDPHGPLGADELRKLREA---------LCPRALDPVSpfVLSGGQ 416
Cdd:COG0411 81 IARTFQNP-RLFPELTVLenvlvaahARLGRGLLAALLRLPRARREEREARERaeellervgLADRADEPAG--NLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 417 KRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPA 495
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 1080238652 496 ADLPASPE 503
Cdd:COG0411 238 AEVRADPR 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
39-245 |
1.69e-23 |
|
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: 99.82 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVD-----GDRVTFvgQDPST-QVL 111
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPT------SGSVLFDGEDITGLPPHeiarlGIGRTF--QIPRLfPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TlrVVDDVSMALEFSLVEAGIVAK----------QSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFD 181
Cdd:cd03219 91 T--VLENVMVAAQARTGSGLLLARarreereareRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 182 EPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPEGIA 245
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ-GRVIAEGTPDEVR 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
286-503 |
1.79e-23 |
|
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: 99.88 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 286 LTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDG------------ASARRVPDA 352
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSgEVLIDGedisglseaelyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 FASWAFqnpehqFTRATVAAEIdsALagtdP---HGPLGADELRKL-REALCPRALDPVS---PFVLSGGQKRRLGIFLA 425
Cdd:cd03261 83 FQSGAL------FDSLTVFENV--AF----PlreHTRLSEEEIREIvLEKLEAVGLRGAEdlyPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGA-GGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-242 |
2.80e-23 |
|
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: 99.73 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 19 RLRVSGAGVRHaDGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDGteRPVDG-- 96
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLL---DG--RDLASls 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 -----DRVTFVGQDPSTqVLTLRVVDDVSMAL--------EFSLVEAGIVAkqsaEALSELGLSELAEKDPWALSGGQRQ 163
Cdd:COG1120 70 rrelaRRIAYVPQEPPA-PFGLTVRELVALGRyphlglfgRPSAEDREAVE----EALERTGLEHLADRPVDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 164 RMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDL----RpfdgWVDTVTILDaDGSVAAH 238
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLnlaaR----YADRLVLLK-DGRIVAQ 219
|
....
gi 1080238652 239 GAPE 242
Cdd:COG1120 220 GPPE 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-242 |
4.20e-23 |
|
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: 104.07 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 15 TAPARLRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPV 94
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 D--GDRVTFVGQDPSTQVLTLRvvDDVSMAlefslvEAGIVAKQSAEALSELGLSELAEKDP-----------WALSGGQ 161
Cdd:COG4988 407 AswRRQIAWVPQNPYLFAGTIR--ENLRLG------RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 162 RQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLrAPGRVILLIEHDLRPFDgWVDTVTILDaDGSVAAHGAP 241
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA-QADRILVLD-DGRIVEQGTH 555
|
.
gi 1080238652 242 E 242
Cdd:COG4988 556 E 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
294-492 |
4.43e-23 |
|
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: 96.34 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGasaRRVpdafaswAFQNPEHQFTR--ATV 370
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSgEILVDG---KEV-------SFASPRDARRAgiAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 aaeidsalagtdphgplgadelrklrealcpraldpvspFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIV 450
Cdd:cd03216 81 ---------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1080238652 451 LDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWS 492
Cdd:cd03216 122 FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
294-498 |
7.73e-23 |
|
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: 98.02 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANFRIDGASARRVPDAFASWAFQnpEHQF 365
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtsgsvlidGTDINKLKGKALRQLRRQIGMIFQ--QFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 T-RATVAAEIDSALAGTDPH-----GPLGADELRKLREAL-----CPRALDPVSPfvLSGGQKRRLGIFLAVAANRRLLL 434
Cdd:cd03256 90 IeRLSVLENVLSGRLGRRSTwrslfGLFPKEEKQRALAALervglLDKAYQRADQ--LSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 435 LDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREEGiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-498 |
1.14e-22 |
|
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: 98.68 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGAnFRIDGASA------------RRVpdafaSWAFQNPEHQ 364
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKptSGT-VTIDGRDItakkkkklkdlrKKV-----GLVFQFPEHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 FTRATVAAEIdsALagtdphGP--LGADE---LRKLREALCPRALDP----VSPFVLSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:TIGR04521 95 LFEETVYKDI--AF------GPknLGLSEeeaEERVKEALELVGLDEeyleRSPFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 436 DEPLAHLDsPSSRI-VLDALAEYAGAGG-TVVFTCHD-RRVARtWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR04521 167 DEPTAGLD-PKGRKeILDLFKRLHKEKGlTVILVTHSmEDVAE-YADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
284-493 |
1.48e-22 |
|
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: 96.43 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVP--DAFASWAFQN 360
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVPpeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 361 PEhQFTRATVAAEIDSALagtDPHGPLGADELRKLREALCPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:cd03259 81 YA-LFPHLTVAENIAFGL---KLRGVPKAEIRARVRELLELVGLEGLlnrYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 438 PLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
299-440 |
1.58e-22 |
|
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: 94.25 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGAnFRIDGASARRVPDAFA----SWAFQNPeHQFTRATVAA 372
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSptEGT-ILLDGQDLTDDERKSLrkeiGYVFQDP-QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 373 EIDSALAGTDPHGPLGADELRKLREAL-----CPRALDpVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKLglgdlADRPVG-ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
284-493 |
1.71e-22 |
|
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: 96.11 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGeIHALVGANGAGKSTLLAVLSG--QMKAGAnFRIDGASARRVPDAFASWAFQNP 361
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATltPPSSGT-IRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EhQFT---RATVAAEID-SALAGTDPHGPLGADELRKLREA-LCPRALDPVSPfvLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:cd03264 79 Q-EFGvypNFTVREFLDyIAWLKGIPSKEVKARVDEVLELVnLGDRAKKKIGS--LSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 437 EPLAHLDsPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03264 156 EPTAGLD-PEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
36-216 |
1.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 36 PDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIpshipidhagfvhivDADGTERPVDGDRVT------------F 101
Cdd:PRK13650 21 YTLNDVSFHVkqGEWLSIIGHNGSGKSTTVRLIDGLL---------------EAESGQIIIDGDLLTeenvwdirhkigM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 102 VGQDPSTQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFD 181
Cdd:PRK13650 86 VFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1080238652 182 EPAAHVDEDGRRSLFAAIRDLRAP-GRVILLIEHDL 216
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
292-504 |
2.09e-22 |
|
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: 97.18 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 292 ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGaNFRIDGASARRVPD-AFA---SWAFQNPEHQF 365
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwSG-EVTFDGRPVTRRRRkAFRrrvQMVFQDPYASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 T-RATVAAEIDSALAGtdpHG-PLGADELRKLREA--LCPRALDPVsPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAH 441
Cdd:COG1124 93 HpRHTVDRILAEPLRI---HGlPDREERIAELLEQvgLPPSFLDRY-PHQLSGGQRQRVAIARALILEPELLLLDEPTSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 442 LDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:COG1124 169 LDVSVQAEILNLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-230 |
2.99e-22 |
|
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: 93.85 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 21 RVSGAGVRHADGRwAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDG--DR 98
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEElrRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 VTFVGQdpstqvltlrvvddvsmalefslveagivakqsaealselglselaekdpwaLSGGQRQRMAIAGAVARAPEVM 178
Cdd:cd00267 75 IGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 179 IFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILD 230
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-244 |
3.26e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLA-HLIAGLIPShipidhAGFVHIVDADGTERPVDGD---RVTFVGQDPSTQV 110
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAkHMNALLIPS------EGKVYVDGLDTSDEENLWDirnKAGMVFQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:PRK13633 99 VATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 191 GRRSLFAAIRDL-RAPGRVILLIEHDLrpfDGWV--DTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK13633 179 GRREVVNTIKELnKKYGITIILITHYM---EEAVeaDRIIVMD-SGKVVMEGTPKEI 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
268-501 |
4.84e-22 |
|
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: 100.99 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 268 APDRPDLESEADAVPLLALTGTHVARGGER-ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGAS 345
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSgSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 346 ARRVPDAF----ASWAFQNPehQFTRATVAAEIdsALAGTDphgplgADElRKLREALcpRALDpVSPFV---------- 411
Cdd:COG4988 401 LSDLDPASwrrqIAWVPQNP--YLFAGTIRENL--RLGRPD------ASD-EELEAAL--EAAG-LDEFVaalpdgldtp 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 412 -------LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAgAGGTVVFTCHDRRVARtWADRASIV 484
Cdd:COG4988 467 lgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLA-QADRILVL 544
|
250
....*....|....*..
gi 1080238652 485 AEGKVAWSGPAADLPAS 501
Cdd:COG4988 545 DDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-244 |
5.06e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 28 RHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSL-AHLIAGLIPShipidhAGFVHIvdaDGteRPVDGDR-------- 98
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILKPT------SGEVLI---KG--EPIKYDKksllevrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 -VTFVGQDPSTQVLTLRVVDDVS---MALEFSLVEagiVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARA 174
Cdd:PRK13639 79 tVGIVFQNPDDQLFAPTVEEDVAfgpLNLGLSKEE---VEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 175 PEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGI 244
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM-SDGKIIKEGTPKEV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-504 |
6.06e-22 |
|
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: 100.53 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVS---GAGVRHA-DGrwapdmVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHiPIDHAGFVHIvdaDGTE---- 91
Cdd:COG4172 12 LSVAfgqGGGTVEAvKG------VSFDIAAGETLALVGESGSGKSVTALSILRLLPDP-AAHPSGSILF---DGQDllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 92 -----RPVDGDRVTFVGQDPSTQ---VLTlrVVDDVSMALEFSLVEAGIVAKQSA-EALSELGLSELAEKD---PWALSG 159
Cdd:COG4172 82 serelRRIRGNRIAMIFQEPMTSlnpLHT--IGKQIAEVLRLHRGLSGAAARARAlELLERVGIPDPERRLdayPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 160 GQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAP-GRVILLIEHDLrpfdGWV----DTVTILDaDGS 234
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDL----GVVrrfaDRVAVMR-QGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 235 VAAHGAPEGIAvkgiatsAAPAgAP------DAStpgtgaPDRPDLESEADAVPLLALTGTHVA-----------RGGER 297
Cdd:COG4172 235 IVEQGPTAELF-------AAPQ-HPytrkllAAE------PRGDPRPVPPDAPPLLEARDLKVWfpikrglfrrtVGHVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTL-LAVL-----SGQMK-AGAnfRIDGASARRVP-----------DAFASWafq 359
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLgLALLrlipsEGEIRfDGQ--DLDGLSRRALRplrrrmqvvfqDPFGSL--- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 NPehqftRATVAAEIDSALAGtdpHGP-LGADELRKL-REALCPRALDPVS----PFVLSGGQKRRLGIFLAVAANRRLL 433
Cdd:COG4172 376 SP-----RMTVGQIIAEGLRV---HGPgLSAAERRARvAEALEEVGLDPAArhryPHEFSGGQRQRIAIARALILEPKLL 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 434 LLDEPLAHLDSPSSRIVLDAL----AEYagaGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLrdlqREH---GLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-239 |
7.22e-22 |
|
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: 94.88 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVD-LSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshiPIDhaGFV-----HIVDADGTE 91
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDdVSFSIkkGETLGLVGESGSGKSTLARAILGLLK---PTS--GSIifdgkDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 92 RPVDGDRVTFVGQDPSTqVL--TLRVVDdvsmALEFSLVEAGIVAKQSA------EALSELGLSE-LAEKDPWALSGGQR 162
Cdd:cd03257 77 RKIRRKEIQMVFQDPMS-SLnpRMTIGE----QIAEPLRIHGKLSKKEArkeavlLLLVGVGLPEeVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 163 QRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRA-PGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHG 239
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYA-GKIVEEG 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
39-262 |
7.57e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFVHIVDADGTE-RPVDgDRVTFVGQDPSTQVLTLRVV 116
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEiKPVR-KKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEFSLVEAGIVAKQSAEALSELGLS-ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 196 FAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGIAVKGIATSAAPAGAPDAS 262
Cdd:PRK13643 184 MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLE-KGHIISCGTPSDVFQEVDFLKAHELGVPKAT 249
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-216 |
7.69e-22 |
|
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: 93.27 E-value: 7.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 21 RVSGAGVRHaDGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipidhagfvhivdadgterPVDGdRVT 100
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK---------------------PSSG-EIL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 101 FVGQDPSTqvLTLRvvddvSMALEFSLVeagivakqsAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIF 180
Cdd:cd03214 58 LDGKDLAS--LSPK-----ELARKIAYV---------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 1080238652 181 DEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDL 216
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDL 158
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
40-185 |
8.43e-22 |
|
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: 92.33 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshiPIdhAGFVHI--VDADGTERPVDGDRVTFVGQDPsTQVLTLRV 115
Cdd:pfam00005 3 NVSLTLnpGEILALVGPNGAGKSTLLKLIAGLLS---PT--EGTILLdgQDLTDDERKSLRKEIGYVFQDP-QLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 116 VDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAE----KDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-244 |
8.70e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 8.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGL-IPS--HI-----PIDHAGFVHIVDADGterpvdgdrvtFVGQDPSTQ 109
Cdd:PRK13648 27 DVSFNIpkGQWTSIVGHNGSGKSTIAKLMIGIeKVKsgEIfynnqAITDDNFEKLRKHIG-----------IVFQNPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 110 VLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDE 189
Cdd:PRK13648 96 FVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 190 DGRRSLFAAIRDLRAPGRV-ILLIEHDLRPFDGwVDTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNItIISITHDLSEAME-ADHVIVMN-KGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
34-241 |
1.13e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 34 WAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSH---IPI------DHAGFVHIVDADGTERPVDGDR----VT 100
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtIQVgdiyigDKKNNHELITNPYSKKIKNFKElrrrVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 101 FVGQDPSTQVLTLRVVDDVS---MALEFSLVEAgivAKQSAEALSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPE 176
Cdd:PRK13631 120 MVFQFPEYQLFKDTIEKDIMfgpVALGVKKSEA---KKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAP 241
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD-KGKILKTGTP 260
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
284-494 |
1.41e-21 |
|
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: 94.17 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGA-----SARRVPDAFASW-- 356
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEvlldgKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 -----AFQNPeHQFtRATVAAEIDSALAgtdPHGPLGADELRKLRE------ALCPRALDPVSPFVLSGGQKRRLGIFLA 425
Cdd:cd03260 81 rrvgmVFQKP-NPF-PGSIYDNVAYGLR---LHGIKLKEELDERVEealrkaALWDEVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAgGTVVFTCHDRRVARTWADRASIVAEGKVAWSGP 494
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
282-502 |
1.70e-21 |
|
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: 94.28 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANfrIDGASARRVPDAF 353
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdsgeilvdGQD--ITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 ASWA--FQNpehqftratvAAEIDS-------ALagtdP---HGPLGADELRKL-REALC----PRALD--PVSpfvLSG 414
Cdd:COG1127 82 RRIGmlFQG----------GALFDSltvfenvAF----PlreHTDLSEAEIRELvLEKLElvglPGAADkmPSE---LSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 415 GQKRRLGIFLAVAANRRLLLLDEPLAHLDsPSSRIVLDAL-----AEYagaGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLD-PITSAVIDELirelrDEL---GLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
250
....*....|...
gi 1080238652 490 AWSGPAADLPASP 502
Cdd:COG1127 221 IAEGTPEELLASD 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
293-493 |
2.21e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGasaRRVPDAFASW-------AFQNPEHQ 364
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMG---REVNAENEKWvrskvglVFQDPDDQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 FTRATVaaEIDSALagtdphGP----LGADEL-RKLREALcpRALD-----PVSPFVLSGGQKRRLGIFLAVAANRRLLL 434
Cdd:PRK13647 92 VFSSTV--WDDVAF------GPvnmgLDKDEVeRRVEEAL--KAVRmwdfrDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 435 LDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
294-488 |
3.10e-21 |
|
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: 91.29 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGaNFRIDGASARRVPDAF----ASWAFQNPeHQFtr 367
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDptSG-EILIDGVDLRDLDLESlrknIAYVPQDP-FLF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 atvaaeidsalAGTdphgplgadelrkLREALcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSS 447
Cdd:cd03228 89 -----------SGT-------------IRENI------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 448 RIVLDALAEYAGaGGTVVFTCHDRRVARTwADRASIVAEGK 488
Cdd:cd03228 133 ALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
139-443 |
4.31e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 97.96 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 139 EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLrAPGRVILLIEHDLrp 218
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 219 fdgwvdtvTILD--ADGSVAAHGAPegiAVKGIATSaaPAGA--------------------PDASTPGTGAPdrpdlES 276
Cdd:PRK13409 272 --------AVLDylADNVHIAYGEP---GAYGVVSK--PKGVrvgineylkgylpeenmrirPEPIEFEERPP-----RD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 277 EADAVPLLALTGTHVArggeriLDGADLTLERGEIHA-----LVGANGAGKSTLLAVLSGQMK--AGANF---------- 339
Cdd:PRK13409 334 ESERETLVEYPDLTKK------LGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKpdEGEVDpelkisykpq 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 340 RIDGASARRVPDAFASwafqnpehqftratVAAEIDSALAGTDPHGPLGADEL--RKLREalcpraldpvspfvLSGGQK 417
Cdd:PRK13409 408 YIKPDYDGTVEDLLRS--------------ITDDLGSSYYKSEIIKPLQLERLldKNVKD--------------LSGGEL 459
|
330 340
....*....|....*....|....*.
gi 1080238652 418 RRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
293-488 |
6.15e-21 |
|
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: 90.71 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGAS----ARRVPDAFASWA--FQNPEhQF 365
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGSILIDGEDltdlEDELPPLRRRIGmvFQDFA-LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TRATVaaeidsalagtdphgplgadelrklrealcpraLDPVSpFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP 445
Cdd:cd03229 89 PHLTV---------------------------------LENIA-LGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080238652 446 SSRIVLDALAE-YAGAGGTVVFTCHDRRVARTWADRASIVAEGK 488
Cdd:cd03229 135 TRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
302-498 |
6.71e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.13 E-value: 6.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 302 ADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVPDAF--ASWAFQnpEHQ-FTRATVAAEIdsA 377
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTALPPAErpVSMLFQ--ENNlFPHLTVAQNI--G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 378 LaGTDPHGPLGADELRKLREalcprALDPVS--------PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDsPSSR- 448
Cdd:COG3840 94 L-GLRPGLKLTAEQRAQVEQ-----ALERVGlaglldrlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PALRq 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 449 ---IVLDALAEYAGAggTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG3840 167 emlDLVDELCRERGL--TVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-221 |
6.98e-21 |
|
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: 91.39 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 18 ARLRVSGAGVRHaDGRWAPDmvDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIVDADGTERPVD 95
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFS--GLSFTLaaGEALALTGPNGSGKTTLLRILAGLLP-----PSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 96 -GDRVTFVGQDPST-QVLTLRvvDDVSMALEFSLVEAGivAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVAR 173
Cdd:COG4133 73 yRRRLAYLGHADGLkPELTVR--ENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1080238652 174 APEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDG 221
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-218 |
8.27e-21 |
|
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: 90.35 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRwAPDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PSH--IPIDHAgfvhivDADGTERPV 94
Cdd:cd03246 1 LEVENVSFRYPGAE-PPVLRNVSFSIepGESLAIIGPSGSGKSTLARLILGLLrPTSgrVRLDGA------DISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 DGDRVTFVGQDpsTQVLTLRVVDDVsmalefslveagivakqsaealselglselaekdpwaLSGGQRQRMAIAGAVARA 174
Cdd:cd03246 74 LGDHVGYLPQD--DELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080238652 175 PEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHdlRP 218
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAH--RP 156
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
282-503 |
8.48e-21 |
|
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: 91.97 E-value: 8.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANfrIDGASARRVPDAF 353
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrsgsirfdGED--ITGLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 ASWAfqnPEHQ--FTRATVAAEIDSALAGTDPHGPLGAD---------ELRKLREAlcpRALDpvspfvLSGGQKRRLGI 422
Cdd:COG0410 80 IGYV---PEGRriFPSLTVEENLLLGAYARRDRAEVRADlervyelfpRLKERRRQ---RAGT------LSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 423 FLAVAANRRLLLLDEPLAHLdSPSsrIV---LDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLP 499
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGL-APL--IVeeiFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....
gi 1080238652 500 ASPE 503
Cdd:COG0410 225 ADPE 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
298-489 |
8.63e-21 |
|
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: 91.40 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGASARRVPDAF--------ASWAFQNPe 362
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrptSGEV------RVDGTDISKLSEKElaafrrrhIGFVFQSF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 HQFTRATVaaeIDSALAGTDPHGPLGADELRKLREALcpRALDPV-----SPFVLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:cd03255 92 NLLPDLTA---LENVELPLLLAGVPKKERRERAEELL--ERVGLGdrlnhYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 438 PLAHLDSPSSRIVLDALAEYA-GAGGTVVFTCHDRRVARTwADRASIVAEGKV 489
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
289-498 |
1.00e-20 |
|
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: 91.41 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 289 THVARGGERI-LDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRIDGASARRVPDAfaswAFQN----P 361
Cdd:cd03263 7 TKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPTSG-TAYINGYSIRTDRKA----ARQSlgycP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EH--QFTRATVAA--EIDSALAGTdPHGPLGADELRKLRE-ALCPRALDPVSpfVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:cd03263 82 QFdaLFDELTVREhlRFYARLKGL-PKSEIKEEVELLLRVlGLTDKANKRAR--TLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 437 EPLAHLDSPSSRIVLDALAEYAGaGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
282-497 |
1.02e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDG---------ASARR--- 348
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSgEVRLNGrpladwspaELARRrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 349 VPDAFA-SWAFQNPE--------HQFTRATVAAEIDSALAGTDphgplgadeLRKLREALCPRaldpvspfvLSGGQKRR 419
Cdd:PRK13548 81 LPQHSSlSFPFTVEEvvamgrapHGLSRAEDDALVAAALAQVD---------LAHLAGRDYPQ---------LSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 420 --LGIFLA----VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAG-AGGTVVFTCHDRRVARTWADRASIVAEGKVAWS 492
Cdd:PRK13548 143 vqLARVLAqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
....*
gi 1080238652 493 GPAAD 497
Cdd:PRK13548 223 GTPAE 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
139-495 |
1.26e-20 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 96.78 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 139 EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLrp 218
Cdd:COG1245 195 ELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 219 fdgwvdtvTILD--ADGSVAAHGAPegiAVKGIATSAAPAGA------------------PDA----STPGTGAPDRPDL 274
Cdd:COG1245 273 --------AILDylADYVHILYGEP---GVYGVVSKPKSVRVginqyldgylpeenvrirDEPiefeVHAPRREKEEETL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 275 eSEADAVpllaltgthvarggERILDGADLTLERGEIH-----ALVGANGAGKSTLLAVLSGQMKAganfriDGASARrv 349
Cdd:COG1245 342 -VEYPDL--------------TKSYGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKP------DEGEVD-- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 350 PDAFASWAFQNPEH-------QFTRATVAAEIDSALAGTDPHGPLGADEL--RKLREalcpraldpvspfvLSGGQKRRL 420
Cdd:COG1245 399 EDLKISYKPQYISPdydgtveEFLRSANTDDFGSSYYKTEIIKPLGLEKLldKNVKD--------------LSGGELQRV 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 421 GIFLAVAANRRLLLLDEPLAHLDSpSSRI----VLDALAEYAGAGGTVVFtcHDRRVARTWADRAsIVAEGKVAWSGPA 495
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDV-EQRLavakAIRRFAENRGKTAMVVD--HDIYLIDYISDRL-MVFEGEPGVHGHA 539
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-248 |
1.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGK-TSLAHLIAGLIPSHipidhaGFVHI---VDADGTE----RPVDgDRVTFVGQDPSTQV 110
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKsTLLQHLNGLLQPTS------GTVTIgerVITAGKKnkklKPLR-KKVGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVVDDVSMA-LEFSLVEAGivAKQSA-EALSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:PRK13634 99 FEETVEKDICFGpMNFGVSEED--AKQKArEMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 188 DEDGRRSL---FAAIRdlRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPEGIAVKG 248
Cdd:PRK13634 177 DPKGRKEMmemFYKLH--KEKGLTTVLVTHSMEDAARYADQIVVMHK-GTVFLQGTPREIFADP 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-242 |
1.98e-20 |
|
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: 95.99 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 9 AGATRGTAPARLRVSGAGVRHAD-GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvda 87
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITL--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 88 DGTE-RPVDGD----RVTFVGQDP---STQVL-TLRVVD-DVSMAlefslveagivakQSAEALSELGLSELAEKDP--- 154
Cdd:COG4987 395 GGVDlRDLDEDdlrrRIAVVPQRPhlfDTTLReNLRLARpDATDE-------------ELWAALERVGLGDWLAALPdgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 155 --W------ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLrAPGRVILLIEHDLRPFDgWVDTV 226
Cdd:COG4987 462 dtWlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLE-RMDRI 539
|
250
....*....|....*.
gi 1080238652 227 TILDaDGSVAAHGAPE 242
Cdd:COG4987 540 LVLE-DGRIVEQGTHE 554
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-245 |
2.04e-20 |
|
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: 91.40 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMV-DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIvdaDGTERPVDG 96
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLkDVSLEVapGESFGLVGESGSGKSTLLRALAGLER-----PWSGEVTF---DGRPVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 DR-----VTFVGQDPSTQV---LTL-RVVDDVSMALEFSLVEAGIvakqsAEALSELGL-SELAEKDPWALSGGQRQRMA 166
Cdd:COG1124 74 RKafrrrVQMVFQDPYASLhprHTVdRILAEPLRIHGLPDREERI-----AELLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 167 IAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGIA 245
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQ-NGRIVEELTVADLL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
265-480 |
2.22e-20 |
|
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: 95.43 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 265 GTGAPDRPDLESEADAVPLLALTG-THVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN-FRID 342
Cdd:TIGR02857 303 AAPRPLAGKAPVTAAPASSLEFSGvSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGsIAVN 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 343 GASARRVPDAF----ASWAFQNPehQFTRATVAAEIDSALAGTDPHGPLGADELRKLREAL--CPRALDPV---SPFVLS 413
Cdd:TIGR02857 383 GVPLADADADSwrdqIAWVPQHP--FLFAGTIAENIRLARPDASDAEIREALERAGLDEFVaaLPQGLDTPigeGGAGLS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 414 GGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGaGGTVVFTCHDRRVARtWADR 480
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAA-LADR 525
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
284-495 |
2.47e-20 |
|
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: 89.51 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK---AGANFRIDGAS---------ARRvpD 351
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGEDitdlppeerARL--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 352 AFAswAFQNPehqftratvaAEIdsalagtdpHGPLGADELRKLREAlcpraldpvspfvLSGGQKRRLGIFLAVAANRR 431
Cdd:cd03217 79 IFL--AFQYP----------PEI---------PGVKNADFLRYVNEG-------------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTW-ADRASIVAEGKVAWSGPA 495
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
39-232 |
2.77e-20 |
|
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: 88.59 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPS---HIPIDHagfVHIVDADGTERPvdgDRVTFVGQDPstqVL---T 112
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtsgEILIDG---VDLRDLDLESLR---KNIAYVPQDP---FLfsgT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRvvddvsmalefslveagivakqsaEALselglselaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGR 192
Cdd:cd03228 92 IR------------------------ENI---------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 193 RSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:cd03228 133 ALILEALRALAK-GKTVIVIAHRLS---------TIRDAD 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-216 |
4.17e-20 |
|
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: 94.66 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 3 GGAPACAGATRGTAPAR-LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGF 81
Cdd:TIGR02857 304 APRPLAGKAPVTAAPASsLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 82 VHIVDADGTERPVDG--DRVTFVGQDPstqvltlrVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAE-------- 151
Cdd:TIGR02857 379 IAVNGVPLADADADSwrDQIAWVPQHP--------FLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAalpqgldt 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 152 ---KDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLrAPGRVILLIEHDL 216
Cdd:TIGR02857 451 pigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL 517
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-244 |
5.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDAD-GTERPVDGDR 98
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-----KGKVLVSGIDtGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 --VTFVGQDPSTQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPE 176
Cdd:PRK13644 77 klVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGwVDTVTILDAdGSVAAHGAPEGI 244
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDR-GKIVLEGEPENV 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
294-480 |
5.75e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 86.73 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKaganfridgasarrvPDAfaswafqnpehqftratvaae 373
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE---------------PDE--------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 idsalaGTDPHGPlgadelrKLREALCPRaldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDA 453
Cdd:cd03221 55 ------GIVTWGS-------TVKIGYFEQ---------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180
....*....|....*....|....*..
gi 1080238652 454 LAEYAgagGTVVFTCHDRRVARTWADR 480
Cdd:cd03221 113 LKEYP---GTVILVSHDRYFLDQVATK 136
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
40-244 |
6.78e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.44 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDGTErpVDGDRVT----FVG---QDPSTQV 110
Cdd:PRK13632 27 NVSFEIneGEYVAILGHNGSGKSTISKILTGLLKPQ-----SGEIKI---DGIT--ISKENLKeirkKIGiifQNPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:PRK13632 97 IGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 191 GRRSLFAAIRDLRAPG-RVILLIEHDLrpfdgwvDTVTILD-----ADGSVAAHGAPEGI 244
Cdd:PRK13632 177 GKREIKKIMVDLRKTRkKTLISITHDM-------DEAILADkvivfSEGKLIAQGKPKEI 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
282-489 |
6.79e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.33 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTG-THVARGGE---RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFAS- 355
Cdd:COG1136 3 PLLELRNlTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSgEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 -------WAFQNPeHQFTRATVA--AEIDSALAGTDphgplgadelRKLREALCPRALDPV--------SPFVLSGGQKR 418
Cdd:COG1136 83 lrrrhigFVFQFF-NLLPELTALenVALPLLLAGVS----------RKERRERARELLERVglgdrldhRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 419 RLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARtWADRASIVAEGKV 489
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGtTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
39-215 |
7.59e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 88.72 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDGDR--VTFVGQDPstQVLTLRVV 116
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMPPPEWRrqVAYVPQEP--ALWGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDvsMALEFSLVEAGIVAKQSAEALSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:COG4619 92 DN--LPFPFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180
....*....|....*....|.
gi 1080238652 196 FAAIRDLRA-PGRVILLIEHD 215
Cdd:COG4619 170 EELLREYLAeEGRAVLWVSHD 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
286-469 |
8.76e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 286 LTGTHVA--RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGaSARRVPDAFASWAFQNPE 362
Cdd:PRK13539 3 LEGEDLAcvRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGlLPPAAGTIKLDG-GDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 HQFTRA-TVAAEID--SALAGTDPHGPLgadelrklrEALCPRALDPVS--PF-VLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:PRK13539 82 NAMKPAlTVAENLEfwAAFLGGEELDIA---------AALEAVGLAPLAhlPFgYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 1080238652 437 EPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCH 469
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
294-498 |
1.23e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVP-DAFA---SWAFQNPeHQFTRA 368
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSgEVLVDGLDVATTPsRELAkrlAILRQEN-HINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAaeiDSALAGTDPH--GPLGADELRKLREA-----LCP---RALDPvspfvLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:COG4604 91 TVR---ELVAFGRFPYskGRLTAEDREIIDEAiayldLEDladRYLDE-----LSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 439 LAHLDSPSSRIVLDALAEYA-GAGGTVVFTCHDRRVARTWADRasIVA--EGKVAWSGPAADL 498
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADH--IVAmkDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
35-241 |
1.86e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.34 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDGD----RVTFVGQDPSTQ 109
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT------SGKIIIDGVDITDKKVKLSdirkKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 110 VLTLRVVDDVsmalEFSLVEAGI----VAKQSAEALSELGLS--ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:PRK13637 96 LFEETIEKDI----AFGPINLGLseeeIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 184 AAHVDEDGRRSLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAP 241
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMN-KGKCELQGTP 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-215 |
2.16e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 18 ARLRVSGAGVRHADGRWAP---DMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PS--HIPIDHagfvHIVDADGTE 91
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQpalQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLaPSsgEITLDG----VPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 92 RPVdgdrvtfVGQD----PstqvlTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAI 167
Cdd:COG4525 78 RGV-------VFQKdallP-----WLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 168 AGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHD 215
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
39-202 |
2.43e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.13 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVdGDR-VTFVGQDPstqVL--TLR 114
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEdPT------SGEILIGGRDVTDLPP-KDRnIAMVFQSY---ALypHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:COG3839 92 VYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVE 171
|
....*...
gi 1080238652 195 LFAAIRDL 202
Cdd:COG3839 172 MRAEIKRL 179
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-241 |
2.91e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADgrwAPDMVDLSFDFGTiNAITGPVG---CGKTSLAHLIAGLIPshiPIDHAGFVHIVDADGTERPVDG 96
Cdd:PRK13638 2 LATSDLWFRYQD---EPVLKGLNLDFSL-SPVTGLVGangCGKSTLFMNLSGLLR---PQKGAVLWQGKPLDYSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 DR--VTFVGQDPSTQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARA 174
Cdd:PRK13638 75 LRqqVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 175 PEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAP 241
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVL-RQGQILTHGAP 220
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
39-217 |
3.72e-19 |
|
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: 87.02 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgtERPVDGDrVTFVGQD----PSTQVLTLR 114
Cdd:TIGR02211 24 VSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL---------------------DNPTSGE-VLFNGQSlsklSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 ------------------VVDDVSMAL---EFSLVEAgivAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVAR 173
Cdd:TIGR02211 82 nkklgfiyqfhhllpdftALENVAMPLligKKSVKEA---KERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1080238652 174 APEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLE 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
40-235 |
3.97e-19 |
|
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: 85.53 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVD-GDRVTFVGQDPST-QVLTLR 114
Cdd:cd03230 18 DISLTVekGEIYGLLGPNGAGKTTLIKIILGLLkPD------SGEIKVLGKDIKKEPEEvKRRIGYLPEEPSLyENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 vvddvsmalefslveagivakqsaEALSelglselaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:cd03230 92 ------------------------ENLK--------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 195 LFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSV 235
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILEEAERLCDRVAILN-NGRI 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-216 |
4.13e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHAdGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFVhiVDADGTERPVdgdr 98
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVpYQHGSITLDGKP--VEGPGAERGV---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 vtfVGQDPStqVLTLR-VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEV 177
Cdd:PRK11248 75 ---VFQNEG--LLPWRnVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDL 216
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDI 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-216 |
4.75e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPShipidhagfvhivdADGTERPVDGDRVTFVGQDPS-TQ 109
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP--------------TSGTVRRAGGARVAYVPQRSEvPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 110 VLTLRVVDDVSMALefsLVEAGIVAKQSAE-------ALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDE 182
Cdd:NF040873 69 SLPLTVRDLVAMGR---WARRGLWRRLTRDdraavddALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 183 PAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
35-202 |
4.93e-19 |
|
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: 87.01 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipiDHA--GFVHIVDADGTERPVDGDRVTFVGQDPST-QVL 111
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-------ERPdsGTILFGGEDATDVPVQERNVGFVFQHYALfRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TlrVVDDVSMALEFSLVEAGIVAKQSAEALSEL----GLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:cd03296 90 T--VFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170
....*....|....*
gi 1080238652 188 DEDGRRSLFAAIRDL 202
Cdd:cd03296 168 DAKVRKELRRWLRRL 182
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
298-498 |
5.61e-19 |
|
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: 91.82 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRV-PDAFASW------------------- 356
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSgRILIDGIDLRQIdPASLRRQigvvlqdvflfsgtireni 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 AFQNPEHQFTRATVAAEidsaLAGTDphgplgaDELRKLrealcPRALD-PVSPF--VLSGGQKRRLGIFLAVAANRRLL 433
Cdd:COG2274 570 TLGDPDATDEEIIEAAR----LAGLH-------DFIEAL-----PMGYDtVVGEGgsNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 434 LLDEPLAHLDSPSSRIVLDALAEYAgAGGTVVFTCHDRRVARtWADRASIVAEGKVAWSGPAADL 498
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEEL 696
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
50-244 |
8.31e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSL-AHLIAGLIPShipidhAGFVHIVDADGTERPVDGDR--VTFVGQDPSTQVLTLRVVDDVSMA-LEF 125
Cdd:PRK13652 34 AVIGPNGAGKSTLfRHFNGILKPT------SGSVLIRGEPITKENIREVRkfVGLVFQNPDDQIFSPTVEQDIAFGpINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 126 SLVEAgIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RA 204
Cdd:PRK13652 108 GLDEE-TVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpET 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 205 PGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMD-KGRIVAYGTVEEI 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
298-489 |
1.06e-18 |
|
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: 84.19 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRV-PDAFaswafqnpehqftRATVA--AE 373
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVRLDGADISQWdPNEL-------------GDHVGylPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 IDSALAGTdphgplgadelrkLREAlcpraldpvspfVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDA 453
Cdd:cd03246 84 DDELFSGS-------------IAEN------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 1080238652 454 LAEYAGAGGTVVFTCHDRRVARTwADRASIVAEGKV 489
Cdd:cd03246 139 IAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
282-498 |
1.23e-18 |
|
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: 86.29 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM--KAGANFRIDGasaRR-----VPD--- 351
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRLFG---ERrggedVWElrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 352 --AFASWAFQnpeHQFTRATVAAE-IDSALAGT-DPHGPLGADELRKLREALcpRALDpVS-----PF-VLSGGQKRRLG 421
Cdd:COG1119 79 riGLVSPALQ---LRFPRDETVLDvVLSGFFDSiGLYREPTDEQRERARELL--ELLG-LAhladrPFgTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 422 IFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-438 |
1.26e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 16 APARLRVSG-----AGVRhadgrwAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIvdaDGT 90
Cdd:COG1129 1 AEPLLEMRGisksfGGVK------ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ-----PDSGEILL---DGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 91 ERPVDGDR------VTFVGQDPStQVLTLRVVDDVSMALEfsLVEAGIV-----AKQSAEALSELGLSElaekDPWA--- 156
Cdd:COG1129 67 PVRFRSPRdaqaagIAIIHQELN-LVPNLSVAENIFLGRE--PRRGGLIdwramRRRARELLARLGLDI----DPDTpvg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 -LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPfdgwV----DTVTILdA 231
Cdd:COG1129 140 dLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDE----VfeiaDRVTVL-R 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 232 DGSVAAHGAPEGIAVKGIATsaapagapdASTPGTGAPDRPDLESEADAVpllALTGTHVARGGEriLDGADLTLERGEI 311
Cdd:COG1129 215 DGRLVGTGPVAELTEDELVR---------LMVGRELEDLFPKRAAAPGEV---VLEVEGLSVGGV--VRDVSFSVRAGEI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 312 HALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASAR-RVPDAfaswAFQN-----PE---HQ--FTRATVAAEIdsALA 379
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPAdSGEIRLDGKPVRiRSPRD----AIRAgiayvPEdrkGEglVLDLSIRENI--TLA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 380 GTDPHGPLG-------ADELRKLREAL---CPRALDPVSpfVLSGG--QKrrlgIFLA--VAANRRLLLLDEP 438
Cdd:COG1129 355 SLDRLSRGGlldrrreRALAEEYIKRLrikTPSPEQPVG--NLSGGnqQK----VVLAkwLATDPKVLILDEP 421
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
295-506 |
1.48e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANFRIDGASARRVPDAfASWAFQNPEHQFT 366
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPtsgevlikGEPIKYDKKSLLEVRKT-VGIVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVaaEIDSALagtdphGP----LGADEL-RKLREALCPRAL---DPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:PRK13639 93 APTV--EEDVAF------GPlnlgLSKEEVeKRVKEALKAVGMegfENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 439 LAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSR 506
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
268-488 |
1.51e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 268 APDRPDLESEADAVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGAnFRIDGAS 345
Cdd:PRK11607 4 AIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeQPTAGQ-IMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 346 ARRVPD-------AFASWAFqnpehqFTRATVAAEIDSALAgtdpHGPLGADELR-KLREALCPRALDPVS---PFVLSG 414
Cdd:PRK11607 83 LSHVPPyqrpinmMFQSYAL------FPHMTVEQNIAFGLK----QDKLPKAEIAsRVNEMLGLVHMQEFAkrkPHQLSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 415 GQKRRLGIFLAVAANRRLLLLDEPLAHLDSP-SSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGK 488
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
258-507 |
1.63e-18 |
|
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: 89.83 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 258 APDASTPGTGAPdrpdleseADAVPLLALTGTHVARGGER--ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA 335
Cdd:COG4987 316 PPAVTEPAEPAP--------APGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 336 GA-NFRIDGASARRVPD----AFASWAFQNPeHQFTrATVAAEIdsALAgtDPhgplGADElRKLREALCPRALDPvspF 410
Cdd:COG4987 388 QSgSITLGGVDLRDLDEddlrRRIAVVPQRP-HLFD-TTLRENL--RLA--RP----DATD-EELWAALERVGLGD---W 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 411 V-----------------LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEyAGAGGTVVFTCHdRRV 473
Cdd:COG4987 454 LaalpdgldtwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITH-RLA 531
|
250 260 270
....*....|....*....|....*....|....
gi 1080238652 474 ARTWADRASIVAEGKVAWSGPAADLPASPESSRR 507
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
32-245 |
1.72e-18 |
|
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: 85.29 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHipidhaGFVHIVDADGTERPVDGDR---VTFVGQDPS 107
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDS------GKILLDGQDITKLPMHKRArlgIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 108 tqVL-TLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAH 186
Cdd:cd03218 86 --IFrKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 187 VDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGIA 245
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYII-YEGKVLAEGTPEEIA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
299-503 |
1.93e-18 |
|
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: 84.94 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVPDAFASWA-------FQNpEHQFTRATV 370
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPTSGSVLVDGTDLTLLSGKELRKArrrigmiFQH-FNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIdsALagtdphgPLgadELRKLREALCPRALDPVSPFV------------LSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:cd03258 100 FENV--AL-------PL---EIAGVPKAEIEERVLELLELVgledkadaypaqLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 439 LAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:cd03258 168 TSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-216 |
3.56e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.95 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgtERPVDGdRV 99
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE---------------------ERPTSG-QV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 TFVGQD----PSTQVLTLR-----------------VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALS 158
Cdd:COG2884 60 LVNGQDlsrlKRREIPYLRrrigvvfqdfrllpdrtVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 159 GGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
294-480 |
3.56e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASAR--------RVPDAF----------AS 355
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqrsEVPDSLpltvrdlvamGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 WAFQNPEHQFTRATVAAeIDSALAGtdphgpLGADELRKlrealcpRALDPvspfvLSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:NF040873 83 WARRGLWRRLTRDDRAA-VDDALER------VGLADLAG-------RQLGE-----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTwADR 480
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
48-245 |
4.75e-18 |
|
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: 86.32 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 48 INAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFVHIVDADGTERPVDGDRVTFVGQDpSTQVLTLRVVDDVSMALEFS 126
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE-ARLFPHLSVRGNLRYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 127 LVEAGIVAKQSAEALseLGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPG 206
Cdd:TIGR02142 104 RPSERRISFERVIEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 207 RV-ILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGIA 245
Cdd:TIGR02142 182 GIpILYVSHSLQEVLRLADRVVVLE-DGRVAAAGPIAEVW 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
39-285 |
5.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPShipidhagFVHIVDADGTERPVDG-----DRVTFVGQDPSTQVLTL 113
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--------FEGKVKIDGELLTAENvwnlrRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 194 SLFAAIRDLRAPGRV-ILLIEHDLRPFDGwVDTVTILDAdGSVAAHGAP-------EGIAVKGIATSAAPAGAPDASTPG 265
Cdd:PRK13642 178 EIMRVIHEIKEKYQLtVLSITHDLDEAAS-SDRILVMKA-GEIIKEAAPselfatsEDMVEIGLDVPFSSNLMKDLRKNG 255
|
250 260
....*....|....*....|
gi 1080238652 266 TGAPDRpdLESEADAVPLLA 285
Cdd:PRK13642 256 FDLPEK--YLSEDELVELLA 273
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-215 |
5.33e-18 |
|
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: 83.83 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDGDRVTFVGQD---- 105
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFEtPT------SGEILLDGKDITNLPPHKRPVNTVFQNyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 106 PStqvltLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:cd03300 85 PH-----LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190
....*....|....*....|....*....|.
gi 1080238652 186 HVDEDGRRSLFAAIRDL-RAPGRVILLIEHD 215
Cdd:cd03300 160 ALDLKLRKDMQLELKRLqKELGITFVFVTHD 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-202 |
6.79e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 16 APARLRVSGAGVRHADGRwAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshiPidHAGFVHIVDADGTERPVD 95
Cdd:COG3842 2 AMPALELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET---P--DSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 96 GDRVTFVGQD----PStqvltLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAV 171
Cdd:COG3842 76 KRNVGMVFQDyalfPH-----LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190
....*....|....*....|....*....|.
gi 1080238652 172 ARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL 202
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRL 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
286-477 |
7.25e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 286 LTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAganfriDGASARRVPDafASWAF--QNPEh 363
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP------DSGEVSIPKG--LRIGYlpQEPP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 QFTRATVA-----------------AEIDSALAGTDPHGP-----------LGADEL-RKLREAL----CPRA-LD-PVS 408
Cdd:COG0488 72 LDDDLTVLdtvldgdaelraleaelEELEAKLAEPDEDLErlaelqeefeaLGGWEAeARAEEILsglgFPEEdLDrPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 409 pfVLSGGQKRRLGifLAVA--ANRRLLLLDEPLAHLDspssrivLDA---LAEY-AGAGGTVVFTCHDR----RVA-RTW 477
Cdd:COG0488 152 --ELSGGWRRRVA--LARAllSEPDLLLLDEPTNHLD-------LESiewLEEFlKNYPGTVLVVSHDRyfldRVAtRIL 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
27-242 |
8.29e-18 |
|
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: 82.80 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 27 VRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIP-----SHIpidhAGFVHIVDADGTERpvdgdRVTF 101
Cdd:cd03265 7 VKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgrATV----AGHDVVREPREVRR-----RIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 102 VGQDPStqvltlrvVDDVSMALEFSLVEAGI-------VAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARA 174
Cdd:cd03265 78 VFQDLS--------VDDELTGWENLYIHARLygvpgaeRRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 175 PEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPE 242
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIID-HGRIIAEGTPE 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-239 |
8.43e-18 |
|
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: 82.63 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHaDGRWAPDMVDLSFDFGtINAITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIVDADGTERPVDG-DR 98
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTP-----PSSGTIRIDGQDVLKQPQKLrRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 VTFVGQDPSTQVlTLRVVDdvsmALEFSLVEAGIVAKQS----AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARA 174
Cdd:cd03264 74 IGYLPQEFGVYP-NFTVRE----FLDYIAWLKGIPSKEVkarvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 175 PEVMIFDEPAAHVDEDGR---RSLFAAIrdlrAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHG 239
Cdd:cd03264 149 PSILIVDEPTAGLDPEERirfRNLLSEL----GEDRIVILSTHIVEDVESLCNQVAVLN-KGKLVFEG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
282-526 |
1.05e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDG-----ASARRVPDAFAS 355
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAgTVLVAGddveaLSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 wafqNPEHqftrATVAAEIDSALA---GTDPH----GPLGADELRKLREALcprALDPVSPFV------LSGGQKRRLGI 422
Cdd:PRK09536 82 ----VPQD----TSLSFEFDVRQVvemGRTPHrsrfDTWTETDRAAVERAM---ERTGVAQFAdrpvtsLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 423 FLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
250 260
....*....|....*....|....
gi 1080238652 503 esSRRDrplpAAGARTSLDESPGT 526
Cdd:PRK09536 231 --TLRA----AFDARTAVGTDPAT 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
294-505 |
1.10e-17 |
|
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: 83.06 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDG-------ASARRVPDAFASWAFqnpehqF 365
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEILLDGkditnlpPHKRPVNTVFQNYAL------F 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TRATVAAEIDSALagtdphgplgadELRKLREAL----CPRALDPV--------SPFVLSGGQKRRLGIFLAVAANRRLL 433
Cdd:cd03300 85 PHLTVFENIAFGL------------RLKKLPKAEikerVAEALDLVqlegyanrKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 434 LLDEPLAHLDS---PSSRIVLDALAEYAGAggTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESS 505
Cdd:cd03300 153 LLDEPLGALDLklrKDMQLELKRLQKELGI--TFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
284-498 |
1.18e-17 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 83.33 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--------AGANFRIDGASARRVPDAFAS 355
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvdlAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 WAFQNPEHQFTRATVA---AEIDSALAGTDPHGPLGADEL--RKLREALCPRALDpvspfVLSGGQKRRLGIFLAVAANR 430
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVAlgrIPHRSLWAGDSPHDAAVVDRAlaRTELSHLADRDMS-----TLSGGERQRVHVARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 431 RLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREV 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
292-470 |
1.41e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.22 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 292 ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRvPDAFASWAFQNPehqftR--- 367
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSgEVLVDGKPVTG-PGPDRGVVFQEP-----Allp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 -ATVAAEIdsALagtdphGPLGADELRKLREALCPRALDPVS--------PFVLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:COG1116 94 wLTVLDNV--AL------GLELRGVPKAERRERARELLELVGlagfedayPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 439 LAHLDSPsSRIVL-DALAEYAGAGG-TVVFTCHD 470
Cdd:COG1116 166 FGALDAL-TRERLqDELLRLWQETGkTVLFVTHD 198
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
294-493 |
1.60e-17 |
|
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: 81.88 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVPDAfaswafqnpehqftRATVAA 372
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQKNIEA--------------LRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSalAGTDPHgpLGADE-------LRKLREALCPRALD----------PVSPFVLsgGQKRRLGIFLAVAANRRLLLL 435
Cdd:cd03268 77 LIEA--PGFYPN--LTAREnlrllarLLGIRKKRIDEVLDvvglkdsakkKVKGFSL--GMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
37-502 |
1.64e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 37 DMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFV-----HIVDAD-GTERPVDGDRVTFVGQDPST-- 108
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIrfhgeSLLHASeQTLRGVRGNKIAMIFQEPMVsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 -----------QVLTLRVvddvSMALEFSLVEA-------GIvaKQSAEALSELglselaekdPWALSGGQRQRMAIAGA 170
Cdd:PRK15134 106 nplhtlekqlyEVLSLHR----GMRREAARGEIlncldrvGI--RQAAKRLTDY---------PHQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 171 VARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDadgsvaahgapEGIAVKGI 249
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQ-----------NGRCVEQN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 250 ATSA---APAGAPD----ASTPgTGAPdrpdLESEADAVPLLALTGTHVA---RGG--------ERILDGADLTLERGEI 311
Cdd:PRK15134 240 RAATlfsAPTHPYTqkllNSEP-SGDP----VPLPEPASPLLDVEQLQVAfpiRKGilkrtvdhNVVVKNISFTLRPGET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 312 HALVGANGAGKST----LLAVLSGQ--------------MKAGANFRidgasaRRVpdafaSWAFQNPEHQFT-RATVAA 372
Cdd:PRK15134 315 LGLVGESGSGKSTtglaLLRLINSQgeiwfdgqplhnlnRRQLLPVR------HRI-----QVVFQDPNSSLNpRLNVLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSALAGTDPHGPLGADELRkLREALCPRALDPVS----PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSR 448
Cdd:PRK15134 384 IIEEGLRVHQPTLSAAQREQQ-VIAVMEEVGLDPETrhryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 449 IVLDAL----AEYAGAggtVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:PRK15134 463 QILALLkslqQKHQLA---YLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
35-231 |
1.73e-17 |
|
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: 80.69 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIP---SHIPIDHAGfvhiVDADGTERPVDGDRVTFVGQDPSTqVL 111
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpdsGSILIDGED----LTDLEDELPPLRRRIGMVFQDFAL-FP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TLRVVDDVSMALefslveagivakqsaealselglselaekdpwalSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:cd03229 90 HLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 192 RRSLFAAIRDLRA-PGRVILLIEHDLRPFDGWVDTVTILDA 231
Cdd:cd03229 136 RREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-215 |
1.77e-17 |
|
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: 81.92 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipIDhAGFVHIVDADGTERPVDGDRVTFVGQD----P 106
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE----PT-SGRIYIGGRDVTDLPPKDRDIAMVFQNyalyP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 107 StqvltLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAH 186
Cdd:cd03301 86 H-----MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190
....*....|....*....|....*....|
gi 1080238652 187 VDEDGRRSLFAAIRDL-RAPGRVILLIEHD 215
Cdd:cd03301 161 LDAKLRVQMRAELKRLqQRLGTTTIYVTHD 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
284-495 |
3.58e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG----QMKAGaNFRIDGAS---------ARR-- 348
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyEVTSG-SILLDGEDilelspderARAgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 349 -VpdafaswAFQNPE-------HQFTRATVAAEIDSALAGTDPHGPLG--ADELrKLREALCPRALDpVSpfvLSGGQKR 418
Cdd:COG0396 80 fL-------AFQYPVeipgvsvSNFLRTALNARRGEELSAREFLKLLKekMKEL-GLDEDFLDRYVN-EG---FSGGEKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 419 RLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVAR-TWADRASIVAEGKVAWSGPA 495
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDyIKPDFVHVLVDGRIVKSGGK 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
28-241 |
3.69e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 28 RHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGfvhivdadgteRPVDGDR-------- 98
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSSGRILFDG-----------KPIDYSRkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 -VTFVGQDPSTQVLTLRVVDDVSM-ALEFSLVEAGiVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPE 176
Cdd:PRK13636 83 sVGMVFQDPDNQLFSASVYQDVSFgAVNLKLPEDE-VRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAP 241
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMK-EGRVILQGNP 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
297-493 |
3.82e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-----------GANFRIDGASAR--RVPDAFASWAFQnpeh 363
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdksagshiellGRTVQREGRLARdiRKSRANTGYIFQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 QFTRATVAAEIDSALAGTDPHGPLGADELRKLREALCPRALDPVSPF-----------VLSGGQKRRLGIFLAVAANRRL 432
Cdd:PRK09984 94 QFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVgmvhfahqrvsTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGiTVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
293-471 |
4.31e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.87 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--G----ANFRIDGASARRVPdafaswA--------F 358
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtsGqvlvNGQDLSRLKRREIP------YlrrrigvvF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QnpEHQF-TRATVAAEIdsALA----GTDPhgplgADELRKLREALcpralDPVS--------PFVLSGGQKRRLGIFLA 425
Cdd:COG2884 86 Q--DFRLlPDRTVYENV--ALPlrvtGKSR-----KEIRRRVREVL-----DLVGlsdkakalPHELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDR 471
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL 197
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
292-498 |
4.35e-17 |
|
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: 81.78 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 292 ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG---QMKAGANFR------IDGASARRV-----------PD 351
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlekPAQGTVSFRgqdlyqLDRKQRRAFrrdvqlvfqdsPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 352 AF-----ASWAFQNPEHQFTRATVAAEIDSALAGTDPHGpLGADELRKLrealcpraldpvsPFVLSGGQKRRLGIFLAV 426
Cdd:TIGR02769 100 AVnprmtVRQIIGEPLRHLTSLDESEQKARIAELLDMVG-LRSEDADKL-------------PRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 427 AANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTV-VFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-242 |
4.62e-17 |
|
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: 81.46 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipIDhAGFVHIVDADGTERPVDG--- 96
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE----PT-SGSVLIDGTDINKLKGKAlrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 --DRVTFVGQDPSTqVLTLRVVDDV------------SMALEFSLVEagivaKQSA-EALSELGLSELAEKDPWALSGGQ 161
Cdd:cd03256 76 lrRQIGMIFQQFNL-IERLSVLENVlsgrlgrrstwrSLFGLFPKEE-----KQRAlAALERVGLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 162 RQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGA 240
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLK-DGRIVFDGP 228
|
..
gi 1080238652 241 PE 242
Cdd:cd03256 229 PA 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-216 |
5.03e-17 |
|
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: 80.42 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTInAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFVHIVDADGTERPVDGDRVTFVGQDpstqvLTLRVVD 117
Cdd:cd03297 17 IDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ-----YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 118 DVSMALEFSL-VEAGIVAKQSAEALSE-LGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:cd03297 91 NVRENLAFGLkRKRNREDRISVDELLDlLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|..
gi 1080238652 196 FAAIRDLRAP-GRVILLIEHDL 216
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDL 192
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
294-498 |
5.15e-17 |
|
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: 81.19 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKA-GANFRIDGASARRVPDAFASWAFQnpEHQF 365
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCInrlvepsSGSILLeGTDITKLRGKKLRKLRRRIGMIFQ--HYNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 T-RATVAAEIDSALAGTDP--HGPLG----ADELRKL----REALCPRALDPVSPfvLSGGQKRRLGIFLAVAANRRLLL 434
Cdd:TIGR02315 91 IeRLTVLENVLHGRLGYKPtwRSLLGrfseEDKERALsaleRVGLADKAYQRADQ--LSGGQQQRVAIARALAQQPDLIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 435 LDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR02315 169 ADEPIASLDPKTSKQVMDYLKRINKEDGiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
293-480 |
6.96e-17 |
|
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: 80.56 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERI--LDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQM---KAGANFRIDGASARRVPD------AFA 354
Cdd:COG4778 19 QGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSIlvrHDGGWVDLAQASPREILAlrrrtiGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 SwafqnpehQFTRAT--VAAE---IDSALA-GTDPHGPLgaDELRKLREALC-PRALDPVSPFVLSGGQKRRLGIFLAVA 427
Cdd:COG4778 99 S--------QFLRVIprVSALdvvAEPLLErGVDREEAR--ARARELLARLNlPERLWDLPPATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 428 ANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADR 480
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
39-242 |
7.26e-17 |
|
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: 80.62 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIpshipidhagfvhivdadgteRPVDGdRVTFVGQDPS----TQVLTLR 114
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL---------------------RPDSG-EVLIDGEDISglseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 -----------------VVDDVSMAL-EFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPE 176
Cdd:cd03261 77 rrmgmlfqsgalfdsltVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPE 242
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVL-YDGKIVAEGTPE 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-238 |
7.57e-17 |
|
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: 78.62 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRwAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipidhagfvhivdADGTERPVDGDRV 99
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK---------------PDSGEILVDGKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 TFvgqdpstqvltlrvvDDVSMALEfslveAGI-VAKQsaealselglselaekdpwaLSGGQRQRMAIAGAVARAPEVM 178
Cdd:cd03216 65 SF---------------ASPRDARR-----AGIaMVYQ--------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 179 IFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAH 238
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLR-DGRVVGT 163
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
295-506 |
8.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.43 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGANFR----IDgASARRVPDAFAS--WAFQNPEHQFT 366
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFdgkpID-YSRKGLMKLRESvgMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEIDsalagtdpHGP----LGADELRK-LREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:PRK13636 97 SASVYQDVS--------FGAvnlkLPEDEVRKrVDNALKRTGIEHLKdkpTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 439 LAHLDSPSSRIVLDALAEYA-GAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSR 506
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
280-499 |
1.04e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 280 AVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARrvpdafaswaF 358
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSgEILLDGEPVR----------F 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QNPE----------HQ----FTRATVAAEIdsaLAGTDPHGPLGAD--ELRKLREALCPR---ALDPVSPfV--LSGGQK 417
Cdd:COG1129 71 RSPRdaqaagiaiiHQelnlVPNLSVAENI---FLGREPRRGGLIDwrAMRRRARELLARlglDIDPDTP-VgdLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 418 RRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHD----RRVartwADRASIVAEGKVAWSG 493
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRldevFEI----ADRVTVLRDGRLVGTG 222
|
....*.
gi 1080238652 494 PAADLP 499
Cdd:COG1129 223 PVAELT 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
41-242 |
1.23e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDF----GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDGDRVTFVGQD----PStqvlt 112
Cdd:COG3840 16 LRFDLtiaaGERVAILGPSGAGKSTLLNLIAGFLPPD-----SGRILWNGQDLTALPPAERPVSMLFQEnnlfPH----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGR 192
Cdd:COG3840 86 LTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 193 RSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVtILDADGSVAAHGAPE 242
Cdd:COG3840 166 QEMLDLVDELcRERGLTVLMVTHDPEDAARIADRV-LLVADGRIAADGPTA 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
294-498 |
1.24e-16 |
|
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: 79.72 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVPD---AFASWAFQNPehqftrat 369
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtSGRATVAGHDVVREPRevrRRIGIVFQDL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 vaaEIDSALAGTDP---HGPL----GADELRKLREALCPRAL-----DPVSPFvlSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:cd03265 83 ---SVDDELTGWENlyiHARLygvpGAERRERIDELLDFVGLleaadRLVKTY--SGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 438 PLAHLDsPSSRivlDALAEY-----AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:cd03265 158 PTIGLD-PQTR---AHVWEYieklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
299-497 |
1.52e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.86 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGA--SARRVPDAF----ASWAFQNPEHQFTRATVA 371
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSgKIIIDGVdiTDKKVKLSDirkkVGLVFQYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 AEIdsalagtdPHGP----LGADEL-RKLREALCPRALD-----PVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAH 441
Cdd:PRK13637 103 KDI--------AFGPinlgLSEEEIeNRVKRAMNIVGLDyedykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 442 LDsPSSR-----IVLDALAEYagaGGTVVFTCHDRR-VARtWADRASIVAEGKVAWSGPAAD 497
Cdd:PRK13637 175 LD-PKGRdeilnKIKELHKEY---NMTIILVSHSMEdVAK-LADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
298-470 |
1.52e-16 |
|
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: 79.44 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFAsWAFQNPeHQFTRATVaaeIDS 376
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSgEVLVDGEPVTGPGPDRG-YVFQQD-ALLPWLTV---LDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 377 ALAGTDPHGPLGADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDA 453
Cdd:cd03293 94 VALGLELQGVPKAEARERAEELLELVGLSGFEnayPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE 173
|
170
....*....|....*...
gi 1080238652 454 LAE-YAGAGGTVVFTCHD 470
Cdd:cd03293 174 LLDiWRETGKTVLLVTHD 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
40-241 |
1.56e-16 |
|
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: 79.09 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDAD-GTERPVDGDRVTFVGQDpSTQVLTLRV 115
Cdd:cd03263 20 DLSLNVykGEIFGLLGHNGAGKTTTLKMLTGELrPT------SGTAYINGYSiRTDRKAARQSLGYCPQF-DALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDdvsmALEFSL----VEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:cd03263 93 RE----HLRFYArlkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 192 RRSLFAAIRDLRaPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAP 241
Cdd:cd03263 169 RRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIM-SDGKLRCIGSP 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-220 |
1.67e-16 |
|
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: 78.99 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGfVHIVDADGTERPVDGDRVTFVGQDpSTQVLTL 113
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElPTSGTIRVNG-QDVSDLRGRAIPYLRRKIGVVFQD-FRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:cd03292 94 NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180
....*....|....*....|....*..
gi 1080238652 194 SLFAAIRDLRAPGRVILLIEHDLRPFD 220
Cdd:cd03292 174 EIMNLLKKINKAGTTVVVATHAKELVD 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-498 |
1.97e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.93 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL---------IPSHIPI-DHAGFVHIVDADGTERPVDGDR-- 98
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgrIIYHVALcEKCGYVERPSKVGEPCPVCGGTle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 99 ---VTFVG-QDPSTQVLTLR----------------VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALS 158
Cdd:TIGR03269 91 peeVDFWNlSDKLRRRIRKRiaimlqrtfalygddtVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 159 GGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAA 237
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKAIWLE-NGEIKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 238 HGAPEGIAVKGIATSAAPAGApdastpgtgapdrPDLESEADAVPLLALTGTH--VARGGERILDGADLTLERGEIHALV 315
Cdd:TIGR03269 250 EGTPDEVVAVFMEGVSEVEKE-------------CEVEVGEPIIKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 316 GANGAGKSTLLAVLSGQMKAGAnfridGASARRVPDAFASWAFQNPE------------HQ----FTRATVAAEIDSALA 379
Cdd:TIGR03269 317 GTSGAGKTTLSKIIAGVLEPTS-----GEVNVRVGDEWVDMTKPGPDgrgrakryigilHQeydlYPHRTVLDNLTEAIG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 380 GTDPhgplgaDELRKLREALC----------PRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRI 449
Cdd:TIGR03269 392 LELP------DELARMKAVITlkmvgfdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVD 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 450 VLDA-LAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR03269 466 VTHSiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
303-493 |
2.38e-16 |
|
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: 78.75 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVP--DAFASWAFQnpEHQ-FTRATVAAEIdsAL 378
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVNDQSHTGLApyQRPVSMLFQ--ENNlFAHLTVRQNI--GL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 379 aGTDPHGPLGADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDsPSSRIVLDALA 455
Cdd:TIGR01277 94 -GLHPGLKLNAEQQEKVVDAAQQVGIADYLdrlPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD-PLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 456 EYAGAGG--TVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:TIGR01277 172 KQLCSERqrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
37-242 |
2.76e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 37 DMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhiVDADGTERPVDGDRVTfvgqDPSTQVLTLRvv 116
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL---------------EEITSGDLIVDGLKVN----DPKVDERLIR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSM------------ALE---FSLVEAGIVAKQSAEA-----LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPE 176
Cdd:PRK09493 77 QEAGMvfqqfylfphltALEnvmFGPLRVRGASKEEAEKqarelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRpFDGWVDTVTILDADGSVAAHGAPE 242
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG-FAEKVASRLIFIDKGRIAEDGDPQ 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
35-241 |
3.64e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.82 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGF-VHIVDADGTERPVDgDRVTFVGQDPSTQVLT 112
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDDItITHKTKDKYIRPVR-KRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 lrvvDDVSMALEFSLVEAGI----VAKQSAEALSELGLS-ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:PRK13646 101 ----DTVEREIIFGPKNFKMnldeVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 188 DEDGRRSLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAP 241
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMK-EGSIVSQTSP 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-216 |
3.96e-16 |
|
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: 78.38 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRwAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFVHIVDADGTERPVDGD-- 97
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 98 --RVTFVGQDPStqVLTLRVVDDVSMALEFSLV-EAGIVAKQSAEALSELGLSELAEK--DPWALSGGQRQRMAIAGAVA 172
Cdd:cd03260 80 rrRVGMVFQKPN--PFPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080238652 173 RAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPgRVILLIEHDL 216
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNM 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
39-244 |
4.56e-16 |
|
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: 78.15 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshiPIdhAGFVHIVDADGTERPVDGDRVTFVGQD----PStqvltLR 114
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIK---PD--SGKILLNGKDITNLPPEKRDISYVPQNyalfPH-----MT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 195 LFAAIRDLRAPGRV-ILLIEHDLRpfDGWV--DTVTILdADGSVAAHGAPEGI 244
Cdd:cd03299 168 LREELKKIRKEFGVtVLHVTHDFE--EAWAlaDKVAIM-LNGKLIQVGKPEEV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
303-493 |
6.54e-16 |
|
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: 77.15 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGA--SARRVPDAFASWAFQNpEHQFTRATVAAEIDSALA 379
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVdvTAAPPADRPVSMLFQE-NNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 380 gtdPHGPLGADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAE 456
Cdd:cd03298 97 ---PGLKLTAEDRQAIEVALARVGLAGLEkrlPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080238652 457 -YAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03298 174 lHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
40-230 |
6.57e-16 |
|
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: 77.26 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIpshipidhagfvhivdadgteRPvDGDRVTFVGQDPSTQVLTLRVV- 116
Cdd:cd03268 18 DISLHVkkGEIYGFLGPNGAGKTTTMKIILGLI---------------------KP-DSGEITFDGKSYQKNIEALRRIg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 ---------DDVSM--ALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:cd03268 76 alieapgfyPNLTAreNLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1080238652 186 HVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILD 230
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
303-503 |
9.33e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.52 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKAGANFRIDGASARRVPD--AFASWAFQNPEHQFTRATVAAE 373
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLngllqptSGTVTIGERVITAGKKNKKLKPlrKKVGIVFQFPEHQLFEETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 IdsalagtdPHGPLG-----ADELRKLREALCPRALDPV----SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDS 444
Cdd:PRK13634 107 I--------CFGPMNfgvseEDAKQKAREMIELVGLPEEllarSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 445 PSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
35-216 |
1.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.59 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSL-AHLIAGLIPSHIPIDHAgFVHIVDADGTERpVDGDRVTFVGQDPST----Q 109
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFiEHLNALLLPDTGTIEWI-FKDEKNKKKTKE-KEKVLEKLVIQKTRFkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 110 VLTLRV-VDDVSMALEFSLVEAGI------------VAKQSAEALSE-----LGLSE-LAEKDPWALSGGQRQRMAIAGA 170
Cdd:PRK13651 100 IKEIRRrVGVVFQFAEYQLFEQTIekdiifgpvsmgVSKEEAKKRAAkyielVGLDEsYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 171 VARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-216 |
1.12e-15 |
|
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: 80.87 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 3 GGAPACAGATRGTAPA---RLRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHA 79
Cdd:TIGR02868 315 GPVAEGSAPAAGAVGLgkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 80 GFVHIVDADGTERpvdGDRVTFVGQDPSTQVLTLRvvddvsmalEFSLVEAGIVAKQSA-EALSELGLSELAEKDPW--- 155
Cdd:TIGR02868 395 DGVPVSSLDQDEV---RRRVSVCAQDAHLFDTTVR---------ENLRLARPDATDEELwAALERVGLADWLRALPDgld 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 156 --------ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLfaaIRDLRA--PGRVILLIEHDL 216
Cdd:TIGR02868 463 tvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAalSGRTVVLITHHL 530
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
39-343 |
1.14e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.46 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipidhagfvhivdADGTERPVDGDRVTF-------------VGQD 105
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ---------------PDSGEILIDGKPVRIrsprdaialgigmVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 106 PStQVLTLRVVDDVSMALEfsLVEAGIVAKQSAEALselgLSELAEK-----DPWA----LSGGQRQRMAIAGAVARAPE 176
Cdd:COG3845 89 FM-LVPNLTVAENIVLGLE--PTKGGRLDRKAARAR----IRELSERygldvDPDAkvedLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 177 VMIFDEPAA-----HVDEdgrrsLFAAIRDLRAPGRVILLIEHDLRPfdgwV----DTVTILdADGSVAAHGAPEGIAVK 247
Cdd:COG3845 162 ILILDEPTAvltpqEADE-----LFEILRRLAAEGKSIIFITHKLRE----VmaiaDRVTVL-RRGKVVGTVDTAETSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 248 GIA-----TSAAPAGAPDASTPGTgapdrpdleseadavPLLALTGTHVA-RGGERILDGADLTLERGEIHALVGANGAG 321
Cdd:COG3845 232 ELAelmvgREVLLRVEKAPAEPGE---------------VVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNG 296
|
330 340
....*....|....*....|...
gi 1080238652 322 KSTLLAVLSGQMKAGA-NFRIDG 343
Cdd:COG3845 297 QSELAEALAGLRPPASgSIRLDG 319
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-239 |
1.29e-15 |
|
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: 76.38 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAG-LIPShipidhAGFVHIVDADGTERPVDGDRVTFVGQDpSTQVLTL 113
Cdd:cd03298 13 QPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ------SGRVLINGVDVTAAPPADRPVSMLFQE-NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:cd03298 86 TVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 194 SLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHG 239
Cdd:cd03298 166 EMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLD-NGRIAAQG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
299-504 |
1.30e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.46 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGasaRRVPdafaswaFQNPE----------HQ-FT 366
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSgEILIDG---KPVR-------IRSPRdaialgigmvHQhFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RA---TVAAEIdsALaGTDPHGPLGADeLRKLRE---ALCPR---ALDPVSPfV--LSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:COG3845 91 LVpnlTVAENI--VL-GLEPTKGGRLD-RKAARArirELSERyglDVDPDAK-VedLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADlpASPES 504
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE--TSEEE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
273-497 |
1.47e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 80.56 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 273 DLESEADAVPLLALTG-------THVARGGER-ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDG 343
Cdd:COG4618 314 AVPAEPERMPLPRPKGrlsvenlTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAgSVRLDG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 344 ASARRV-PDAFASW---AFQNPEhqFTRATVA------AEIDSA-------LAGTD------PHG---PLGADELRklre 397
Cdd:COG4618 394 ADLSQWdREELGRHigyLPQDVE--LFDGTIAeniarfGDADPEkvvaaakLAGVHemilrlPDGydtRIGEGGAR---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 398 alcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTw 477
Cdd:COG4618 468 --------------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA- 532
|
250 260
....*....|....*....|
gi 1080238652 478 ADRASIVAEGKVAWSGPAAD 497
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDE 552
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
290-504 |
1.60e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.58 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGAS-----------ARR--- 348
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllerptSGSV------LVDGVDltalserelraARRkig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 349 -VpdafaswaFQnpehQF---TRATVAAEIDSAL--AGTDphgplgadelRKLREAlcpRA---LDPV--------SPFV 411
Cdd:COG1135 86 mI--------FQ----HFnllSSRTVAENVALPLeiAGVP----------KAEIRK---RVaelLELVglsdkadaYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 412 LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDAL----AEYagaGGTVVFTCHDRRVARTWADRASIVAEG 487
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdinREL---GLTIVLITHEMDVVRRICDRVAVLENG 217
|
250
....*....|....*..
gi 1080238652 488 KVAWSGPAADLPASPES 504
Cdd:COG1135 218 RIVEQGPVLDVFANPQS 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
283-507 |
1.84e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGA--------NFRIDGASARRVPDA 352
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRpqKGAvlwqgkplDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 FAswaFQNPEHQFtratVAAEIDSALAGTDPHGPLGADEL-RKLREALcprALDPVSPF------VLSGGQKRRLGIFLA 425
Cdd:PRK13638 81 TV---FQDPEQQI----FYTDIDSDIAFSLRNLGVPEAEItRRVDEAL---TLVDAQHFrhqpiqCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 426 VAANRRLLLLDEPLAHLDsPSSRIVLDALAE-YAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLD-PAGRTQMIAIIRrIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
...
gi 1080238652 505 SRR 507
Cdd:PRK13638 230 MEQ 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
291-493 |
2.09e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 291 VARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKAGANfRIDGASARRVPDAFASWAFQN--P 361
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDK-PISMLSSRQLARRLALLPQHHltP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EHQFTRATVAAeidsalaGTDPH----GPLGADELRKLREALCPRALD-----PVSPfvLSGGQKRRLGIFLAVAANRRL 432
Cdd:PRK11231 89 EGITVRELVAY-------GRSPWlslwGRLSAEDNARVNQAMEQTRINhladrRLTD--LSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
39-244 |
2.20e-15 |
|
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: 76.17 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVH-----IVDADGTERPVDGDRVTFVGQDP----St 108
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPD------SGEILvdgqdITGLSEKELYELRRRIGMLFQGGalfdS- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 qvltLRVVDDVSMAL-EFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:COG1127 97 ----LTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 188 DEDGRRSLFAAIRDLR-APGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGI 244
Cdd:COG1127 173 DPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVL-ADGKIIAEGTPEEL 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
293-493 |
2.67e-15 |
|
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: 74.89 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA---NFRIDGasarrvpdafaswaFQNPEHQFTRAT 369
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsgEVLING--------------RPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDSALagtdpHGPLGADE-LR---KLRealcpraldpvspfVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP 445
Cdd:cd03213 85 GYVPQDDIL-----HPTLTVREtLMfaaKLR--------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 446 SSRIVLDALAEYAGAGGTVVFTCHDRRVARTWA-DRASIVAEGKVAWSG 493
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIHQPSSEIFELfDKLLLLSQGRVIYFG 194
|
|
| EcfT |
cd16914 |
T component of ECF-type transporters; The transmembrane component (T component) of the energy ... |
561-750 |
2.76e-15 |
|
T component of ECF-type transporters; The transmembrane component (T component) of the energy coupling-factor (ECF)-type transporter is a transmembrane protein important for vitamin uptake in prokaryotes. In addition to the T component, energy-coupling factor (ECF) transporters contain an energy-coupling module that consists of two ATP-binding proteins (known as the A and A' components) and a substrate-binding (S) component. ECF transporters comprise a subgroup of ATP-binding cassette (ABC) transporters that do not make use of water-soluble substrate binding proteins or domains, but instead employ integral membrane proteins for substrate binding, the S component, in contrast to classical ABC importers. The T component links the S component to the ATP-binding subcomplex that is composed of the A and A' components.
Pssm-ID: 410987 Cd Length: 233 Bit Score: 76.04 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 561 VLALTVVAFLALAAIAERDVRATAGK------VLLVLLIGVFFGLLGWRSEFYGGGDA--SEAVRHGIHHGLLLMAVFAG 632
Cdd:cd16914 25 LLLLLLLLLLLLLLLAGLPLRLLRLLkrllflLLFLLLILLLLPLGGGGGVFGLGGLGitLEGLLYALLLALRLLAIVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 633 TVLVSACMRVEELFDAMvQRLRVPYTWCTIAISGVSIAAFLRSEIPQLTWAIRLRSMRPERSFRSgfiRATTPARIAFPL 712
Cdd:cd16914 105 ALLLLLTTPPSELLAAL-RRLGVPPKLALLLSLALRFIPLLLEEARRIRDAQRARGGDFSGGGLR---RLRSLGPLLGPL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080238652 713 FVSAVRCAEKLSLTLAMRNFGLYPRRTFRTDHPWRVRD 750
Cdd:cd16914 181 LVRSLRRAEELALAMEARGFGGGKRRTSYRELKFRRRD 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
294-503 |
2.81e-15 |
|
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: 76.04 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVP---DAFASWAFQNPEHQ-FTRA 368
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSgKILLDGQDITKLPmhkRARLGIGYLPQEASiFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAAEIDSALAGtdpHGPLGADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP 445
Cdd:cd03218 91 TVEENILAVLEI---RGLSKKEREEKLEELLEEFHITHLRkskASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 446 SSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
50-236 |
2.99e-15 |
|
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: 75.32 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGL-IPShipidhAGFVHIVDADGTE-RPVDGDR-VTFVGQDPSTQVLTLRvvDDVSMALEFS 126
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLyKPT------SGSVLLDGTDIRQlDPADLRRnIGYVPQDVTLFYGTLR--DNITLGAPLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 127 LVEAGIvakqsaEALSELGLSELAEKDP-----------WALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:cd03245 106 DDERIL------RAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 196 FAAIRDLRAPgRVILLIEHDLrPFDGWVDTVTILDADGSVA 236
Cdd:cd03245 180 KERLRQLLGD-KTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
40-244 |
3.01e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.88 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDAD-GTERPVdGDR-VTFVGQDPStqvL--T 112
Cdd:COG1118 20 DVSLEIasGELVALLGPSGSGKTTLLRIIAGLEtPD------SGRIVLNGRDlFTNLPP-RERrVGFVFQHYA---LfpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP--A--AHVD 188
Cdd:COG1118 90 MTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPfgAldAKVR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 189 EDGRRSLFAAIRDLrapGRVILLIEHD----LRpfdgWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:COG1118 170 KELRRWLRRLHDEL---GGTTVFVTHDqeeaLE----LADRVVVMN-QGRIEQVGTPDEV 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
37-203 |
3.01e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.84 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 37 DMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPShipidhAGFVHIVDADGTERPVDGDRVTFVGQD----PStqvl 111
Cdd:PRK11432 23 DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPT------EGQIFIDGEDVTHRSIQQRDICMVFQSyalfPH---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 tLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:PRK11432 93 -MSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170
....*....|..
gi 1080238652 192 RRSLFAAIRDLR 203
Cdd:PRK11432 172 RRSMREKIRELQ 183
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-239 |
3.16e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.31 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 19 RLRVSGAGVRHADGRwAPDMVDLSF--DFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDAD--GTERPV 94
Cdd:TIGR01842 316 HLSVENVTIVPPGGK-KPTLRGISFslQAGEALAIIGPSGSGKSTLARLIVGIWPPT-----SGSVRLDGADlkQWDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 DGDRVTFVGQDpsTQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEAlSELGL-------SELAEkDPWALSGGQRQRMAI 167
Cdd:TIGR01842 390 FGKHIGYLPQD--VELFPGTVAENIARFGENADPEKIIEAAKLAGV-HELILrlpdgydTVIGP-GGATLSGGQRQRIAL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 168 AGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHdlRP-FDGWVDTVTILDaDGSVAAHG 239
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH--RPsLLGCVDKILVLQ-DGRIARFG 535
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
298-493 |
3.61e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA------------GANFRIDGASA----RRVPDA-----FASW 356
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkygtiqvgdiyiGDKKNNHELITnpysKKIKNFkelrrRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 AFQNPEHQFTRATVAAEIdsalagtdPHGP--LGADELRKLREA---LCPRALD----PVSPFVLSGGQKRRLGIFLAVA 427
Cdd:PRK13631 121 VFQFPEYQLFKDTIEKDI--------MFGPvaLGVKKSEAKKLAkfyLNKMGLDdsylERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 428 ANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
275-499 |
4.16e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 275 ESEADAVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVPDAF 353
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGiVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 AS-----WAFQNPeHQFTRATVAAEIDSALAGTdphgplgADELRKLREAL----CPRALDpVSPFVLSGGQKRRLGIFL 424
Cdd:PRK15439 83 AHqlgiyLVPQEP-LLFPNLSVKENILFGLPKR-------QASMQKMKQLLaalgCQLDLD-SSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 425 AVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLP 499
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
303-498 |
4.20e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVPDAF--ASWAFQnpEHQ-FTRATVAAEIdsAL 378
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPSRrpVSMLFQ--ENNlFSHLTVAQNI--GL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 379 aGTDPHGPLGADELRKLR--------EALCPRAldpvsPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDsPSSRI- 449
Cdd:PRK10771 95 -GLNPGLKLNAAQREKLHaiarqmgiEDLLARL-----PGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-PALRQe 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 450 VLDALAEyagaggtvvfTCHDRRV-----------ARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK10771 168 MLTLVSQ----------VCQERQLtllmvshsledAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
294-506 |
4.49e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLL-------AVLSGQMKAGANFRIDGASARRVPDAFASWAFQNpEHQFT 366
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQ-FYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATvaaeidsALAGTdPHGPL-----GADELRKLREALcpraLDPVS--------PFVLSGGQKRRLGIFLAVAANRRLL 433
Cdd:PRK09493 91 HLT-------ALENV-MFGPLrvrgaSKEEAEKQAREL----LAKVGlaerahhyPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 434 LLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSR 506
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQR 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
284-497 |
4.50e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARggeRiLDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDA----FASW--- 356
Cdd:COG4138 1 LQLNDVAVAG---R-LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAelarHRAYlsq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 ----AFQNPEHQFTratvaaeidsALAGtdpHGPLGADELRKLREALCPR-ALD-----PVSPfvLSGG--QKRRL-GIF 423
Cdd:COG4138 77 qqspPFAMPVFQYL----------ALHQ---PAGASSEAVEQLLAQLAEAlGLEdklsrPLTQ--LSGGewQRVRLaAVL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 424 LAV--AAN--RRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAAD 497
Cdd:COG4138 142 LQVwpTINpeGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
39-216 |
4.58e-15 |
|
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: 74.87 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhiVDADGTERPVDGDRVTfvgqDPSTQVLTLRvvDD 118
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLL---------------EEPDSGTIIIDGLKLT----DDKKNINELR--QK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 VSM------------ALEfSLVEAGI----VAKQSAEA-----LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEV 177
Cdd:cd03262 78 VGMvfqqfnlfphltVLE-NITLAPIkvkgMSKAEAEEralelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
286-489 |
4.99e-15 |
|
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: 74.49 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 286 LTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRIDGasaRRVPDAFASWA------ 357
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPDSG-TIIIDG---LKLTDDKKNINelrqkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 ---FQNpEHQFTRATVAAEIdsALAGTDPHGPLGADELRKLREALCPRALDP---VSPFVLSGGQKRRLGIFLAVAANRR 431
Cdd:cd03262 79 gmvFQQ-FNLFPHLTVLENI--TLAPIKVKGMSKAEAEERALELLEKVGLADkadAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
299-489 |
5.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AG----ANFRIDGASARRVPDAF---ASWAFQNPEHQFTRAT 369
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpsSGtitiAGYHITPETGNKNLKKLrkkVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDsalagtdpHGPL--GADE-------LRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:PRK13641 103 VLKDVE--------FGPKnfGFSEdeakekaLKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 441 HLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
39-183 |
5.30e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.03 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipIDhAGFVHivdadgterpVDGDRVTfvgqDPSTQVLTLRvvDD 118
Cdd:COG1126 20 ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE----PD-SGTIT----------VDGEDLT----DSKKDINKLR--RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 VSM------------ALEfSLVEAGI-VAKQS-AEA-------LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEV 177
Cdd:COG1126 79 VGMvfqqfnlfphltVLE-NVTLAPIkVKKMSkAEAeeramelLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
....*.
gi 1080238652 178 MIFDEP 183
Cdd:COG1126 158 MLFDEP 163
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
40-239 |
5.69e-15 |
|
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: 74.62 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDGteRPVDGDRVTFVGQDPSTQVLTLRV-V 116
Cdd:cd03269 18 DISFSVekGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLF---DG--KPLDIAARNRIGYLPEERGLYPKMkV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALE----FSLVEAgivAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGR 192
Cdd:cd03269 88 IDQLVYLAqlkgLKKEEA---RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 193 RSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHG 239
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLN-KGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
295-506 |
5.85e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKAGaNFRIDGA-------SARRVPDAFASWAFQN 360
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVG-DITIDTArslsqqkGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 361 pEHQFTRATVAAEIdsalagtdPHGPLGAD-ELRKLREALCPRALDPVS--------PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:PRK11264 94 -FNLFPHRTVLENI--------IEGPVIVKgEPKEEATARARELLAKVGlagketsyPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSR 506
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
39-242 |
5.92e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGlIPSHIPIDhaGFVHIVDADGTERPVDgDRVT---FVG-QDP------ST 108
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKYEVTS--GSILLDGEDILELSPD-ERARagiFLAfQYPveipgvSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVLtLR-----VVDDVSMALEFSlveagivaKQSAEALSELGLSE------LAEKdpwaLSGGQRQRMAIAGAVARAPEV 177
Cdd:COG0396 95 SNF-LRtalnaRRGEELSAREFL--------KLLKEKMKELGLDEdfldryVNEG----FSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLR------PfdgwvDTVTILdADGSVAAHGAPE 242
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRildyikP-----DFVHVL-VDGRIVKSGGKE 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
51-244 |
6.15e-15 |
|
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: 76.76 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 51 ITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDGDRVTFVGQD----PStqvltLRVVDDVSMALEF 125
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEqPD------SGSIMLDGEDVTNVPPHLRHINMVFQSyalfPH-----MTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 126 SLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RA 204
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 205 PGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMR-KGKIAQIGTPEEI 188
|
|
| EcfT |
COG0619 |
ECF-type transporter transmembrane protein EcfT [Coenzyme transport and metabolism]; |
560-750 |
6.23e-15 |
|
ECF-type transporter transmembrane protein EcfT [Coenzyme transport and metabolism];
Pssm-ID: 440384 Cd Length: 249 Bit Score: 75.31 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 560 AVLALTVVAFLALAAIAERDVRATAGKVLLVLLIGVFFGLLGWrseFYGGGDA----------SEAVRHGIHHGLLLMAV 629
Cdd:COG0619 40 LVLLVLLLLALLLLLLAGIPLRRLLKRLLPLLPFLLLLLLLLP---LFVPGTVlfslgpltitREGLLLALLLALRLLAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 630 FAGTVLVSACMRVEELFDAMvQRLRVPYTWCTIAISGVSIAAFLRSEIPQLTWAIRLRSMRPERSFRsgfiRATTPARIA 709
Cdd:COG0619 117 VLAALLLLLTTPPSDLLAAL-RRLGVPPELALMLLLALRFIPVLLEEARRIREAQRARGGDFGKLRR----RLRSLGPLL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 710 FPLFVSAVRCAEKLSLTLAMRNFGLYPRRTFRTDHPWRVRD 750
Cdd:COG0619 192 GPLLVRSLRRAERLALAMEARGFGGGGKRTSLRELRFSRRD 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
299-493 |
8.03e-15 |
|
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: 74.33 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANF-RIDG-------ASARR----VPDAFASWAfqnpehqft 366
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFaTVDGfdvvkepAEARRrlgfVSDSTGLYD--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEID--SALAGTDPHGPLGAdeLRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDS 444
Cdd:cd03266 92 RLTARENLEyfAGLYGLKGDELTAR--LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 445 PSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
298-505 |
9.60e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN-----FRIDG--ASARRVPDAFASWAFQNPEHQF----T 366
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRqtagrVLLDGkpVAPCALRGRKIATIMQNPRSAFnplhT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEIDSALAGTDPHGPLgADELRKLREALCPRALDpVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPS 446
Cdd:PRK10418 98 MHTHARETCLALGKPADDATL-TAALEAVGLENAARVLK-LYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 447 SRIVLDALAEYAGAGGT-VVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESS 505
Cdd:PRK10418 176 QARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
297-489 |
1.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDG-----ASARRVPDAF-----ASWAFQNPEHQFT 366
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipANLKKIKEVKrlrkeIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEIdsalagtdPHGP--LGADE---LRKLREAL----CPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:PRK13645 105 QETIEKDI--------AFGPvnLGENKqeaYKKVPELLklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 438 PLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
289-512 |
1.24e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.84 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 289 THVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANF------RIDGASARRVpDAFASWAFQNPE 362
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgePITKENIREV-RKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 HQFTRATVaaEIDSALAGTDphgpLGADE---LRKLREALCPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:PRK13652 89 DQIFSPTV--EQDIAFGPIN----LGLDEetvAHRVSSALHMLGLEELrdrVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 437 EPLAHLDSPSSRIVLDALAEYAGA-GGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSRRDR----PL 511
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHldlpSL 242
|
.
gi 1080238652 512 P 512
Cdd:PRK13652 243 P 243
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
291-469 |
1.25e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 73.05 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 291 VARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAG---ANFRIDGasaRRVPDAFA---SWAFQNPEHq 364
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvitGEILING---RPLDKNFQrstGYVEQQDVH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 FTRATVaaeidsalagtdphgplgadelrklREAL----CPRAldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:cd03232 91 SPNLTV-------------------------REALrfsaLLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180
....*....|....*....|....*....
gi 1080238652 441 HLDSPSSRIVLDALAEYAGAGGTVVFTCH 469
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
32-244 |
1.28e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDGDRVTFVGQDPSTQVL 111
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-----AGNIIIDDEDISLLPLHARARRGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 --TLRVVDDVSMALEfslVEAGIVAKQSA----EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:PRK10895 90 frRLSVYDNLMAVLQ---IRDDLSAEQREdranELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 186 HVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGI 244
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIV-SQGHLIAHGTPTEI 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-183 |
1.37e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPShipidhAGFVHIVDADGTERPVDGDRVTFVGQD---- 105
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPD------SGRIMLDGQDITHVPAENRHVNTVFQSyalf 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 106 PStqvltLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:PRK09452 99 PH-----MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
39-241 |
1.38e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL--IPShipidhaGFVHIVDADGTERPVDGDRVTFVGQD----PStqvlt 112
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLedITS-------GDLFIGEKRMNDVPPAERGVGMVFQSyalyPH----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGR 192
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 193 RSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAP 241
Cdd:PRK11000 170 VQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDA-GRVAQVGKP 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
293-502 |
1.49e-14 |
|
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: 75.92 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDgADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDG-------------ASARRVpdafaSWAF 358
Cdd:TIGR02142 8 RLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPdEGEIVLNGrtlfdsrkgiflpPEKRRI-----GYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QNPEhQFTRATVAAEIDSALAGTDPhgplgadELRKLREALCPR--ALDPV---SPFVLSGGQKRRLGIFLAVAANRRLL 433
Cdd:TIGR02142 82 QEAR-LFPHLSVRGNLRYGMKRARP-------SERRISFERVIEllGIGHLlgrLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 434 LLDEPLAHLDSPSSRIVLDALAEYAGAGGT-VVFTCHD-RRVARTwADRASIVAEGKVAWSGPAADLPASP 502
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSlQEVLRL-ADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-296 |
1.57e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGrwapdmVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDadgteRPVDGDRV 99
Cdd:PRK09536 9 LSVEFGDTTVLDG------VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-----AGTVLVAG-----DDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 TFVGQdpstQVLTlrVVDDVSMALEFS---LVEAGIVAKQS-------------AEALSELGLSELAEKDPWALSGGQRQ 163
Cdd:PRK09536 73 RAASR----RVAS--VPQDTSLSFEFDvrqVVEMGRTPHRSrfdtwtetdraavERAMERTGVAQFADRPVTSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 164 RMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEG 243
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL-ADGRVRAAGPPAD 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 244 IAVKGIATSAAPAGAPDASTPGTGAPDRPDLeSEADAVPLLALTGTHVARGGE 296
Cdd:PRK09536 226 VLTADTLRAAFDARTAVGTDPATGAPTVTPL-PDPDRTEAAADTRVHVVGGGQ 277
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
294-489 |
1.94e-14 |
|
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: 73.06 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGasaRRVPDAFA-----SWAFQN----Peh 363
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGG---RDVTDLPPkdrdiAMVFQNyalyP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 qftRATVAAEIDSALagtdphgplgadELRKLREALCPRALDPVS------------PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:cd03301 86 ---HMTVYDNIAFGL------------KLRKVPKDEIDERVREVAellqiehlldrkPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 432 LLLLDEPLAHLDSP---SSRIVLDALAEYAGAggTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03301 151 VFLMDEPLSNLDAKlrvQMRAELKRLQQRLGT--TTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
295-515 |
2.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN----FRIDGASARRVPD--AFASWAFQNPEHQFTRA 368
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvlvSGIDTGDFSKLQGirKLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVaaEIDSALagtdphGP----LGADELRKLRE-ALCPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:PRK13644 94 TV--EEDLAF------GPenlcLPPIEIRKRVDrALAEIGLEKYrhrSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 441 HLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTwADRASIVAEGKVAWSGpaadlpaSPESSRRDRPLPAAG 515
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEG-------EPENVLSDVSLQTLG 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
299-489 |
2.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGAS-ARRVPDAF-------ASWAFQNPEHQFTRAT 369
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITiTHKTKDKYirpvrkrIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDsalagtdpHGP---------LGADELRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:PRK13646 103 VEREII--------FGPknfkmnldeVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 441 HLDSPSSRIVLDALAEYA-GAGGTVVFTCHD-RRVARtWADRASIVAEGKV 489
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVAR-YADEVIVMKEGSI 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
282-494 |
2.31e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.37 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRIDG-------ASARRVPDA 352
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfeTPDSG-RIMLDGqdithvpAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 FASWAFqnpehqFTRATV--------------AAEIDsalagtdphgPLGADELRKLR-EALCPRaldpvSPFVLSGGQK 417
Cdd:PRK09452 92 FQSYAL------FPHMTVfenvafglrmqktpAAEIT----------PRVMEALRMVQlEEFAQR-----KPHQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 418 RRLGIFLAVAANRRLLLLDEPLAHLD---SPSSRIVLDALAEYAGAggTVVFTCHDRRVARTWADRASIVAEGKVAWSGP 494
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDyklRKQMQNELKALQRKLGI--TFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
40-242 |
2.45e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAG-LIPSHipidhaGFVHIVD---ADGTERPVdGDRVTFVGQDPST-QVLT 112
Cdd:PRK11231 20 DLSLSLptGKITALIGPNGCGKSTLLKCFARlLTPQS------GTVFLGDkpiSMLSSRQL-ARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRvvddvsmalefSLVEAG------IVAKQSAE-------ALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMI 179
Cdd:PRK11231 93 VR-----------ELVAYGrspwlsLWGRLSAEdnarvnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 180 FDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPE 242
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVL-ANGHVMAQGTPE 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
35-239 |
2.48e-14 |
|
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: 72.79 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhiVDADGTERPVDGDRVTfvgQDPSTQVLTLR 114
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL---------------LEPDAGFATVDGFDVV---KEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDvSMAL--EFSLVE-----------AGIVAKQSAEALSE-LGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIF 180
Cdd:cd03266 82 FVSD-STGLydRLTAREnleyfaglyglKGDELTARLEELADrLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 181 DEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHG 239
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVL-HRGRVVYEG 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
284-469 |
2.61e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.39 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVPDAFAswafQNPE 362
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNGTPLAEQRDEPH----ENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 HQFTRATVAAEIdSALAGTDPHGPLGADELRKLREALCPRALDPVS--PF-VLSGGQKRRLGIFLAVAANRRLLLLDEPL 439
Cdd:TIGR01189 77 YLGHLPGLKPEL-SALENLHFWAAIHGGAQRTIEDALAAVGLTGFEdlPAaQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1080238652 440 AHLDSPSSRIVLDALAEYAGAGGTVVFTCH 469
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
284-469 |
2.83e-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: 72.14 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM-KAGANFRIDGASARRVPDAFAS---WAfq 359
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLDFQRDSIARgllYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 npEHQFTRATVAaeidSALAGTDPHGPLGADElrKLREALCP---RALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:cd03231 79 --GHAPGIKTTL----SVLENLRFWHADHSDE--QVEEALARvglNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|...
gi 1080238652 437 EPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCH 469
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
35-239 |
2.93e-14 |
|
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: 73.00 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgtERPVDGdRVTFVGQDPST----QV 110
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL---------------------ERPTSG-SVLVDGTDLTLlsgkEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLR-----------------VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVAR 173
Cdd:cd03258 78 RKARrrigmifqhfnllssrtVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 174 APEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHG 239
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVME-KGEVVEEG 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
40-242 |
3.05e-14 |
|
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: 76.41 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIVDADGTERPVDG--DRVTFVGQDPstqVL---T 112
Cdd:COG2274 493 NISLTIkpGERVAIVGRSGSGKSTLLKLLLGLYE-----PTSGRILIDGIDLRQIDPASlrRQIGVVLQDV---FLfsgT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRvvDDVSMAL-EFSLVEAgivakqsAEALSELGLSELAEKDPW-----------ALSGGQRQRMAIAGAVARAPEVMIF 180
Cdd:COG2274 565 IR--ENITLGDpDATDEEI-------IEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 181 DEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD-------GSVAAHGAPE 242
Cdd:COG2274 636 DEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS---------TIRLADriivldkGRIVEDGTHE 694
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
302-493 |
3.89e-14 |
|
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: 71.94 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 302 ADLTLErGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDG-------------ASARRVpdafaSWAFQNPEhQFTR 367
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVLNGtvlfdsrkkinlpPQQRKI-----GLVFQQYA-LFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAEIDSALAGTDPhgplgaDELRKLREALCPR-ALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:cd03297 90 LNVRENLAFGLKRKRN------REDRISVDELLDLlGLDHLlnrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 444 SPSSRIVLDALAE-YAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03297 164 RALRLQLLPELKQiKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
282-502 |
4.17e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGAnFRIDGASARRVPDA------- 352
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDSGR-ILLDGRDVTGLPPEkrnvgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 FASWA-------FQN----PEHQ-FTRATVAAEIDSALAGTDphgpLGADELRKLREalcpraldpvspfvLSGGQKRRL 420
Cdd:COG3842 83 FQDYAlfphltvAENvafgLRMRgVPKAEIRARVAELLELVG----LEGLADRYPHQ--------------LSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 421 GIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL- 498
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIy 224
|
....*.
gi 1080238652 499 --PASP 502
Cdd:COG3842 225 erPATR 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
294-489 |
4.44e-14 |
|
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: 71.93 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN-FRIDGASA--------------------RRVPDA 352
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGeVLFDGKPLdiaarnrigylpeerglypkMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 ---FASWafqnpeHQFTRATVAAEIDSALAGTDphgpLGADELRKLREalcpraldpvspfvLSGGQKRRLGIFLAVAAN 429
Cdd:cd03269 91 lvyLAQL------KGLKKEEARRRIDEWLERLE----LSEYANKRVEE--------------LSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 430 RRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
299-489 |
4.92e-14 |
|
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: 71.67 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN-FRIDGASARRVPDAFASW-------AFQNPEHQFTRaTV 370
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtIRVNGQDVSDLRGRAIPYlrrkigvVFQDFRLLPDR-NV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIDSALAGTDpHGPlgadelRKLREALcPRALDPVS--------PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHL 442
Cdd:cd03292 96 YENVAFALEVTG-VPP------REIRKRV-PAALELVGlshkhralPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 443 DSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-489 |
6.39e-14 |
|
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: 74.86 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 27 VRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipiDHAGFVHIVDADGTERPV-DGDR--VTFVG 103
Cdd:TIGR02633 8 VKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG---TWDGEIYWSGSPLKASNIrDTERagIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 104 QDpSTQVLTLRVVDDVSMALEFSLvEAGIVA-----KQSAEALSELGLSELAEKDPWA-LSGGQRQRMAIAGAVARAPEV 177
Cdd:TIGR02633 85 QE-LTLVPELSVAENIFLGNEITL-PGGRMAynamyLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGIAVKGIATSAapAG 257
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI-RDGQHVATKDMSTMSEDDIITMM--VG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 258 APDASTPGTGAPDRPDLESEADAVPLLALTGTHVARggeriLDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM--KA 335
Cdd:TIGR02633 240 REITSLYPHEPHEIGDVILEARNLTCWDVINPHRKR-----VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 336 GANFRIDG--ASARRVPDAFASWAFQNPEHQFTRATV---AAEIDSALAGTDPHGPLG----ADELRKLREALCPRALDP 406
Cdd:TIGR02633 315 EGNVFINGkpVDIRNPAQAIRAGIAMVPEDRKRHGIVpilGVGKNITLSVLKSFCFKMridaAAELQIIGSAIQRLKVKT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 407 VSPFV----LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRAS 482
Cdd:TIGR02633 395 ASPFLpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVL 474
|
....*..
gi 1080238652 483 IVAEGKV 489
Cdd:TIGR02633 475 VIGEGKL 481
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-242 |
6.78e-14 |
|
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: 73.98 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHipidhaGFVHI-----VDAD-GTERPVDGDRVTFVGQDPStqvL 111
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLErPDS------GRIRLggevlQDSArGIFLPPHRRRIGYVFQEAR---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 --TLRVVDDvsmaLEFSLVEAGIVAKQS--AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:COG4148 89 fpHLSVRGN----LLYGRKRAPRAERRIsfDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 188 DEDGRRSLFAAIRDLRAPGRV-ILLIEHDLRPfdgwV----DTVTILDaDGSVAAHGAPE 242
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIpILYVSHSLDE----VarlaDHVVLLE-QGRVVASGPLA 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
283-493 |
6.88e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.37 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGA-NFRIDGASARRVPDAfaswafq 359
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLDDGRiIYEQDLIVARLQQDP------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 nPEHQ------FTRATVAAEID--------SALAGTDPHGPLgADELRKLREAL---------------CPR-ALDPVSP 409
Cdd:PRK11147 76 -PRNVegtvydFVAEGIEEQAEylkryhdiSHLVETDPSEKN-LNELAKLQEQLdhhnlwqlenrinevLAQlGLDPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 410 FV-LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAggtVVFTCHDRRVARTWADRASIVAEGK 488
Cdd:PRK11147 154 LSsLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHDRSFIRNMATRIVDLDRGK 230
|
....*.
gi 1080238652 489 -VAWSG 493
Cdd:PRK11147 231 lVSYPG 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
31-215 |
7.22e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.10 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSH--IPIDHAGFVHIvdaDGTERPVDgdrVTFvgqdps 107
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAgqIMLDGVDLSHV---PPYQRPIN---MMF------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 108 tQVLTL----RVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:PRK11607 98 -QSYALfphmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|...
gi 1080238652 184 AAHVDEDGRRSLFAAIRD-LRAPGRVILLIEHD 215
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDiLERVGVTCVMVTHD 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
28-244 |
8.32e-14 |
|
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: 71.95 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 28 RHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTER-PVDGDR-VTFVGQ 104
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT------SGEIFIDGEDIREQdPVELRRkIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 105 D----PStqvltLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGL--SELAEKDPWALSGGQRQRMAIAGAVARAPEVM 178
Cdd:cd03295 83 QiglfPH-----MTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 179 IFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMK-NGEIVQVGTPDEI 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
294-498 |
9.48e-14 |
|
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: 74.69 E-value: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRV-PDAFASWAFQNPEH-QFTRATV 370
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGiWPPTSGSVRLDGADLKQWdRETFGKHIGYLPQDvELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIDSALAGTDPHGPLGADELRKLREALC--PRALDPV-----SPfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:TIGR01842 409 AENIARFGENADPEKIIEAAKLAGVHELILrlPDGYDTVigpggAT--LSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 444 SPSSRIVLDALAEYAGAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR01842 487 EEGEQALANAIKALKARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
299-489 |
9.56e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM--KAGAnFRIDGasarRVPDAFASW--------AFQNPEHQFTRA 368
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlpEAGT-ITVGG----MVLSEETVWdvrrqvgmVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAaeiDSALAGTDPHG-PlgadelrklREALCPR---ALDPV--------SPFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:PRK13635 98 TVQ---DDVAFGLENIGvP---------REEMVERvdqALRQVgmedflnrEPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 437 EPLAHLDsPSSRI-VLDALAEYAGAGG-TVVFTCHD-RRVARtwADRASIVAEGKV 489
Cdd:PRK13635 166 EATSMLD-PRGRReVLETVRQLKEQKGiTVLSITHDlDEAAQ--ADRVIVMNKGEI 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
39-242 |
9.73e-14 |
|
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: 70.63 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGlipshipidHAGFvhivdadgteRPVDGdRVTFVGQDpstqVLTLRVVDD 118
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMG---------HPKY----------EVTEG-EILFKGED----ITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 VSMalefslveaGI-VAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFA 197
Cdd:cd03217 75 ARL---------GIfLAFQYPPEIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 198 AIRDLRAPGRVILLIEHDLRPFDGWV-DTVTILDaDGSVAAHGAPE 242
Cdd:cd03217 146 VINKLREEGKSVLIITHYQRLLDYIKpDRVHVLY-DGRIVKSGDKE 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
272-469 |
9.77e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 272 PDLESEADAVPLLALTGT----HVA---RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM--KAGAnFRID 342
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEiefeNVSfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdpTSGR-ILID 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 343 GASARRVPdaFASW------AFQNPeHQFTRaTVAAEIdsALagtdphGPLGADElRKLREALcpRALDpVSPFV----- 411
Cdd:COG1132 401 GVDIRDLT--LESLrrqigvVPQDT-FLFSG-TIRENI--RY------GRPDATD-EEVEEAA--KAAQ-AHEFIealpd 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 412 ------------LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAgAGGTVVFTCH 469
Cdd:COG1132 465 gydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAH 533
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-509 |
1.40e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 280 AVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFR------IDGASARRVPDAF 353
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdvlLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 -----ASWAFQNPeHQFTRATvaaeIDSALAGTDPHGPLGADELRKLREALCPRA--LDPV------SPFVLSGGQKRRL 420
Cdd:PRK14271 98 efrrrVGMLFQRP-NPFPMSI----MDNVLAGVRAHKLVPRKEFRGVAQARLTEVglWDAVkdrlsdSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 421 GIFLAVAANRRLLLLDEPLAHLDsPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPA 500
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALD-PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
....*....
gi 1080238652 501 SPESSRRDR 509
Cdd:PRK14271 252 SPKHAETAR 260
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
314-504 |
1.46e-13 |
|
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: 72.53 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 314 LVGANGAGKSTLLAVLSG--QMKAGaNFRIDGASARRVPD-------AFASWAFqnpehqFTRATVAAEIDSALagtdph 384
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGfeQPDSG-SIMLDGEDVTNVPPhlrhinmVFQSYAL------FPHMTVEENVAFGL------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 385 gplgadELRKL-REALCPRALDPVS-----------PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP-SSRIVL 451
Cdd:TIGR01187 68 ------KMRKVpRAEIKPRVLEALRlvqleefadrkPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlRDQMQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 452 DALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:TIGR01187 142 ELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
294-502 |
1.62e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 72.49 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMK-AGANFRID-GASARRVpdafaSWAFQNPehq 364
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdSGRIVlNGRDLFTNlPPRERRV-----GFVFQHY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 ftrA-----TVAAEIDSALagtdPHGPLGADELRKLREALcpraLDPVS--------PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:COG1118 85 ---AlfphmTVAENIAFGL----RVRPPSKAEIRARVEEL----LELVQlegladryPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 432 LLLLDEPLAHLDS---PSSRIVL-DALAEYagaGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL---PASP 502
Cdd:COG1118 154 VLLLDEPFGALDAkvrKELRRWLrRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVydrPATP 228
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
128-489 |
1.76e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.05 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 128 VEAGIVAKQSAEALSELGLSELAEKDP-WALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDgrrslfAAI---RDLR 203
Cdd:PRK10636 120 IDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD------AVIwleKWLK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 204 APGRVILLIEHDLRPFDGWVDTV------TILDADGSVAA----------------HGAPEGIA--------VKGIATSA 253
Cdd:PRK10636 194 SYQGTLILISHDRDFLDPIVDKIihieqqSLFEYTGNYSSfevqratrlaqqqamyESQQERVAhlqsyidrFRAKATKA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 254 ----------------APAGAPDASTPGTGAPdrpdlesEADAVPLLALTGTHVARGGERILDGADLTLERGEIHALVGA 317
Cdd:PRK10636 274 kqaqsrikmlermeliAPAHVDNPFHFSFRAP-------ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 318 NGAGKSTLLAVLSGQMkagANFRIDGASARRVPDAFaswaFQNPEHQFTRATvaaeiDSALAGTDPHGPLGADElrKLRE 397
Cdd:PRK10636 347 NGAGKSTLIKLLAGEL---APVSGEIGLAKGIKLGY----FAQHQLEFLRAD-----ESPLQHLARLAPQELEQ--KLRD 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 398 ALC------PRALDPVSPFvlSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAggtVVFTCHDR 471
Cdd:PRK10636 413 YLGgfgfqgDKVTEETRRF--SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDR 487
|
410
....*....|....*...
gi 1080238652 472 RVARTWADRASIVAEGKV 489
Cdd:PRK10636 488 HLLRSTTDDLYLVHDGKV 505
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
253-470 |
2.72e-13 |
|
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: 73.16 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 253 AAPAGAPDASTPGTGAPDRPDLEseadavpllaLTGTHVAR-GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG 331
Cdd:TIGR02868 314 AGPVAEGSAPAAGAVGLGKPTLE----------LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 332 QMKA-GANFRIDGASARRVPD----AFASWAFQNPeHQFTrATVAAEIdsALAGTDPHGPLGADELRKLREALCPRAL-D 405
Cdd:TIGR02868 384 LLDPlQGEVTLDGVPVSSLDQdevrRRVSVCAQDA-HLFD-TTVRENL--RLARPDATDEELWAALERVGLADWLRALpD 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 406 PVSPFV------LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEyAGAGGTVVFTCHD 470
Cdd:TIGR02868 460 GLDTVLgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-216 |
3.00e-13 |
|
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: 70.75 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIvdaDGTE---------RPVDGDRVTFVGQdpST 108
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePT------SGKVLI---DGQDiaamsrkelRELRRKKISMVFQ--SF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVLTLR-VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHV 187
Cdd:cd03294 112 ALLPHRtVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190
....*....|....*....|....*....|
gi 1080238652 188 DEDGRRSLFAAIRDLRAP-GRVILLIEHDL 216
Cdd:cd03294 192 DPLIRREMQDELLRLQAElQKTIVFITHDL 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
298-493 |
3.32e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.40 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGA--SARRVPDA--FASWAFQNPEHQFTRATVAA 372
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSgEIKIDGItiSKENLKEIrkKIGIIFQNPDNQFIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSALAG--TDPhgplgaDELRKLREALCPRA-----LDPvSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP 445
Cdd:PRK13632 104 DIAFGLENkkVPP------KKMKDIIDDLAKKVgmedyLDK-EPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 446 SSRIVLDALAEYAGAGG-TVVFTCHDRRVArTWADRASIVAEGKVAWSG 493
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-222 |
3.56e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 5 APACAGATRGTAPARLRVSGAGVRHADGRwaPDMVDLSFdfgTINA-----ITGPVGCGKTSLAHLIAGLIPShipidha 79
Cdd:COG4178 348 LPEAASRIETSEDGALALEDLTLRTPDGR--PLLEDLSL---SLKPgerllITGPSGSGKSTLLRAIAGLWPY------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 80 gfvhivdADGT-ERPvDGDRVTFVGQDPSTQVLTLRvvddvsMALEFSLVEAGIVAKQSAEALSELGLSELAEK----DP 154
Cdd:COG4178 416 -------GSGRiARP-AGARVLFLPQRPYLPLGTLR------EALLYPATAEAFSDAELREALEAVGLGHLAERldeeAD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 155 WA--LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDlRAPGRVILLIEH------------DLRPFD 220
Cdd:COG4178 482 WDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHrstlaafhdrvlELTGDG 560
|
..
gi 1080238652 221 GW 222
Cdd:COG4178 561 SW 562
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
39-217 |
3.67e-13 |
|
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: 69.77 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPShipidhAGFVHIVDAD---GTERP---VDGDRVTFVGQdpSTQVL 111
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPT------SGTVRLAGQDlfaLDEDArarLRARHVGFVFQ--SFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 -TLRVVDDVSMALEfsLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:COG4181 103 pTLTALENVMLPLE--LAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180
....*....|....*....|....*...
gi 1080238652 191 GRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:COG4181 181 TGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
40-236 |
3.76e-13 |
|
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: 69.12 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDFGTINAITGPVGCGKTSLAHLIAGLIpshIPIDHAGFVHIVDADGT---ERPVdgdrvTFVGQDpSTQVLTLRVV 116
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFI---EPASGSIKVNDQSHTGLapyQRPV-----SMLFQE-NNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLF 196
Cdd:TIGR01277 89 QNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 197 AAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILdADGSVA 236
Cdd:TIGR01277 169 ALVKQLcSERQRTLLMVTHHLSDARAIASQIAVV-SQGKIK 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
295-498 |
3.76e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAG------ANFRIDGASARRVPDAF---ASWAFQNPEHQF 365
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtvGDIVVSSTSKQKEIKPVrkkVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TRATVAAEIdsalagtdPHGPLGADELRKLREALCPRALDPV---------SPFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:PRK13643 98 FEETVLKDV--------AFGPQNFGIPKEKAEKIAAEKLEMVgladefwekSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 437 EPLAHLDsPSSRIVLDALAE-YAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK13643 170 EPTAGLD-PKARIEMMQLFEsIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
41-242 |
3.93e-13 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 69.49 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDGTERPVDGDRVTFVGQ----------DPSTQV 110
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPA-----KGTVKV---AGASPGKGWRHIGYVPQrhefawdfpiSVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRvvddvsmALEFSLVEAGIVAKQSA--EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:TIGR03771 73 MSGR-------TGHIGWLRRPCVADFAAvrDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 189 EDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdaDGSVAAHGAPE 242
Cdd:TIGR03771 146 MPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLL--NGRVIADGTPQ 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
294-502 |
4.15e-13 |
|
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: 69.68 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDG--ASARRVPDAFASWAFQNpEHQFTRATV 370
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGedATDVPVQERNVGFVFQH-YALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIDSALAGTDPHGPLGADELR-KLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPS 446
Cdd:cd03296 92 FDNVAFGLRVKPRSERPPEAEIRaKVHELLKLVQLDWLAdryPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 447 SRIVLDALAE-YAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL---PASP 502
Cdd:cd03296 172 RKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVydhPASP 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
20-188 |
4.49e-13 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 69.70 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshipidhagfvhivdadgterPVDGdRV 99
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE---------------------PTSG-EI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 TFVGQDPSTQ---------------------VLTLRVVDDV------------SMALEFSLVEagivaKQSA-EALSELG 145
Cdd:COG3638 61 LVDGQDVTALrgralrrlrrrigmifqqfnlVPRLSVLTNVlagrlgrtstwrSLLGLFPPED-----RERAlEALERVG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1080238652 146 LSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:COG3638 136 LADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
285-497 |
4.77e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 285 ALTGTHVARGGE-RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGaNFRIDGasarRVpdafaSW----- 356
Cdd:COG1134 27 LLLRRRRTRREEfWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptSG-RVEVNG----RV-----SAllelg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 -AFqNPE-------------HQFTRATVAAEIDS--ALAGtdphgpLGadelrklrealcpRALD-PVSpfVLSGGQKRR 419
Cdd:COG1134 97 aGF-HPEltgreniylngrlLGLSRKEIDEKFDEivEFAE------LG-------------DFIDqPVK--TYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 420 LGiFlAVAANRR--LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAAD 497
Cdd:COG1134 155 LA-F-AVATAVDpdILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-214 |
5.31e-13 |
|
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: 68.65 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 26 GVRHADGRWAPD-------MVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdadgterpvdG 96
Cdd:cd03250 2 SVEDASFTWDSGeqetsftLKDINLEVpkGELVAIVGPVGSGKSSLLSALLGELEKL-----SGSVSV-----------P 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 DRVTFVGQDPSTQVLTLR----------------VVDDVSMALEFSLVEAGIvakqsaealselgLSELAEKDPwALSGG 160
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRenilfgkpfdeeryekVIKACALEPDLEILPDGD-------------LTEIGEKGI-NLSGG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 161 QRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFA-AIRDLRAPGRVILLIEH 214
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTH 186
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-242 |
6.64e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 72.09 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 18 ARLRVSGAGVRHADGRwAPDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGT--ERP 93
Cdd:COG4618 329 GRLSVENLTVVPPGSK-RPILRGVSFSLepGEVLGVIGPSGSGKSTLARLLVGVWPPT-----AGSVRLDGADLSqwDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 94 VDGDRVTFVGQDPstQVLTLRVVDDVSMALEFSlVEAGIVAKQSAEA--------------LSELGLselaekdpwALSG 159
Cdd:COG4618 403 ELGRHIGYLPQDV--ELFDGTIAENIARFGDAD-PEKVVAAAKLAGVhemilrlpdgydtrIGEGGA---------RLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 160 GQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGwVDTVTILDaDGSVAAHG 239
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLR-DGRVQAFG 548
|
...
gi 1080238652 240 APE 242
Cdd:COG4618 549 PRD 551
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-217 |
7.37e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 28 RHADGRWAPDMV-DLSFDF--GTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgtERPVDGDrVTFVGQ 104
Cdd:PRK11629 14 RYQEGSVQTDVLhNVSFSIgeGEMMAIVGSSGSGKSTLLHLLGGL---------------------DTPTSGD-VIFNGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 105 DPSTQVLTLRV----------------------VDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQR 162
Cdd:PRK11629 72 PMSKLSSAAKAelrnqklgfiyqfhhllpdftaLENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 163 QRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
39-245 |
7.45e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPShipiDhAGFVHIVDADGTERPVDGdR----VTFVGQDPStqV---L 111
Cdd:COG1137 22 VSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKP----D-SGRIFLDGEDITHLPMHK-RarlgIGYLPQEAS--IfrkL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TlrVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD--- 188
Cdd:COG1137 94 T--VEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpia 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 189 -EDGRRSlfaaIRDLRAPGRVILLIEHDLRpfdgwvDTVTILD-----ADGSVAAHGAPEGIA 245
Cdd:COG1137 172 vADIQKI----IRHLKERGIGVLITDHNVR------ETLGICDrayiiSEGKVLAEGTPEEIL 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
284-501 |
7.64e-13 |
|
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: 68.71 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGAnFRIDGASARRVPD---AFASWAF 358
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGllPVKSGS-IRLDGEDITKLPPherARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QnPEHQ--FTRATVAAEIDSALAGTDPHGPLGADELRK----LREALCPRALDpvspfvLSGGQKRRLGIFLAVAANRRL 432
Cdd:TIGR03410 80 V-PQGReiFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpvLKEMLGRRGGD------LSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 433 LLLDEPLAHLdSPSsrIVLD---ALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPAS 501
Cdd:TIGR03410 153 LLLDEPTEGI-QPS--IIKDigrVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
283-506 |
8.90e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.48 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGasaRRVPDAFAS 355
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI------TVDG---EDLTDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 WA---------FQNPeHQFTRATVAAEIdsALAGTDPHGpLGADELRKLREALcpraLDPV--------SPFVLSGGQKR 418
Cdd:COG1126 72 INklrrkvgmvFQQF-NLFPHLTVLENV--TLAPIKVKK-MSKAEAEERAMEL----LERVgladkadaYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 419 RLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
....*...
gi 1080238652 499 PASPESSR 506
Cdd:COG1126 224 FENPQHER 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-242 |
1.06e-12 |
|
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: 68.57 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 17 PARLRVSGAGVRHaDGRWAPDMVDLsfdfgTIN-----AITGPVGCGKTSLAHLIAGLIPshipidhagfvhivdadgte 91
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISW-----TVKpgehwAILGPNGAGKSTLLSLITGDLP-------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 92 rPVDGDRVTFVGQDP-STQVLTLR----VVDDvSMALEFSLVEAG--IVA------------------KQSAEALSELGL 146
Cdd:COG1119 55 -PTYGNDVRLFGERRgGEDVWELRkrigLVSP-ALQLRFPRDETVldVVLsgffdsiglyreptdeqrERARELLELLGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 147 SELAEKdPWA-LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVD 224
Cdd:COG1119 133 AHLADR-PFGtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGIT 211
|
250
....*....|....*...
gi 1080238652 225 TVTILDaDGSVAAHGAPE 242
Cdd:COG1119 212 HVLLLK-DGRVVAAGPKE 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
39-215 |
1.06e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.89 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDhaGFVHIVDADGTERPVDGDRVTFVGQDPstqVL--TLRVV 116
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAS--GEVLLNGRRLTALPAEQRRIGILFQDD---LLfpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEFSLVEAgivAKQS--AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:COG4136 95 ENLAFALPPTIGRA---QRRArvEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180
....*....|....*....|....*
gi 1080238652 195 L----FAAIRDLRAPgrvILLIEHD 215
Cdd:COG4136 172 FrefvFEQIRQRGIP---ALLVTHD 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-467 |
1.20e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.03 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDAF----ASWAFQNPE--HQFTRA 368
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESwrkhLSWVGQNPQlpHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVA--------AEIDSALAGTD-----PHGPLGADELRKLREALcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:PRK11174 442 NVLlgnpdasdEQLQQALENAWvseflPLLPQGLDTPIGDQAAG------------LSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190
....*....|....*....|....*....|..
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAGGTVVFT 467
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRRQTTLMVT 541
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
282-516 |
1.28e-12 |
|
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: 70.87 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGE----RILDGADLTLERGEIHALVGANGAGKS-TLLAVL----------SGQMK-AGAN-FRIDGA 344
Cdd:COG4172 5 PLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpdpaahpSGSILfDGQDlLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 345 SARRVPDAFASWAFQ------NPEHqftraTVAAEIDSALAgtdPHGPLGADELRK-----LREALCPRALDPVS--PFV 411
Cdd:COG4172 85 ELRRIRGNRIAMIFQepmtslNPLH-----TIGKQIAEVLR---LHRGLSGAAARAralelLERVGIPDPERRLDayPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 412 LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGT-VVFTCHDRRVARTWADRASIVAEGKVA 490
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMaLLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 1080238652 491 WSGPAADLPASP-----------ESSRRDRPLPAAGA 516
Cdd:COG4172 237 EQGPTAELFAAPqhpytrkllaaEPRGDPRPVPPDAP 273
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
283-444 |
1.37e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.57 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA------NFRIDGASARR----VPDA 352
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHgsitldGKPVEGPGAERgvvfQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 FASWafqnpehQFTRATVAAEIDsaLAGTDphgplgadelRKLREALCPRALDPVS--------PFVLSGGQKRRLGIFL 424
Cdd:PRK11248 81 LLPW-------RNVQDNVAFGLQ--LAGVE----------KMQRLEIAHQMLKKVGlegaekryIWQLSGGQRQRVGIAR 141
|
170 180
....*....|....*....|
gi 1080238652 425 AVAANRRLLLLDEPLAHLDS 444
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDA 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-216 |
1.37e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSHIPIDHAGFvHIVDADGTERPVDGDRVTFVGQDPSTqV 110
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGH-DITRLKNREVPFLRRQIGMIFQDHHL-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180
....*....|....*....|....*.
gi 1080238652 191 GRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
297-452 |
1.52e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.57 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVPD----AFASWAFQNPehqftratva 371
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdSGSILIDGKDVTKLPEykraKYIGRVFQDP---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 aeidsaLAGTDPH-------------------GP-LGADELRKLREALCPRAL-------DPVSpfVLSGGQKRRLGIFL 424
Cdd:COG1101 90 ------MMGTAPSmtieenlalayrrgkrrglRRgLTKKRRELFRELLATLGLglenrldTKVG--LLSGGQRQALSLLM 161
|
170 180
....*....|....*....|....*...
gi 1080238652 425 AVAANRRLLLLDEPLAHLDSPSSRIVLD 452
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLE 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
284-489 |
1.57e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGAsarrvpdAFASWAFQNPEH 363
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT-------APLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 QFTRATV---AAEIDSAlaGTDPHGPLGADELRKLRE-ALCPRALDpvSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPL 439
Cdd:PRK11247 86 MFQDARLlpwKKVIDNV--GLGLKGQWRDAALQALAAvGLADRANE--WPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 440 AHLDSpSSRIVLDALAE--YAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:PRK11247 162 GALDA-LTRIEMQDLIEslWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
290-502 |
1.99e-12 |
|
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: 68.93 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTL-LAVL---------SGQMK-AGAN-FRIDGASARRVPDAFASWA 357
Cdd:COG0444 12 PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILgllpppgitSGEILfDGEDlLKLSEKELRKIRGREIQMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNPehqFT----RATVAAEIDSALAGtdpHGPLGADELR-KLREALcpRAL---DPVS-----PFVLSGGQKRRLGIFL 424
Cdd:COG0444 92 FQDP---MTslnpVMTVGDQIAEPLRI---HGGLSKAEAReRAIELL--ERVglpDPERrldryPHELSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 425 AVAANRRLLLLDEPLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
299-499 |
2.05e-12 |
|
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: 67.49 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGAnFRIDGASARRV-PDAFAswAFQNPE---HQFTRATVAA 372
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlaQPTSGG-VILEGKQITEPgPDRMV--VFQNYSllpWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSALagtdPHGPLGADE--------LRKLREALCPRaldpvsPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDS 444
Cdd:TIGR01184 78 AVDRVL----PDLSKSERRaiveehiaLVGLTEAADKR------PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 445 PSSRIVLDALAEYAG-AGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLP 499
Cdd:TIGR01184 148 LTRGNLQEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVP 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
299-493 |
2.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.19 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLlavlSGQMKA-----GANFRIDGASARRVPDAF-----ASWAFQNPEHQFTrA 368
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTI----AKHMNAllipsEGKVYVDGLDTSDEENLWdirnkAGMVFQNPDNQIV-A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAAEiDSALagtdphGP--LG--ADELRKLREalcpRALDPV--------SPFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:PRK13633 101 TIVEE-DVAF------GPenLGipPEEIRERVD----ESLKKVgmyeyrrhAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 437 EPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTwADRASIVAEGKVAWSG 493
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
296-470 |
2.16e-12 |
|
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: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 296 ERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKaganfridgasarrvpDAFASWAFQNPEHQFTRatVAAEID 375
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK----------------GTPVAGCVDVPDNQFGR--EASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 376 SALAGTDPHGPLGADELRKLREALCPRAldpvSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALA 455
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLSDAVLWLR----RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*..
gi 1080238652 456 EYAGAGGT--VVFTCHD 470
Cdd:COG2401 181 KLARRAGItlVVATHHY 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
295-469 |
2.25e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERIL-DGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFAS---WAfqnpEHQftrat 369
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAgEVLWQGEPIRRQRDEYHQdllYL----GHQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 vaAEIDSALAGTDP-------HGPLGADELRKLREA--LCPRALDPVSpfVLSGGQKRRLGifLA--VAANRRLLLLDEP 438
Cdd:PRK13538 83 --PGIKTELTALENlrfyqrlHGPGDDEALWEALAQvgLAGFEDVPVR--QLSAGQQRRVA--LArlWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|.
gi 1080238652 439 LAHLDSPSSRIVLDALAEYAGAGGTVVFTCH 469
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-216 |
2.75e-12 |
|
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: 67.11 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSHIPIDHAGfvHIVDADGTERPVdgdrvtfVGQDPST-QVLTLRvv 116
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEG--KQITEPGPDRMV-------VFQNYSLlPWLTVR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEFSLVEAGIVAKQSA--EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|...
gi 1080238652 195 LFAAIRDLRAPGRV-ILLIEHDL 216
Cdd:TIGR01184 153 LQEELMQIWEEHRVtVLMVTHDV 175
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
289-505 |
2.97e-12 |
|
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: 67.33 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 289 THVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMK-AGANFR-IDGASARRVpdafASWAFQ 359
Cdd:cd03295 7 TKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptSGEIFiDGEDIReQDPVELRRK----IGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 NPeHQFTRATVAAEIdsalaGTDPH--GPLGADELRKLREALCPRALDPVS-----PFVLSGGQKRRLGIFLAVAANRRL 432
Cdd:cd03295 83 QI-GLFPHMTVEENI-----ALVPKllKWPKEKIRERADELLALVGLDPAEfadryPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 433 LLLDEPLAHLDSpssrIVLDALAE-----YAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESS 505
Cdd:cd03295 157 LLMDEPFGALDP----ITRDQLQEefkrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
40-202 |
3.16e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLipshipiDH--AGFVHIVDADGTERPVDGDRVTFVGQDPSTqVLTLRV 115
Cdd:PRK10851 20 DISLDIpsGQMVALLGPSGSGKTTLLRIIAGL-------EHqtSGHIRFHGTDVSRLHARDRKVGFVFQHYAL-FRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDDVSMALEF----SLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:PRK10851 92 FDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170
....*....|.
gi 1080238652 192 RRSLFAAIRDL 202
Cdd:PRK10851 172 RKELRRWLRQL 182
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
299-489 |
3.30e-12 |
|
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: 66.46 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDA----------------FASW----A 357
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSgSVLLDGTDIRQLDPAdlrrnigyvpqdvtlfYGTLrdniT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNPEHQFTRATVAAEIDSALAGTDPHgPLGADelRKLREalcpraldpvSPFVLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:cd03245 100 LGAPLADDERILRAAELAGVTDFVNKH-PNGLD--LQIGE----------RGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 438 PLAHLDSPSSRIVLDALAEYAGaGGTVVFTCHdRRVARTWADRASIVAEGKV 489
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLG-DKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
284-501 |
3.54e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 68.56 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRIDG-------ASARRVpdafa 354
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSG-EILIGGrdvtdlpPKDRNI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 SWAFQNP---EHQftraTVAAEIDSAL--AGTDPhgplgaDEL-RKLREALcpRALDpVSPFV------LSGGQKRRLGI 422
Cdd:COG3839 78 AMVFQSYalyPHM----TVYENIAFPLklRKVPK------AEIdRRVREAA--ELLG-LEDLLdrkpkqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 423 FLAVAANRRLLLLDEPLAHLDsPSSRIVLDA-LAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL-- 498
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLD-AKLRVEMRAeIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELyd 223
|
....
gi 1080238652 499 -PAS 501
Cdd:COG3839 224 rPAN 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
39-216 |
4.93e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.70 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSHIPIdHAGFVHIvdadGTERPVDGDR---------VTFVGQdpST 108
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeQPEAGTI-RVGDITI----DTARSLSQQKglirqlrqhVGFVFQ--NF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVLTLRVVddvsmaLEfSLVEAGIVAK----QSAEA-----LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMI 179
Cdd:PRK11264 95 NLFPHRTV------LE-NIIEGPVIVKgepkEEATArarelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1080238652 180 FDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
295-493 |
5.48e-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: 70.04 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVPDAFASWAFQNPEHQ--FTRATVA 371
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTVLVGGKDIETNLDAVRQSLGMCPQHNilFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 AEI--DSALAGTDphgplgADELRKLREALCP----------RALDpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPL 439
Cdd:TIGR01257 1022 EHIlfYAQLKGRS------WEEAQLEMEAMLEdtglhhkrneEAQD------LSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 440 AHLDSPSSRIVLDALAEYAgAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
282-498 |
6.05e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAG---ANFRIDGA--SARRVPDAfasw 356
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyeGEIIFEGEelQASNIRDT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 afqnpE-------HQ----FTRATVAAEIdsaLAGTD--PHGPLGADE--------LRKLREALCPRAldPVSPfvLSGG 415
Cdd:PRK13549 80 -----EragiaiiHQelalVKELSVLENI---FLGNEitPGGIMDYDAmylraqklLAQLKLDINPAT--PVGN--LGLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 416 QKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPA 495
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPA 227
|
...
gi 1080238652 496 ADL 498
Cdd:PRK13549 228 AGM 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
284-514 |
6.72e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLS------------------------GQMKAGANF 339
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpsegsivvngqtinlvrdkdGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 340 RIDGASAR--RVPDAFASWAFQnpehqftraTVAAEIDSAlagtdPHGPLGADELRKLREALcpRALDPVS--------- 408
Cdd:PRK10619 86 QLRLLRTRltMVFQHFNLWSHM---------TVLENVMEA-----PIQVLGLSKQEARERAV--KYLAKVGideraqgky 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 409 PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGK 488
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
250 260
....*....|....*....|....*.
gi 1080238652 489 VAWSGPAADLPASPESSRRDRPLPAA 514
Cdd:PRK10619 230 IEEEGAPEQLFGNPQSPRLQQFLKGS 255
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
282-475 |
8.56e-12 |
|
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: 65.53 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTH--VARGGER--ILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRIDGAS---------- 345
Cdd:COG4181 7 PIIELRGLTktVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGldRPTSG-TVRLAGQDlfaldedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 346 ---ARRVpdafaSWAFQNpehqFTR-ATVAAEIDSALagtdphgPLgadELRKLREA--LCPRALDPVS--------PFV 411
Cdd:COG4181 86 rlrARHV-----GFVFQS----FQLlPTLTALENVML-------PL---ELAGRRDAraRARALLERVGlghrldhyPAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 412 LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDAL-AEYAGAGGTVVFTCHDRRVAR 475
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVTHDPALAA 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
35-241 |
9.60e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSH----------IPidhAGFVHIVDADGTERpvdgdRVTFVGQ 104
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivgdyaIP---ANLKKIKEVKRLRK-----EIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 105 DPSTQVLTLRVVDDVSmaleFSLVEAGI----VAKQSAEALSELGL-SELAEKDPWALSGGQRQRMAIAGAVARAPEVMI 179
Cdd:PRK13645 98 FPEYQLFQETIEKDIA----FGPVNLGEnkqeAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 180 FDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAP 241
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMH-EGKVISIGSP 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
298-498 |
9.99e-12 |
|
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: 65.33 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDG--------ASARR----VP-------- 350
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSI------LIDGqdirevtlDSLRRaigvVPqdtvlfnd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 351 DAFASWAFQNP---EHQFTRATVAAEIDsalagtdphgplgaDELRKLREA----LCPRALDpvspfvLSGGQKRRLGIF 423
Cdd:cd03253 90 TIGYNIRYGRPdatDEEVIEAAKAAQIH--------------DKIMRFPDGydtiVGERGLK------LSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 424 LAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEyAGAGGTVVFTCHDRRVARTwADRASIVAEGKVAWSGPAADL 498
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-216 |
1.09e-11 |
|
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: 63.99 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 16 APARLRVSGAGVRHADGrwapdmvDLSFDF--GTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgteRP 93
Cdd:cd03215 1 GEPVLEVRGLSVKGAVR-------DVSFEVraGEIVGIAGLVGNGQTELAEALFGL----------------------RP 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 94 VDGDRVTFVGQDpstqvLTLRVVDDvSMALEFSLV-----EAGIVAKQSAEalSELGLSELaekdpwaLSGGQRQRMAIA 168
Cdd:cd03215 52 PASGEITLDGKP-----VTRRSPRD-AIRAGIAYVpedrkREGLVLDLSVA--ENIALSSL-------LSGGNQQKVVLA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1080238652 169 GAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:cd03215 117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSEL 164
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
305-497 |
1.10e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 305 TLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGAS---------ARR-------VPDAFASWAFQNPE-HQFTR 367
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPleawsaaelARHraylsqqQTPPFAMPVFQYLTlHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAeidsalagtdphgplGADELRKLREAL-----CPRaldPVSPfvLSGG--QKRRL-GIFLAVA----ANRRLLLL 435
Cdd:PRK03695 98 TRTEA---------------VASALNEVAEALglddkLGR---SVNQ--LSGGewQRVRLaAVVLQVWpdinPAGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 436 DEPLAHLDSpSSRIVLDAL-AEYAGAGGTVVFTCHD-RRVARTwADRASIVAEGKVAWSGPAAD 497
Cdd:PRK03695 158 DEPMNSLDV-AQQAALDRLlSELCQQGIAVVMSSHDlNHTLRH-ADRVWLLKQGKLLASGRRDE 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
297-498 |
1.11e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASAR--------RVPDAFASWAFQNPEHQFTR 367
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlHVPTQGSVRVDDTLITstsknkdiKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAEIdsalagtdPHGP----LGADELRKL-REALCPRALDP----VSPFVLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:PRK13649 101 ETVLKDV--------AFGPqnfgVSQEEAEALaREKLALVGISEslfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 439 LAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
157-242 |
1.39e-11 |
|
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: 64.94 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD---- 232
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS---------TIVNADkiiv 207
|
90
....*....|...
gi 1080238652 233 ---GSVAAHGAPE 242
Cdd:cd03253 208 lkdGRIVERGTHE 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
144-229 |
1.44e-11 |
|
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: 65.47 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 144 LGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWV 223
Cdd:cd03236 127 LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLS 206
|
....*.
gi 1080238652 224 DTVTIL 229
Cdd:cd03236 207 DYIHCL 212
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
134-217 |
1.50e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 65.21 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 134 AKQSAEALSE-LGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLI 212
Cdd:COG4598 131 AIERAEALLAkVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVV 210
|
....*
gi 1080238652 213 EHDLR 217
Cdd:COG4598 211 THEMG 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
125-490 |
1.51e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 125 FSLVEAGIVAKQSAEALSELGLselaEKDPWA----LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIR 200
Cdd:PRK11288 109 GGIVNRRLLNYEAREQLEHLGV----DIDPDTplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 201 DLRAPGRVILLIEHDLRPFDGWVDTVTILdADGS-VAAHGAPEGIAVKGIAtsAAPAGAPDASTPGTGAPDRPDLESEAD 279
Cdd:PRK11288 185 ELRAEGRVILYVSHRMEEIFALCDAITVF-KDGRyVATFDDMAQVDRDQLV--QAMVGREIGDIYGYRPRPLGEVRLRLD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 280 AVPllaltgthvargGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGAnFRIDGA--SARRVPDAFAS 355
Cdd:PRK11288 262 GLK------------GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGatRRTAGQ-VYLDGKpiDIRSPRDAIRA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 WAFQNPEHQ-----FTRATVAAEID-SALAGTDPHGPL-----GADELRKLREALCPRALDPVSPFV-LSGG--QKRRLG 421
Cdd:PRK11288 329 GIMLCPEDRkaegiIPVHSVADNINiSARRHHLRAGCLinnrwEAENADRFIRSLNIKTPSREQLIMnLSGGnqQKAILG 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 422 IFLavAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVA 490
Cdd:PRK11288 409 RWL--SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
50-242 |
1.57e-11 |
|
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: 67.97 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGLIPshiPIdhAGFVHIVDADGTE-RPVD-GDRVTFVGQDPSTQVLTLR--------VVDDV 119
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQ---PT--EGSVLLDGVDIRQiDPADlRRNIGYVPQDPRLFYGTLRdnialgapYADDE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 120 SM--ALEFSLVEAgiVAKQSAEAL----SELGLSelaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:TIGR03375 570 EIlrAAELAGVTE--FVRRHPDGLdmqiGERGRS---------LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEE 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 194 SLFAAIRDLRApGRVILLIEH-----DLrpfdgwVDTVTILDaDGSVAAHGAPE 242
Cdd:TIGR03375 639 RFKDRLKRWLA-GKTLVLVTHrtsllDL------VDRIIVMD-NGRIVADGPKD 684
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
41-244 |
1.67e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.98 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDFGTINAITGPVGCGKTSLAHLIAGLIP---SHIPIDHAGFVHIVDADgtERPVDGDRVTFVGQDPSTqVLTLRVVD 117
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEptrGQVLIDGVDIAKISDAE--LREVRRKKIAMVFQSFAL-MPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 118 DVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFA 197
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1080238652 198 AIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGI 244
Cdd:PRK10070 206 ELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQ-NGEVVQVGTPDEI 252
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
40-218 |
1.86e-11 |
|
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: 64.60 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHIPIdhAGFVHIvdaDGTERPVD--GDRVTFVGQDpSTQVLTLRV 115
Cdd:cd03234 25 DVSLHVesGQVMAILGSSGSGKTTLLDAISGRVEGGGTT--SGQILF---NGQPRKPDqfQKCVAYVRQD-DILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDDVSMALEFSLVE--AGIVAKQSAE--ALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:cd03234 99 RETLTYTAILRLPRksSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180
....*....|....*....|....*..
gi 1080238652 192 RRSLFAAIRDLRAPGRVILLIEHDLRP 218
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQPRS 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
299-493 |
1.90e-11 |
|
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: 64.66 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMkaganfRIDGASAR---RVPdafasWAfQNPEH--QFT-----RA 368
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL------QPTSGEVRvagLVP-----WK-RRKKFlrRIGvvfgqKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAAEI---DS-----ALAGTDPHGplGADELRKLREAL-CPRALD-PVSPfvLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:cd03267 105 QLWWDLpviDSfyllaAIYDLPPAR--FKKRLDELSELLdLEELLDtPVRQ--LSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 439 LAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
283-512 |
1.92e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANfrIDGASARRVPDA-- 352
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPdhgeilfdGEN--IPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 353 -----FASWAFqnpehqFTRATVAAEIDSALAgtdPHGPLGADELR-----KLrEALCPRALDPVSPFVLSGGQKRRLGI 422
Cdd:PRK11831 85 rmsmlFQSGAL------FTDMNVFDNVAYPLR---EHTQLPAPLLHstvmmKL-EAVGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 423 FLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGA-GGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPAS 501
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
250
....*....|....*...
gi 1080238652 502 PESSRR-------DRPLP 512
Cdd:PRK11831 235 PDPRVRqfldgiaDGPVP 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
39-257 |
1.93e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSHIPIDHAGfVHIVDADGTERPVDGDRVTFVGQDPSTQV---LTLR 114
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRG-EPLAKLNRAQRKAFRRDIQMVFQDSISAVnprKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDVSMALEFSLVEAGIVAKqSAEALSELGLS-ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:PRK10419 110 EIIREPLRHLLSLDKAERLAR-ASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 194 SLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILDADGSVaahgapEGIAVKGIATSAAPAG 257
Cdd:PRK10419 189 GVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV------ETQPVGDKLTFSSPAG 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
39-244 |
1.97e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.72 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDGTE-RPVDGD----RVTFVGQDPSTqVLTL 113
Cdd:COG4604 20 VSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLV---DGLDvATTPSRelakRLAILRQENHI-NSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDdvsmalefsLVEAG---------------IVAkqsaEALSELGLSELAEK--DpwALSGGQRQRMAIAGAVARAPE 176
Cdd:COG4604 91 TVRE---------LVAFGrfpyskgrltaedreIID----EAIAYLDLEDLADRylD--ELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGI 244
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAM-KDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
299-503 |
2.00e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANF-RIDGA--SARRVPDAF--ASWAFQNPEHQFTRATVAae 373
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKvKIDGEllTAENVWNLRrkIGMVFQNPDNQFVGATVE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 iDSALAGTDPHGPLGADELRKLREALCP-RALD--PVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIV 450
Cdd:PRK13642 101 -DDVAFGMENQGIPREEMIKRVDEALLAvNMLDfkTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 451 LDALAEYAGAGG-TVVFTCHDRRVARTwADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:PRK13642 180 MRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
39-244 |
2.11e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSHIPIDHAG-FVHIV-DADGTERPVDGD-------RVTFVGQDPST 108
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLeKPSEGSIVVNGqTINLVrDKDGQLKVADKNqlrllrtRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVLtLRVVDDVSMALEFSLVEAGIVAKQSAEA-LSELGLSELAE-KDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAH 186
Cdd:PRK10619 104 WSH-MTVLENVMEAPIQVLGLSKQEARERAVKyLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 187 VDEDGRRSLFAAIRDLRAPGRVILLIEHDLRpFDGWVDTVTILDADGSVAAHGAPEGI 244
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAEEGKTMVVVTHEMG-FARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-506 |
2.30e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 292 ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--------AGANF-RIDGASARrvpdAF---ASWAFQ 359
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpsqgnvswRGEPLaKLNRAQRK----AFrrdIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 NPEHQFT-RATVAAEIDSA---LAGTDPhgplgADELRKLREALCPRALDPVS----PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:PRK10419 97 DSISAVNpRKTVREIIREPlrhLLSLDK-----AERLARASEMLRAVDLDDSVldkrPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTV-VFTCHDRRVARTWADRASIVAEGKV----------AWSGPA----- 495
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIvetqpvgdklTFSSPAgrvlq 251
|
250
....*....|..
gi 1080238652 496 -ADLPASPESSR 506
Cdd:PRK10419 252 nAVLPAFPVRRR 263
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
299-493 |
2.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM--KAGA-NFRIDGASARRVPDAFASWA------------------ 357
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpDTGTiEWIFKDEKNKKKTKEKEKVLeklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 --------FQNPEHQFTRATVAAEIdsaLAGTDPHGPLGADELRKLREALCPRALD----PVSPFVLSGGQKRRLGIFLA 425
Cdd:PRK13651 103 irrrvgvvFQFAEYQLFEQTIEKDI---IFGPVSMGVSKEEAKKRAAKYIELVGLDesylQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
40-206 |
2.36e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGL-IPShipidhAGFVHIVdadgterpvdGDRVTFVGQDPSTQVLTLRvv 116
Cdd:COG4161 20 DINLECpsGETLVLLGPSGAGKSSLLRVLNLLeTPD------SGQLNIA----------GHQFDFSQKPSEKAIRLLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEF-----------SLVEAGI-VAKQSAEA--------LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPE 176
Cdd:COG4161 82 QKVGMVFQQynlwphltvmeNLIEAPCkVLGLSKEQarekamklLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDLRAPG 206
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTG 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
294-504 |
2.57e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.88 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDG-------ASARRVPDAFASWAFqnpehqF 365
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlEHQTSGHIRFHGtdvsrlhARDRKVGFVFQHYAL------F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TRATVAAEIDSALAGTDPHGPLGADELRK----LREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAH 441
Cdd:PRK10851 87 RHMTVFDNIAFGLTVLPRRERPNAAAIKAkvtqLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 442 LDSPSS---RIVLDALAEYAGAggTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:PRK10851 167 LDAQVRkelRRWLRQLHEELKF--TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-241 |
2.58e-11 |
|
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: 64.35 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDFGTIN-----AITGPVGCGKTSLAHLIAGLIpshipidhagfvhivDADGTERPVDGDRVTFVGQ--DPSTQVlTL 113
Cdd:cd03237 15 LEVEGGSISeseviGILGPNGIGKTTFIKMLAGVL---------------KPDEGDIEIELDTVSYKPQyiKADYEG-TV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RvvddvsmALEFSLVE-AGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGR 192
Cdd:cd03237 79 R-------DLLSSITKdFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 193 RSLFAAIRdlrapgRVIL-------LIEHDLRPFDGWVDTVTILDADGSVAAHGAP 241
Cdd:cd03237 152 LMASKVIR------RFAEnnektafVVEHDIIMIDYLADRLIVFEGEPSVNGVANP 201
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
127-206 |
2.87e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.27 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 127 LVEAGI----VAKQSA-----EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFA 197
Cdd:PRK11124 103 LIEAPCrvlgLSKDQAlaraeKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS 182
|
....*....
gi 1080238652 198 AIRDLRAPG 206
Cdd:PRK11124 183 IIRELAETG 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
30-216 |
2.95e-11 |
|
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: 64.04 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 30 ADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPS---HIPIDHAGFVhIVDADGTERpvdgdRVTFVGQDp 106
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPengRVLVDGHDLA-LADPAWLRR-----QVGVVLQE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 107 sTQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEA---LSEL--GLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFD 181
Cdd:cd03252 85 -NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAhdfISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1080238652 182 EPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDL 216
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA-GRTVIIIAHRL 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
32-232 |
3.35e-11 |
|
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: 63.78 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPS--HIPIDHagfvhiVDADGTERPVDGDRVTFVGQDPSt 108
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQkgQILIDG------IDIRDISRKSLRSMIGVVLQDTF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 qVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSEL-----GLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:cd03254 88 -LFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 184 AAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLS---------TIKNAD 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
296-493 |
3.53e-11 |
|
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: 63.83 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 296 ERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFR----IDGASARR--VPDAFA--------------- 354
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSgqilFNGQPRKPdqFQKCVAyvrqddillpgltvr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 -SWAF----QNPEHQ--FTRATVAAEIDSALAGtdpHGPLGADELRKLrealcpraldpvspfvlSGGQKRRLGIFLAVA 427
Cdd:cd03234 100 eTLTYtailRLPRKSsdAIRKKRVEDVLLRDLA---LTRIGGNLVKGI-----------------SGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 428 ANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRR--VARTWaDRASIVAEGKVAWSG 493
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdLFRLF-DRILLLSSGEIVYSG 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
289-493 |
4.58e-11 |
|
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: 63.32 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 289 THVARGGER-ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGAnFRIDGasarRVPDAFASWAFQNPE--- 362
Cdd:cd03220 27 GRKGEVGEFwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdSGT-VTVRG----RVSSLLGLGGGFNPEltg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 ----------HQFTRATVAAEIDSALAGTDphgpLGADELRKLREalcpraldpvspfvLSGGQKRRLGIFLAVAANRRL 432
Cdd:cd03220 102 reniylngrlLGLSRKEIDEKIDEIIEFSE----LGDFIDLPVKT--------------YSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
296-493 |
4.81e-11 |
|
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: 62.33 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 296 ERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVPDAFASW-AFQNPE-HQFtratvaa 372
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPqQGEITLDGVPVSDLEKALSSLiSVLNQRpYLF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 eidsalAGTdphgplgadelrkLREALCPRaldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLD 452
Cdd:cd03247 88 ------DTT-------------LRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 453 ALAEYAgAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSG 493
Cdd:cd03247 140 LIFEVL-KDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
298-489 |
5.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.98 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGA--SARRVPDA--FASWAFQNPEHQFTRATVaa 372
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESgQIIIDGDllTEENVWDIrhKIGMVFQNPDNQFVGATV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSALaGTDPHGpLGADELR-KLREALcprALDPVSPFV------LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDsP 445
Cdd:PRK13650 100 EDDVAF-GLENKG-IPHEEMKeRVNEAL---ELVGMQDFKereparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD-P 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 446 SSRIVL-----DALAEYagaGGTVVFTCHD-RRVArtWADRASIVAEGKV 489
Cdd:PRK13650 174 EGRLELiktikGIRDDY---QMTVISITHDlDEVA--LSDRVLVMKNGQV 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
40-216 |
6.29e-11 |
|
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: 64.30 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHIP----IDHAGfVHIVDADGTE-RPVDGDRVTFVGQDPSTqVL- 111
Cdd:COG0444 23 GVSFDVrrGETLGLVGESGSGKSTLARAILGLLPPPGItsgeILFDG-EDLLKLSEKElRKIRGREIQMIFQDPMT-SLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 -TLRVVDDVSMALEFSLVEAGIVAKQSA-EALSELGLS---ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP--A 184
Cdd:COG0444 101 pVMTVGDQIAEPLRIHGGLSKAEARERAiELLERVGLPdpeRRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPttA 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1080238652 185 AHVdedgrrSLFAAI----RDLRA-PGRVILLIEHDL 216
Cdd:COG0444 181 LDV------TIQAQIlnllKDLQReLGLAILFITHDL 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
40-216 |
6.51e-11 |
|
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: 62.87 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVhIVDadgtERPVDG-------DRVTFVGQDPstQV 110
Cdd:cd03248 32 DVSFTLhpGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQV-LLD----GKPISQyehkylhSKVSLVGQEP--VL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVVDDVSMALEFSLVEAGIVAKQSAEALS-----ELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:cd03248 100 FARSLQDNIAYGLQSCSFECVKEAAQKAHAHSfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190
....*....|....*....|....*....|.
gi 1080238652 186 HVDEDGRRSLFAAIRDLRApGRVILLIEHDL 216
Cdd:cd03248 180 ALDAESEQQVQQALYDWPE-RRTVLVIAHRL 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
39-215 |
6.78e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSHIPIdHAGFVHIVDADgterpvDGDRVTFvgQDpsTQVLTL-RVV 116
Cdd:PRK11247 31 LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGEL-LAGTAPLAEAR------EDTRLMF--QD--ARLLPWkKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEfslveaGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLF 196
Cdd:PRK11247 100 DNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180
....*....|....*....|
gi 1080238652 197 AAIRDL-RAPGRVILLIEHD 215
Cdd:PRK11247 174 DLIESLwQQHGFTVLLVTHD 193
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
157-331 |
6.86e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIehdLRPFD---GWVDTVTILdADG 233
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV---LNRFDeipDFVQFAGVL-ADC 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 234 SVAAHGAPEGIAVKG-IATSAAPAGAPDASTPGTGAPD-RPDLeseADAVPLLALTGTHVARGGERILDGADLTLERGEI 311
Cdd:PRK10938 212 TLAETGEREEILQQAlVAQLAHSEQLEGVQLPEPDEPSaRHAL---PANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEH 288
|
170 180
....*....|....*....|
gi 1080238652 312 HALVGANGAGKSTLLAVLSG 331
Cdd:PRK10938 289 WQIVGPNGAGKSTLLSLITG 308
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
294-503 |
7.20e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKST-------LLAVLSGQMkaganfRIDGASARRVPdafaswafqnpEHQ-- 364
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSGRI------FLDGEDITHLP-----------MHKra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 -------------FTRATVAAEIDSALagtdphgplgadELRKL----REALCPRALD-----PV--SP-FVLSGGQKRR 419
Cdd:COG1137 77 rlgigylpqeasiFRKLTVEDNILAVL------------ELRKLskkeREERLEELLEefgitHLrkSKaYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 420 LGIFLAVAANRRLLLLDEPLAHLDsPSS-----RIVLDaLAEyAGAGgtVVFTCHDRRVARTWADRASIVAEGKVAWSGP 494
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVD-PIAvadiqKIIRH-LKE-RGIG--VLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
....*....
gi 1080238652 495 AADLPASPE 503
Cdd:COG1137 220 PEEILNNPL 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
298-519 |
7.45e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN-FRIDGAS-ARRVPDAFAS-------WAFQNpEHQFTRA 368
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtYRVAGQDvATLDADALAQlrrehfgFIFQR-YHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVA--AEIDSALAGTDPHGPLGADELRKLREALCPRAldPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPS 446
Cdd:PRK10535 102 TAAqnVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV--EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 447 SRIVLDALAEYAGAGGTVVFTCHDRRVARTwADRASIVAEGKVawsgpAADLPASPESSRRDRPLPAAGARTS 519
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI-----VRNPPAQEKVNVAGGTEPVVNTASG 246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-244 |
7.62e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.09 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHAdGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIpshipidhagfvhivdadgteRPVDGDrV 99
Cdd:PRK11300 6 LSVSGLMMRFG-GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY---------------------KPTGGT-I 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 TFVGQD----PSTQVLTLRVV---DDVSMALEFSLVEAGIVAK---------------------------QSAEALSELG 145
Cdd:PRK11300 63 LLRGQHieglPGHQIARMGVVrtfQHVRLFREMTVIENLLVAQhqqlktglfsgllktpafrraesealdRAATWLERVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 146 LSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRV-ILLIEHDLRPFDGWVD 224
Cdd:PRK11300 143 LLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHDMKLVMGISD 222
|
250 260
....*....|....*....|
gi 1080238652 225 TVTILDaDGSVAAHGAPEGI 244
Cdd:PRK11300 223 RIYVVN-QGTPLANGTPEEI 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
291-445 |
8.08e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.11 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 291 VARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANF---------RIDG--ASARRVpdafaSWAFQ 359
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAsgevllngrRLTAlpAEQRRI-----GILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 360 NPeHQFTRATVAAEIDSALAGTDPhgplgadelRKLREALCPRALDPVS--------PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:COG4136 84 DD-LLFPHLSVGENLAFALPPTIG---------RAQRRARVEQALEEAGlagfadrdPATLSGGQRARVALLRALLAEPR 153
|
170
....*....|....
gi 1080238652 432 LLLLDEPLAHLDSP 445
Cdd:COG4136 154 ALLLDEPFSKLDAA 167
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
290-498 |
8.26e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDAFASWAFQNPEHQFTRAT 369
Cdd:PRK13547 8 HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDSALA---------GTDPHGPLGADELRKLRE-ALCPRALDPVSPFV------LSGGQKRRLGIFLAVA------ 427
Cdd:PRK13547 88 LPQAAQPAFAfsareivllGRYPHARRAGALTHRDGEiAWQALALAGATALVgrdvttLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 428 ---ANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFT-CHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-252 |
9.43e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDFGTIN-----AITGPVGCGKTSLAHLIAGLIpshipidhagfvhivDADGTErpVDGD-RVTFVGQdpstqvltlR 114
Cdd:COG1245 356 LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVL---------------KPDEGE--VDEDlKISYKPQ---------Y 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDVSMALEFSLVEAGIVAKQS----AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:COG1245 410 ISPDYDGTVEEFLRSANTDDFGSsyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 191 GRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDadgsvaahGAPegiAVKGIATS 252
Cdd:COG1245 490 QRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMVFE--------GEP---GVHGHASG 541
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
292-506 |
1.03e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 292 ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVP---DAFASWAFQNPEHQ-FT 366
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAgNIIIDDEDISLLPlhaRARRGIGYLPQEASiFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEIDSALA-GTDPHGPLGADELRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDsP 445
Cdd:PRK10895 92 RLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD-P 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 446 SSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPESSR 506
Cdd:PRK10895 171 ISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
294-471 |
1.06e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.20 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGANF----RIDGASARRVP--DAFASWAFQNpEHQF 365
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGieRPSAGKIWfsghDITRLKNREVPflRRQIGMIFQD-HHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TRATVAAEIDSALAGTDPHGplgaDELRKLREAlcprALDPVS--------PFVLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASG----DDIRRRVSA----ALDKVGlldkaknfPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 438 PLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDR 471
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
299-502 |
1.08e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.60 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTL---LAVL----SGQMK-AGAN-FRIDGASARRVP--------DAFASWafqNP 361
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLgrlLLRLeeptSGEILfDGQDiTGLSGRELRPLRrrmqmvfqDPYASL---NP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 ehqftRATVAAEIDSALagtDPHGPLGADELR-KLREALCPRALDPVS----PFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:COG4608 111 -----RMTVGDIIAEPL---RIHGLASKAERReRVAELLELVGLRPEHadryPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 437 EPLAHLD-SPSSRIV---LDALAEYagaGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:COG4608 183 EPVSALDvSIQAQVLnllEDLQDEL---GLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
39-239 |
1.09e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.94 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgtERPVDGdRVTFVGQD----PSTQVLTLR 114
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKSTLIRCINLL---------------------ERPTSG-SVLVDGVDltalSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 -----------------VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEV 177
Cdd:COG1135 82 rkigmifqhfnllssrtVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDLRAP-GRVILLIEHDLRpfdgwV-----DTVTILDaDGSVAAHG 239
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMD-----VvrricDRVAVLE-NGRIVEQG 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
40-242 |
1.12e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.80 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDADGTERPVDG--DRVTFVGQDPstqVL--- 111
Cdd:COG1132 358 DISLTIppGETVALVGPSGSGKSTLVNLLLRFYdPT------SGRILIDGVDIRDLTLESlrRQIGVVPQDT---FLfsg 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TLRvvDDVSMA-LEFSLVEagIVakqsaEALSELGLSELAEKDPW-----------ALSGGQRQRMAIAGAVARAPEVMI 179
Cdd:COG1132 429 TIR--ENIRYGrPDATDEE--VE-----EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 180 FDEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD-------GSVAAHGAPE 242
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLS---------TIRNADrilvlddGRIVEQGTHE 559
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
295-498 |
1.17e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLS-GQMKAGANFRIDG---------ASARRVpdAFASWAFQNPEHQ 364
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGrHQPPSEGEILLDAqpleswsskAFARKV--AYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 FTRATVAAeidsalaGTDP-HGPLG---ADELRKLREALCPRALDPVSPFV---LSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:PRK10575 101 TVRELVAI-------GRYPwHGALGrfgAADREKVEEAISLVGLKPLAHRLvdsLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 438 PLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
295-498 |
1.20e-10 |
|
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: 62.25 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGASARRV--PDAFASWAFQNPEHQF 365
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRI------LIDGHDVRDYtlASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TRATVAAEIDSALAGTDPHGPLGADELRKLREALC--PRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:cd03251 88 FNDTVAENIAYGRPGATREEVEEAARAANAHEFIMelPEGYDTVigeRGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 441 HLDSPSSRIVLDALaEYAGAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:cd03251 168 ALDTESERLVQAAL-ERLMKNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
284-471 |
1.21e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARG--GERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKAGANFRIdGASARRVPDAFA 354
Cdd:PRK15064 318 NALEVENLTKGfdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvgelepdSGTVKWSENANI-GYYAQDHAYDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 S------WAFQ--NPEH--QFTRATVaaeidsalagtdphGPL--GADELRKlrealcpraldpvSPFVLSGGQKRRLgI 422
Cdd:PRK15064 397 NdltlfdWMSQwrQEGDdeQAVRGTL--------------GRLlfSQDDIKK-------------SVKVLSGGEKGRM-L 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 423 FLAVAANR-RLLLLDEPLAHLDSPSSRIVLDALAEYAgagGTVVFTCHDR 471
Cdd:PRK15064 449 FGKLMMQKpNVLVMDEPTNHMDMESIESLNMALEKYE---GTLIFVSHDR 495
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
39-242 |
1.71e-10 |
|
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: 61.68 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDgDRVTF-VGQDPSTQVL--TLRV 115
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR-----SGSIRFDGRDITGLPPH-ERARAgIGYVPEGRRIfpELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 116 VDDVSMALEFSLVEAGivaKQSAEALSEL--GLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAH-----VD 188
Cdd:cd03224 93 EENLLLGAYARRRAKR---KARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGlapkiVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 189 EdgrrsLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPE 242
Cdd:cd03224 170 E-----IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLER-GRVVLEGTAA 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
302-517 |
1.92e-10 |
|
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: 63.20 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 302 ADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDG-------------ASARRVpdafaSWAFQNPeHQFTR 367
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGlERPDSGRIRLGGevlqdsargiflpPHRRRI-----GYVFQEA-RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAEIDSALAGTDP-HGPLGADELRKLR--EALCPRaldpvSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDS 444
Cdd:COG4148 92 LSVRGNLLYGRKRAPRaERRISFDEVVELLgiGHLLDR-----RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 445 PSSRIVLDALAEYAGAGGT-VVFTCHDRR-VARTwADRASIVAEGKVAWSGPAADLPASPESsrrdrpLPAAGAR 517
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpILYVSHSLDeVARL-ADHVVLLEQGRVVASGPLAEVLSRPDL------LPLAGGE 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-503 |
1.96e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVR-HADGRWAPDMVDLSFDF--GTINAITGPVGCGKT----SLAHLI---AGLIPSHIPIDHAGFVHIVD--- 86
Cdd:PRK10261 13 LAVENLNIAfMQEQQKIAAVRNLSFSLqrGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRQVIElse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 87 -ADGTERPVDGDRVTFVGQDPSTQ---VLTL--RVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGG 160
Cdd:PRK10261 93 qSAAQMRHVRGADMAMIFQEPMTSlnpVFTVgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 161 QRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRV-ILLIEHDLRPFDGWVDTVTILdADGSVAAHG 239
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVM-YQGEAVETG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 240 APEGI--AVKGIATSAAPAGAPD-ASTPGTGAPDRPDLESEADAVPLLALTGTHVARGGERILDGADLT----------- 305
Cdd:PRK10261 252 SVEQIfhAPQHPYTRALLAAVPQlGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLVtrfplrsglln 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 306 ---------------LERGEIHALVGANGAGKST-------LLAVLSGQMKAGANfRIDGASARRVPDAF--ASWAFQNP 361
Cdd:PRK10261 332 rvtrevhavekvsfdLWPGETLSLVGESGSGKSTtgrallrLVESQGGEIIFNGQ-RIDTLSPGKLQALRrdIQFIFQDP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EHQF-TRATVAAEIDSALAgtdPHGPLGADELRKLREALCPR-ALDPVS----PFVLSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:PRK10261 411 YASLdPRQTVGDSIMEPLR---VHGLLPGKAAAARVAWLLERvGLLPEHawryPHEFSGGQRQRICIARALALNPKVIIA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 436 DEPLAHLD-SPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:PRK10261 488 DEAVSALDvSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-232 |
2.34e-10 |
|
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: 61.48 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIagliPSHIPIDhAGFVHIVDADGTERPVDGDR--VTFVGQDpsT 108
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYDVD-SGRILIDGHDVRDYTLASLRrqIGLVSQD--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALS-----ELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:cd03251 86 FLFNDTVAENIAYGRPGATREEVEEAARAANAHEfimelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 184 AAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:cd03251 166 TSALDTESERLVQAALERLMK-NRTTFVIAHRLS---------TIENAD 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-239 |
2.46e-10 |
|
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: 63.97 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 16 APARLRVSGAGVRH-ADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGlipshipidhagFVHIvdaDGTERPV 94
Cdd:TIGR02203 327 ARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPR------------FYEP---DSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 DGD------------RVTFVGQDpstqvLTL---RVVDDVSMALEFSLVEAGIV-AKQSAEALS-----ELGLSELAEKD 153
Cdd:TIGR02203 392 DGHdladytlaslrrQVALVSQD-----VVLfndTIANNIAYGRTEQADRAEIErALAAAYAQDfvdklPLGLDTPIGEN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 154 PWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRaPGRVILLIEHDLRPFDGwVDTVTILDaDG 233
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMD-DG 543
|
....*.
gi 1080238652 234 SVAAHG 239
Cdd:TIGR02203 544 RIVERG 549
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
294-331 |
2.61e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 2.61e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG 331
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
48-242 |
2.87e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 48 INAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFVhIVDAD-GTERPVDGDRVTFVGQD----PSTQVL-TLRVVDDVS 120
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTrPQKGRIVLNGRV-LFDAEkGICLPPEKRRIGYVFQDarlfPHYKVRgNLRYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 121 MALEF-SLVEAgivakqsaealseLGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAI 199
Cdd:PRK11144 105 MVAQFdKIVAL-------------LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 200 ----RDLRAPgrvILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPE 242
Cdd:PRK11144 172 erlaREINIP---ILYVSHSLDEILRLADRVVVLE-QGKVKAFGPLE 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
282-489 |
2.93e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGAN---FR----IDGASARRVPDAFA 354
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGrivFDgkdiTDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 SWafqnPEHQ--FTRATVaaEIDSALAGTDPHGPLGADELRKLREaLCPRALDPVS--PFVLSGGQKRRLGIFLAVAANR 430
Cdd:PRK11614 84 IV----PEGRrvFSRMTV--EENLAMGGFFAERDQFQERIKWVYE-LFPRLHERRIqrAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 431 RLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
290-444 |
3.32e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.42 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGasaRRV--PDAFASWAFQNpEHQFT 366
Cdd:COG4525 14 PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApSSGEITLDG---VPVtgPGADRGVVFQK-DALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEIDSAL--AGTDPHGplgadelrklREALCPRALDPV--------SPFVLSGGQKRRLGIFLAVAANRRLLLLD 436
Cdd:COG4525 90 WLNVLDNVAFGLrlRGVPKAE----------RRARAEELLALVgladfarrRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
....*...
gi 1080238652 437 EPLAHLDS 444
Cdd:COG4525 160 EPFGALDA 167
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
302-502 |
3.47e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.74 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 302 ADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVPDA--------FASWAFQNpehqFTRATVAA 372
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAelrevrrkKIAMVFQS----FALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSALAGTDPHGPLGADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRI 449
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAhsyPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 450 VLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-474 |
3.51e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.42 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGlipshipIDHagfvhivDADGTERPVDGDRVTFVGQ----DPSTQVL--- 111
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-------VDK-------DFNGEARPQPGIKVGYLPQepqlDPTKTVRenv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 ---------TLRVVDDVSMAleFSLVEA---GIVAKQSA--EALSELGLSELAEK----------DPW-----ALSGGQR 162
Cdd:TIGR03719 90 eegvaeikdALDRFNEISAK--YAEPDAdfdKLAAEQAElqEIIDAADAWDLDSQleiamdalrcPPWdadvtKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 163 QRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLraPGRVILlIEHDlRPFdgwVDTVT--ILDADgsvaaHGa 240
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVA-VTHD-RYF---LDNVAgwILELD-----RG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 241 pEGIAVKGIATS-------------------------------AAPAGAPDASTPGTGAPDrpDLESEADA--------- 280
Cdd:TIGR03719 235 -RGIPWEGNYSSwleqkqkrleqeekeesarqktlkrelewvrQSPKGRQAKSKARLARYE--ELLSQEFQkrnetaeiy 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 281 VPL------LALTGTHVARG-GERIL-DGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGAnFRIdGASARrvp 350
Cdd:TIGR03719 312 IPPgprlgdKVIEAENLTKAfGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdSGT-IEI-GETVK--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 351 dafASWAFQNPEHQFTRATVAAEIDSalagtdphgplGADELRKLREALCPRALdpVSPF------------VLSGGQKR 418
Cdd:TIGR03719 387 ---LAYVDQSRDALDPNKTVWEEISG-----------GLDIIKLGKREIPSRAY--VGRFnfkgsdqqkkvgQLSGGERN 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 419 RLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAgagGTVVFTCHDR----RVA 474
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA---GCAVVISHDRwfldRIA 507
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
283-498 |
3.71e-10 |
|
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: 62.92 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAG---ANFRIDGAS--ARRVPDA-FASW 356
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwdGEIYWSGSPlkASNIRDTeRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 AFQNPEHQFTRA-TVAAEIDSALAGTDPHGPLGADELRKLREALCPR---ALDPVSPFV--LSGGQKRRLGIFLAVAANR 430
Cdd:TIGR02633 81 VIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRElqlDADNVTRPVgdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 431 RLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
272-502 |
4.03e-10 |
|
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: 61.12 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 272 PDLESEADAVPLLALTGTHVArggeriLDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGANFrIDGASARRV 349
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVG------VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEptSGKVL-IDGQDIAAM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 350 PDA--------FASWAFQN----PeHQFTRATVAAEIDsaLAGTDphgplgadelRKLREALCPRALDPVS--------P 409
Cdd:cd03294 92 SRKelrelrrkKISMVFQSfallP-HRTVLENVAFGLE--VQGVP----------RAEREERAAEALELVGlegwehkyP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 410 FVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDsPSSRI-----VLDALAEYagaGGTVVFTCHDRRVARTWADRASIV 484
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRRemqdeLLRLQAEL---QKTIVFITHDLDEALRLGDRIAIM 234
|
250
....*....|....*...
gi 1080238652 485 AEGKVAWSGPAADLPASP 502
Cdd:cd03294 235 KDGRLVQVGTPEEILTNP 252
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
288-498 |
4.34e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.66 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 288 GTHVArggeriLDGADLTLERGEIHALVGANGAGKSTL----LAVL---SGQmkaganFRIDGAsarrvpdAFASWAFQN 360
Cdd:COG4152 12 GDKTA------VDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGILapdSGE------VLWDGE-------PLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 361 ----PE--------------------HQFTRATVAAEIDSALagtDPHGpLGADELRKLREalcpraldpvspfvLSGGQ 416
Cdd:COG4152 73 igylPEerglypkmkvgeqlvylarlKGLSKAEAKRRADEWL---ERLG-LGDRANKKVEE--------------LSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 417 KRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAA 496
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
..
gi 1080238652 497 DL 498
Cdd:COG4152 215 EI 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-189 |
4.80e-10 |
|
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: 60.77 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PS--HIPIDHAgfvHIVDADGTERPVDG 96
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSsgSILLEGT---DITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 DRVTFVGQDPSTqVLTLRVVDDVSMA-LEFSLVEAGIVA------KQSA-EALSELGLSELAEKDPWALSGGQRQRMAIA 168
Cdd:TIGR02315 79 RRIGMIFQHYNL-IERLTVLENVLHGrLGYKPTWRSLLGrfseedKERAlSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180
....*....|....*....|.
gi 1080238652 169 GAVARAPEVMIFDEPAAHVDE 189
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDP 178
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-214 |
5.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGrwapdmVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFVHIVDADGTERPVD--GD 97
Cdd:PRK14247 9 LKVSFGQVEVLDG------VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 98 RVTFVGQDPSTqVLTLRVVDDVSMALEFSLVeagivAKQSAEaLSELGLSELAEKDPW------------ALSGGQRQRM 165
Cdd:PRK14247 83 RVQMVFQIPNP-IPNLSIFENVALGLKLNRL-----VKSKKE-LQERVRWALEKAQLWdevkdrldapagKLSGGQQQRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 166 AIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPgRVILLIEH 214
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
46-244 |
5.28e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 46 GTINAITGPVGCGKTSLAHLIAGLI-PSHipidhaGFVHIvDADGTERPVDGD---RVTFVGQDPSTQvltlrvvDDVSM 121
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMtPAH------GHVWL-DGEHIQHYASKEvarRIGLLAQNATTP-------GDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 122 AlefSLVEAGIVAKQS-------------AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:PRK10253 99 Q---ELVARGRYPHQPlftrwrkedeeavTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 189 EDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGI 244
Cdd:PRK10253 176 ISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIAL-REGKIVAQGAPKEI 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
51-204 |
6.62e-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: 58.70 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 51 ITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHivdadgteRPVDGDrVTFVGQDPSTQVLTLRvvddvsmalefslvea 130
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWG-----SGRIG--------MPEGED-LLFLPQRPYLPLGTLR---------------- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 131 givakqsaEALSElglselaekdPW--ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRA 204
Cdd:cd03223 82 --------EQLIY----------PWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI 139
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
294-489 |
6.88e-10 |
|
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: 60.04 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVPDAFASWAFQNPEHQ-FTRATVA 371
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPdSGKILLNGKDITNLPPEKRDISYVPQNYAlFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 AEIDSALAGTDPHGPLGADELRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVL 451
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080238652 452 DALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03299 170 EELKKIRKEFGvTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-241 |
7.82e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVhIVDADGTERPVDGDRVTfVGQDPSTQVL 111
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-----SGTV-LVGGKDIETNLDAVRQS-LGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 tlrvVDDVSMAlEFSLVEAGIVAKQSAEA-------LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPA 184
Cdd:TIGR01257 1015 ----FHHLTVA-EHILFYAQLKGRSWEEAqlemeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 185 AHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAP 241
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAII-SQGRLYCSGTP 1144
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
294-469 |
9.65e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.25 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPdaFASW--AFQN-PEHQFTratv 370
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVP--LQKWrkAFGViPQKVFI---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 aaeidsaLAGT-----DPHGPLGADELRKLREAL--------CPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLL 434
Cdd:cd03289 89 -------FSGTfrknlDPYGKWSDEEIWKVAEEVglksvieqFPGQLDFVlvdGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1080238652 435 LDEPLAHLDSPSSRIVLDALaEYAGAGGTVVFTCH 469
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTL-KQAFADCTVILSEH 195
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-344 |
9.84e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGL-IPSH--IPIDHAGFVHIVDADGTERPVDG--------DRVT--- 100
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKgtITINNINYNKLDHKLAAQLGIGIiyqelsviDELTvle 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 101 --FVGQDPSTQVLTLRVVDDVSMAlefslveagivaKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVM 178
Cdd:PRK09700 100 nlYIGRHLTKKVCGVNIIDWREMR------------VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 179 IFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDaDGSVAAHGAPEGIAVKGIATSAAPAGA 258
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMK-DGSSVCSGMVSDVSNDDIVRLMVGREL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 259 PD---ASTPGTGAPDRpDLESEADAVpllaltgthVARGGERILDgADLTLERGEIHALVGANGAGKSTLLAVLSG-QMK 334
Cdd:PRK09700 247 QNrfnAMKENVSNLAH-ETVFEVRNV---------TSRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKR 315
|
330
....*....|
gi 1080238652 335 AGANFRIDGA 344
Cdd:PRK09700 316 AGGEIRLNGK 325
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
282-508 |
1.02e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVPDAFAS----- 355
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKpTGGTILLRGQHIEGLPGHQIArmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 WAFQNPEhQFTRATVaaeIDSALAGTdpHGPLGADELRKL----------REALcPRA---LDPVS--PFV------LSG 414
Cdd:PRK11300 84 RTFQHVR-LFREMTV---IENLLVAQ--HQQLKTGLFSGLlktpafrraeSEAL-DRAatwLERVGllEHAnrqagnLAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 415 GQKRRLGIFLAVAANRRLLLLDEPLAHLDsPSSRIVLDAL-----AEYagaGGTVVFTCHDRRVARTWADRASIVAEGKv 489
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLN-PKETKELDELiaelrNEH---NVTVLLIEHDMKLVMGISDRIYVVNQGT- 231
|
250
....*....|....*....
gi 1080238652 490 awsgPAADlpASPESSRRD 508
Cdd:PRK11300 232 ----PLAN--GTPEEIRNN 244
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
282-454 |
1.04e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK---AGANFRIDGASARRV-PDAFAS-- 355
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykiLEGDILFKGESILDLePEERAHlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 --WAFQNP-------EHQFTRATVAA--------EIDsalagtdphgPLGADELrkLREALCPRALDPVspFV------- 411
Cdd:CHL00131 86 ifLAFQYPieipgvsNADFLRLAYNSkrkfqglpELD----------PLEFLEI--INEKLKLVGMDPS--FLsrnvneg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1080238652 412 LSGGQKRRLGIFlavaanrRLLLLDEPLAHLDSPSSRIVLDAL 454
Cdd:CHL00131 152 FSGGEKKRNEIL-------QMALLDSELAILDETDSGLDIDAL 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
39-202 |
1.08e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIP-SHIPIDHAGFV-HIVDADGT-ERPVDGDRVT--FVGQDPSTqVLTL 113
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgDKSAGSHIELLgRTVQREGRlARDIRKSRANtgYIFQQFNL-VNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDDVSMALEFS-------LVEAGIVAKQSA-EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:PRK09984 102 SVLENVLIGALGStpfwrtcFSWFTREQKQRAlQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170
....*....|....*..
gi 1080238652 186 HVDEDGRRSLFAAIRDL 202
Cdd:PRK09984 182 SLDPESARIVMDTLRDI 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
305-508 |
1.10e-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: 59.73 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 305 TLERGEIHALVGANGAGKSTLLAVLSGQMKAGanfriDGASARRVPDAfaSWAFQNPEHQFT---RATVAAEIDSAlaGT 381
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD-----EGDIEIELDTV--SYKPQYIKADYEgtvRDLLSSITKDF--YT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 382 DPH------GPLGADEL--RKLREalcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSpSSRI---- 449
Cdd:cd03237 92 HPYfkteiaKPLQIEQIldREVPE--------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV-EQRLmask 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 450 VLDALAEYAGAGGTVVFtcHDRRVARTWADRAsIVAEGKvawsgPAADLPASPESSRRD 508
Cdd:cd03237 157 VIRRFAENNEKTAFVVE--HDIIMIDYLADRL-IVFEGE-----PSVNGVANPPQSLRS 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
299-502 |
1.10e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMK-AGANFRIDGASARRVPDAFASWAFQNPEHQFT-RAT 369
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYyQGQDLLKADPEAQKLLRQKIQIVFQNPYGSLNpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDSALA-GTDphgpLGADELR-KLREALCPRALDPVS----PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:PRK11308 111 VGQILEEPLLiNTS----LSAAERReKALAMMAKVGLRPEHydryPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 444 SPSSRIVLDALAEYAGAGGTV-VFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
293-471 |
1.10e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA--------------------------NFRIDGASA 346
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGgsytfpgnwqlawvnqetpalpqpalEYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 347 -RRVPDAFASWAFQNPEHQFtrATVAAEIDS-------ALAGTDPHGpLGADElrklrealcPRALDPVSPFvlSGGQKR 418
Cdd:PRK10636 91 yRQLEAQLHDANERNDGHAI--ATIHGKLDAidawtirSRAASLLHG-LGFSN---------EQLERPVSDF--SGGWRM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 419 RLGIFLAVAANRRLLLLDEPLAHLDspssrivLDA-------LAEYAgagGTVVFTCHDR 471
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD-------LDAviwlekwLKSYQ---GTLILISHDR 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
299-502 |
1.16e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDG-----------ASARR----Vpdafasw 356
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRV------LVDGqdltalsekelRKARRqigmI------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 aFQnpeHqF---TRATVAAEIDSAL--AGTDphgplgADELRKLREALcpraLDPVS--------PFVLSGGQKRRLGIF 423
Cdd:PRK11153 88 -FQ---H-FnllSSRTVFDNVALPLelAGTP------KAEIKARVTEL----LELVGlsdkadryPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 424 LAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
40-239 |
1.17e-09 |
|
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: 58.72 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHIpidHAGFVHIvdaDGTERPVD--GDRVTFVGQDpsTQVL-TLR 114
Cdd:cd03213 27 NVSGKAkpGELTAIMGPSGAGKSTLLNALAGRRTGLG---VSGEVLI---NGRPLDKRsfRKIIGYVPQD--DILHpTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDdvsmALEFSLVEAGIvakqsaealselglselaekdpwalSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:cd03213 99 VRE----TLMFAAKLRGL-------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 195 LFAAIRDLRAPGRVILLIEHDLRPFD-GWVDTVTILdADGSVAAHG 239
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPSSEIfELFDKLLLL-SQGRVIYFG 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
280-449 |
1.22e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 280 AVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASAR--RVPDAFASW 356
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAgSILIDGQEMRfaSTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 357 -AFQNPE-HQFTRATVAAEIdsaLAGTDPH--GPLGADELRK-LREALCPRA--LDPVSPF-VLSGGQKRRLGIFLAVAA 428
Cdd:PRK11288 81 vAIIYQElHLVPEMTVAENL---YLGQLPHkgGIVNRRLLNYeAREQLEHLGvdIDPDTPLkYLSIGQRQMVEIAKALAR 157
|
170 180
....*....|....*....|.
gi 1080238652 429 NRRLLLLDEPLAHLDSPSSRI 449
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQ 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
298-503 |
1.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFR----IDGA--SARRVPDAF--ASWAFQNPEHQFTRAT 369
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskitVDGItlTAKTVWDIRekVGIVFQNPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAaeiDSALAGTDPHGPLGADELRKLREALCPRA-LDPVS--PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPS 446
Cdd:PRK13640 102 VG---DDVAFGLENRAVPRPEMIKIVRDVLADVGmLDYIDsePANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 447 SRIVLDALAEYAGAGG-TVVFTCHDRRVArTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:PRK13640 179 KEQILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
294-495 |
1.30e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMK-AGANFRI-------DGASARR-VPDAFASWa 357
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiAGNHFDFsktpsdkAIRELRRnVGMVFQQY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 fqnpeHQFTRATVAAEIDSAlagtdPHGPLGADELRKLREA---LCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:PRK11124 92 -----NLWPHLTVQQNLIEA-----PCRVLGLSKDQALARAeklLERLRLKPYAdrfPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPA 495
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
294-506 |
1.33e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMK-AGANFridgaSARRVPDAFASWA-------- 357
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNiAGHQF-----DFSQKPSEKAIRLlrqkvgmv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNpEHQFTRATVAAEIDSAlagtdPHGPLG---ADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRR 431
Cdd:COG4161 88 FQQ-YNLWPHLTVMENLIEA-----PCKVLGlskEQAREKAMKLLARLRLTDKAdrfPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLpASPESSR 506
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF-TQPQTEA 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
39-218 |
1.38e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipiDHAGFVHIVDADgterpvdgdrvtfVGQDPStqvltlrVV 116
Cdd:COG2401 47 RDLNLEIepGEIVLIVGASGSGKSTLLRLLAGALKGT---PVAGCVDVPDNQ-------------FGREAS-------LI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMALEFslveagivaKQSAEALSELGLSE--LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:COG2401 104 DAIGRKGDF---------KDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190
....*....|....*....|....*....|.
gi 1080238652 195 LFAAIRDL-RAPGRVILLIEH------DLRP 218
Cdd:COG2401 175 VARNLQKLaRRAGITLVVATHhydvidDLQP 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
299-494 |
1.43e-09 |
|
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: 61.42 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAF----ASWAFQNPEHQFtrATVAAE 373
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEgSVLLDGVDIRQIDPADlrrnIGYVPQDPRLFY--GTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 IDSALAGTDPHGPLGADELRKLRE--ALCPRALD-PVSP--FVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSR 448
Cdd:TIGR03375 559 IALGAPYADDEEILRAAELAGVTEfvRRHPDGLDmQIGErgRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEE 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 449 IVLDALAEYAgAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGP 494
Cdd:TIGR03375 639 RFKDRLKRWL-AGKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGP 682
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
39-214 |
1.61e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.20 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgtERPVDGdRVTFVGQD----PSTQVLTLR 114
Cdd:PRK11153 24 VSLHIPAGEIFGVIGASGAGKSTLIRCINLL---------------------ERPTSG-RVLVDGQDltalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 -----------------VVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEV 177
Cdd:PRK11153 82 rqigmifqhfnllssrtVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEH 214
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDInRELGLTIVLITH 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
289-498 |
1.69e-09 |
|
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: 61.27 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 289 THVARGGER-ILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGasarrvpDAFASWAFQN 360
Cdd:TIGR02203 337 TFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGQI------LLDG-------HDLADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 361 PEHQFtrATVAAEI---DSALAGTDPHG-PLGADELRKLREALCPRALDPVSPF-------------VLSGGQKRRLGIF 423
Cdd:TIGR02203 404 LRRQV--ALVSQDVvlfNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLplgldtpigengvLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 424 LAVAANRRLLLLDEPLAHLDSPSSRIVLDALaEYAGAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAAL-ERLMQGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
295-444 |
1.70e-09 |
|
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: 58.25 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKaganfRIDGASARRVPDAFASwafQNPEHQftRATVAAEI 374
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-----KLSGSVSVPGSIAYVS---QEPWIQ--NGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 375 dsaLAGTdphgPLGADELRKLREAlCprALDP-----------------VSpfvLSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:cd03250 87 ---LFGK----PFDEERYEKVIKA-C--ALEPdleilpdgdlteigekgIN---LSGGQKQRISLARAVYSDADIYLLDD 153
|
....*..
gi 1080238652 438 PLAHLDS 444
Cdd:cd03250 154 PLSAVDA 160
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-214 |
1.84e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFVHIVDADGTERPVDG----DRVTFVGQDPSTqVLTLR 114
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPievrREVGMVFQYPNP-FPHLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDVSMALEFS-LVEAGIVAKQSAE-ALSELGLSELAE---KD-PWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:PRK14267 102 IYDNVAIGVKLNgLVKSKKELDERVEwALKKAALWDEVKdrlNDyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
170 180
....*....|....*....|....*.
gi 1080238652 189 EDGRRSLFAAIRDLRAPgRVILLIEH 214
Cdd:PRK14267 182 PVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
298-504 |
1.90e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLS-------GQMKAGAN--------FRIDGASARRVpdafASWAFQNPe 362
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKvlyfgkdiFQIDAIKLRKE----VGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 HQFTRATVAAEIDSALAGtdpHGPLGADELRKLREAlCPRAL-----------DPVSPfvLSGGQKRRLGIFLAVAANRR 431
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKS---HGIKEKREIKKIVEE-CLRKVglwkevydrlnSPASQ--LSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTwADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARV-ADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
37-244 |
2.11e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 37 DMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPShipidhagfvhivdaDGTERPVDGDRVTFVGQD----------- 105
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP---------------DHGEILFDGENIPAMSRSrlytvrkrmsm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 106 --PSTQVLT-LRVVDDVSMAL-EFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFD 181
Cdd:PRK11831 89 lfQSGALFTdMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 182 EPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGI 244
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIV-ADKKIVAHGSAQAL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
290-503 |
2.25e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGA---SARRV--PDAFA-------SWA 357
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEvrlFGRNIysPDVDPievrrevGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNPeHQFTRATVaaeIDSALAGTDPHGPL-GADELRKLRE-ALCPRAL-DPVS------PFVLSGGQKRRLGIFLAVAA 428
Cdd:PRK14267 91 FQYP-NPFPHLTI---YDNVAIGVKLNGLVkSKKELDERVEwALKKAALwDEVKdrlndyPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 429 NRRLLLLDEPLAHLDSPSSRIVLDALAEYAgAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELK-KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
56-183 |
2.31e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.75 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 56 GCGKTSLAHLIAGLI-PSHIPIDHAGfVHIVDADGTE----RPvdgdRVTFVGQDPSTQV---LTlrvvddVSMALEFSL 127
Cdd:COG4608 54 GCGKSTLGRLLLRLEePTSGEILFDG-QDITGLSGRElrplRR----RMQMVFQDPYASLnprMT------VGDIIAEPL 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 128 VEAGIVAKQS-----AEALSELGLS-ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:COG4608 123 RIHGLASKAErrervAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
284-503 |
2.88e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.39 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 284 LALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDAF---------- 353
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 ASWAFQNPE-----HQFTRATVAAEIDSALAGTdphgplgADELRKLREALCPRAL-DPVSPFV------LSGGQKRRLG 421
Cdd:PRK14247 84 VQMVFQIPNpipnlSIFENVALGLKLNRLVKSK-------KELQERVRWALEKAQLwDEVKDRLdapagkLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 422 IFLAVAANRRLLLLDEPLAHLDsPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPAS 501
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLD-PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
..
gi 1080238652 502 PE 503
Cdd:PRK14247 236 PR 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
278-493 |
3.28e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 278 ADAVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDAFAS- 355
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgEVHYRMRDGQLRDLYALSe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 ----------WAF--QNPEhQFTRATVAA--EIDSALAGtdphgpLGADELRKLREA---------LCPRALDPVsPFVL 412
Cdd:PRK11701 81 aerrrllrteWGFvhQHPR-DGLRMQVSAggNIGERLMA------VGARHYGDIRATagdwlerveIDAARIDDL-PTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 413 SGGQKRRLGIFLAVAANRRLLLLDEPLAHLD-SPSSRIvLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVA 490
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvSVQARL-LDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
...
gi 1080238652 491 WSG 493
Cdd:PRK11701 232 ESG 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
33-241 |
3.70e-09 |
|
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: 57.42 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 33 RWAPDM------VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPS---HIPIDHAGFVHIVDADGTERpvdgdrVTFVG 103
Cdd:cd03369 15 RYAPDLppvlknVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeegKIEIDGIDISTIPLEDLRSS------LTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 104 QDPSTQVLTLRVVDDVSMalEFSLVEAgivakQSAEALSELGLSelaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:cd03369 89 QDPTLFSGTIRSNLDPFD--EYSDEEI-----YGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 184 AAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRPFDGWvDTVTILDAdGSVAAHGAP 241
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDA-GEVKEYDHP 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
39-216 |
3.77e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 57.83 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAG-LIPS--HIPIDHAGfvHIVD-ADGTERPVDGDR---VTFVGQdpstqvl 111
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDsgSILVRHDG--GWVDlAQASPREILALRrrtIGYVSQ------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TLRVVDDVSmALEF---SLVEAGI---VAKQSAEA-LSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEP 183
Cdd:COG4778 101 FLRVIPRVS-ALDVvaePLLERGVdreEARARARElLARLNLPErLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190
....*....|....*....|....*....|...
gi 1080238652 184 AAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:COG4778 180 TASLDAANRAVVVELIEEAKARGTAIIGIFHDE 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
39-227 |
5.34e-09 |
|
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: 55.53 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIpshipIDHAGFVHivdadgterpvdgdrvtfvgqdpstqvltlrvvdd 118
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL-----EPDEGIVT----------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 VSMALEFSLVEagivakQsaealselglselaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAA 198
Cdd:cd03221 59 WGSTVKIGYFE------Q--------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180
....*....|....*....|....*....
gi 1080238652 199 IRDLRapgRVILLIEHDlRPFdgwVDTVT 227
Cdd:cd03221 113 LKEYP---GTVILVSHD-RYF---LDQVA 134
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
234-535 |
6.13e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 234 SVAAHGAPEGiavKGIATSAAPAGAPDASTPGTGAPDRPDLESEAdavpllaltgthvarggerILDGADLTLERGEIHA 313
Cdd:PTZ00243 633 SASRHIVEGG---TGGGHEATPTSERSAKTPKMKTDDFFELEPKV-------------------LLRDVSVSVPRGKLTV 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 314 LVGANGAGKSTLLAVLSGQmkaganFRIdgaSARRVPdAFASWAFQNPEHQFTRATVAAEI------DSA-LAGTDPHGP 386
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQ------FEI---SEGRVW-AERSIAYVPQQAWIMNATVRGNIlffdeeDAArLADAVRVSQ 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 387 LGADeLRKLREALCPRALDpvSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVF 466
Cdd:PTZ00243 761 LEAD-LAQLGGGLETEIGE--KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL 837
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 467 TCHD-RRVARtwADRASIVAEGKVAWSGPAADLPASPESsrrdrplpaAGARTSLDESPGTSESAARRRA 535
Cdd:PTZ00243 838 ATHQvHVVPR--ADYVVALGDGRVEFSGSSADFMRTSLY---------ATLAAELKENKDSKEGDADAEV 896
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
35-230 |
6.22e-09 |
|
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: 57.34 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFVhivdaDGTERPVDGDRVTFV-GQdpSTQVL- 111
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAGLV-----PWKRRKKFLRRIGVVfGQ--KTQLWw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TLRVVDDVSMALEFSLVEAGiVAKQSAEALSE-LGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDED 190
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPA-RFKKRLDELSElLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 191 GRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILD 230
Cdd:cd03267 188 AQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
48-216 |
6.36e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 48 INAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFVHIVDADGTERPVDGDR----VTFVgqDPSTQVLTLRVVDDVSMAL 123
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRlrrqVSMV--HPKPNLFPMSVYDNVAYGV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 124 EF----------SLVEAGIvakQSAEALSELglSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:PRK14258 113 KIvgwrpkleidDIVESAL---KDADLWDEI--KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
170 180
....*....|....*....|....
gi 1080238652 194 SLFAAIRDLRAPGRV-ILLIEHDL 216
Cdd:PRK14258 188 KVESLIQSLRLRSELtMVIVSHNL 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
294-469 |
7.22e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVpdAFASW--AFQN-PEHQFTratv 370
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSV--TLQTWrkAFGViPQKVFI---- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 aaeidsaLAGT-----DPHGPLGADELRKLREAL--------CPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLL 434
Cdd:TIGR01271 1304 -------FSGTfrknlDPYEQWSDEEIWKVAEEVglksvieqFPDKLDFVlvdGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190
....*....|....*....|....*....|....*
gi 1080238652 435 LDEPLAHLDSPSSRIVLDALaEYAGAGGTVVFTCH 469
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTL-KQSFSNCTVILSEH 1410
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-242 |
7.68e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 22 VSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGlipshipidhagFVHIVDAD------GTERPVD 95
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMG------------FVRLASGKisilgqPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 96 GDRVTFVGQ----DPSTQVLtlrvVDDVSMALEFSlvEAGIVAKQSA-------EALSELGLSELAEKDPWALSGGQRQR 164
Cdd:PRK15056 77 KNLVAYVPQseevDWSFPVL----VEDVVMMGRYG--HMGWLRRAKKrdrqivtAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 165 MAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVD-TVTIldaDGSVAAHGAPE 242
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDyTVMV---KGTVLASGPTE 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
51-216 |
8.63e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 51 ITGPVGCGKTSLAHLIAGLI-PshipidhagfvhivdadgTERPVDGD-RVTFVGQdpstqvltlRVVDDVSMALEFSLv 128
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLkP------------------DEGEVDPElKISYKPQ---------YIKPDYDGTVEDLL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 129 eAGIVAKQSA-----EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL- 202
Cdd:PRK13409 422 -RSITDDLGSsyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIa 500
|
170
....*....|....
gi 1080238652 203 RAPGRVILLIEHDL 216
Cdd:PRK13409 501 EEREATALVVDHDI 514
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-239 |
8.65e-09 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 58.99 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 33 RWAPD----MVDLSFDF--GTINAITGPVGCGKTSLAHLIAGL-IPSH--IPIDHAGfVHIVDADGTERpvdgdRVTFVG 103
Cdd:TIGR01846 464 RYAPDspevLSNLNLDIkpGEFIGIVGPSGSGKSTLTKLLQRLyTPQHgqVLVDGVD-LAIADPAWLRR-----QMGVVL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 104 QDpstQVLTLR-VVDDVSMALEFSLVEAGIVAKQSAEAL---SELGL---SELAEKDPwALSGGQRQRMAIAGAVARAPE 176
Cdd:TIGR01846 538 QE---NVLFSRsIRDNIALCNPGAPFEHVIHAAKLAGAHdfiSELPQgynTEVGEKGA-NLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRPFDGwVDTVTILDaDGSVAAHG 239
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLE-KGQIAESG 673
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
286-496 |
9.90e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.92 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 286 LTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGA-------SARR----VPDaf 353
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgKITVLGVpvpararLARArigvVPQ-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 aswaFQNPEHQFTratvaaeIDSALAGTDPHGPLGADELrklrEALCPRALD----------PVSPfvLSGGQKRRLGIF 423
Cdd:PRK13536 122 ----FDNLDLEFT-------VRENLLVFGRYFGMSTREI----EAVIPSLLEfarleskadaRVSD--LSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 424 LAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEG-KVAWSGPAA 496
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
39-183 |
1.00e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGL--IPShipidhaGFVHIvdadgterpvDGDRVTFVgqDPSTQvltlrvv 116
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLerITS-------GEIWI----------GGRVVNEL--EPADR------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 dDVSM-----AL----------EFSLVEAGI----VAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEV 177
Cdd:PRK11650 77 -DIAMvfqnyALyphmsvrenmAYGLKIRGMpkaeIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
....*.
gi 1080238652 178 MIFDEP 183
Cdd:PRK11650 156 FLFDEP 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-293 |
1.34e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 27 VRHADGRWAPDM------VDLSFDFGTINAITGPVGCGKTSLahlIAGLIPSHIPIDhaGFVHIVDAdgterpvdgdrVT 100
Cdd:TIGR00957 639 VHNATFTWARDLpptlngITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDKVE--GHVHMKGS-----------VA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 101 FVGQDPSTQVLTLRVVDDVSMALEFSLVEAGIvakQSAEALSELGL------SELAEKDPwALSGGQRQRMAIAGAVARA 174
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKALNEKYYQQVL---EACALLPDLEIlpsgdrTEIGEKGV-NLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 175 PEVMIFDEPAAHVDEDGRRSLFAAIRDLRA--PGRVILLIEHDLRpFDGWVDTVTILdADGSVAAHGA-PEGIAVKG--- 248
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGIS-YLPQVDVIIVM-SGGKISEMGSyQELLQRDGafa 856
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 249 -----IATSAAPAGAPDASTPGTGAPDRPDLESEaDAVPLLALTGTHVAR 293
Cdd:TIGR00957 857 eflrtYAPDEQQGHLEDSWTALVSGEGKEAKLIE-NGMLVTDVVGKQLQR 905
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
293-494 |
1.35e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQ----MKAGANFRIDG----ASARRVPDAFA---------- 354
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRspkgVKGSGSVLLNGmpidAKEMRAISAYVqqddlfiptl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 355 --------SWAFQNPEHQFTRATVAAeIDSALagtdphgplgaDELRkLREALCPRALDPVSPFVLSGGQKRRLGIFLAV 426
Cdd:TIGR00955 115 tvrehlmfQAHLRMPRRVTKKEKRER-VDEVL-----------QALG-LRKCANTRIGVPGRVKGLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 427 AANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHD--RRVARTWaDRASIVAEGKVAWSGP 494
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELF-DKIILMAEGRVAYLGS 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
297-469 |
1.37e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAG--------ANFR-IDGASARRVpdafaSWAFQNPEHQFTR 367
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGvitggdrlVNGRpLDSSFQRSI-----GYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAAEIDSALAGTDPHGPLGAD-----------ELRKLREALCpraldPVSPFVLSGGQKRRLGIFLAVAANRRLLL-L 435
Cdd:TIGR00956 852 TVRESLRFSAYLRQPKSVSKSEKmeyveevikllEMESYADAVV-----GVPGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCH 469
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
40-214 |
1.38e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPShipidHAGFVHIvDADGTERPVDGDRVTFVG-QDPSTQVLTlrvv 116
Cdd:PRK13539 20 GLSFTLaaGEALVLTGPNGSGKTTLLRLIAGLLPP-----AAGTIKL-DGGDIDDPDVAEACHYLGhRNAMKPALT---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 ddVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAG-AVARAPeVMIFDEPAAHVDEDGRRSL 195
Cdd:PRK13539 90 --VAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARlLVSNRP-IWILDEPTAALDAAAVALF 166
|
170
....*....|....*....
gi 1080238652 196 FAAIRDLRAPGRVILLIEH 214
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATH 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
39-242 |
1.86e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PShipidhagfvhivdaDGTERPVDGDRVTFVGQ----DPsTQVLTL 113
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPD---------------EGVIKRNGKLRIGYVPQklylDT-TLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RvvddvsmalEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:PRK09544 87 N---------RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 194 SLFAAIRDLRAP-GRVILLIEHDLRPFDGWVDTVTILdaDGSVAAHGAPE 242
Cdd:PRK09544 158 ALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL--NHHICCSGTPE 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
299-448 |
2.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.91 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA------NFRIDGASARRVPDAFASwAFQNPEHQFTRATVAA 372
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSgeifynNQAITDDNFEKLRKHIGI-VFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 373 EIDSALAGTD-PHgplgaDELRKLrealCPRALDPVS--------PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:PRK13648 104 DVAFGLENHAvPY-----DEMHRR----VSEALKQVDmleradyePNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
....*
gi 1080238652 444 sPSSR 448
Cdd:PRK13648 175 -PDAR 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
298-501 |
2.41e-08 |
|
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: 55.57 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGqMKAGANFR--IDGASARRVPDAF--ASWAFQNPEHQFTRATVAAE 373
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR-FYVPENGRvlVDGHDLALADPAWlrRQVGVVLQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 IDSALAGTDPHGPLGADELRKLREALC--PRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSR 448
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGAHDFISelPEGYDTIvgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 449 IVLDALAEYAgAGGTVVFTCHDRRVARTwADRASIVAEGKVAWSGPAADLPAS 501
Cdd:cd03252 176 AIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
294-471 |
2.52e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKaganfridgASARRVpdafaswafqnpeHQFTRATVA-- 371
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQ---------ADSGRI-------------HCGTKLEVAyf 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 ----AEID------SALA---------GTDPHgplgadELRKLREALCP--RALDPVSpfVLSGGQKRRL---GIFLAvA 427
Cdd:PRK11147 388 dqhrAELDpektvmDNLAegkqevmvnGRPRH------VLGYLQDFLFHpkRAMTPVK--ALSGGERNRLllaRLFLK-P 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080238652 428 ANrrLLLLDEPLAHLDSPSSRIVLDALAEYAgagGTVVFTCHDR 471
Cdd:PRK11147 459 SN--LLILDEPTNDLDVETLELLEELLDSYQ---GTVLLVSHDR 497
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
280-498 |
2.58e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 280 AVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVPDAFASWAF 358
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QNPEHQftRATVAAEI---DSALAGTDP-HGPLGAD-----ELRKLREALCPRALDPVSP--FV--LSGGQKRRLGIFLA 425
Cdd:PRK09700 82 IGIIYQ--ELSVIDELtvlENLYIGRHLtKKVCGVNiidwrEMRVRAAMMLLRVGLKVDLdeKVanLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
293-494 |
2.66e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.66 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARR-VPDAFASWAFQNPEHQFTRATV 370
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILGQPTRQaLQKNLVAYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAeiDSALAGTdpHGPLGADELRKLRE-ALCPRALDPVSPF--------VLSGGQKRRLGIFLAVAANRRLLLLDEPLAH 441
Cdd:PRK15056 97 VE--DVVMMGR--YGHMGWLRRAKKRDrQIVTAALARVDMVefrhrqigELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 442 LDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRaSIVAEGKVAWSGP 494
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGP 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
281-496 |
3.00e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 281 VPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGANFRIDGASARRVPDAFASWA- 357
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGltHPDAGSISLCGEPVPSRARHARQRVGv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 ---FQNPEHQFTratvaaeIDSALAGTDPHGPLGADELRKLREALCP------RALDPVSPfvLSGGQKRRLGIFLAVAA 428
Cdd:PRK13537 85 vpqFDNLDPDFT-------VRENLLVFGRYFGLSAAAARALVPPLLEfaklenKADAKVGE--LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 429 NRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEG-KVAWSGPAA 496
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHA 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
27-260 |
3.25e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 27 VRHADGRWAPDMVDLSFDFGTINAITGPVGcgktslAHLIAGLIPSHIPIDHAG-----FV-------HIVDADGTERPV 94
Cdd:NF000106 20 VKHFGEVKAVDGVDLDVREGTVLGVLGP*G------AA**RGALPAHV*GPDAGrrpwrF*twcanrrALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 -DGDRVTFVGQDPSTQVltlrvvddvSMALEFSLVEAgivAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVAR 173
Cdd:NF000106 94 r*GRRESFSGRENLYMI---------GR*LDLSRKDA---RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 174 APEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPEGIAVK--GIAT 251
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDR-GRVIADGKVDELKTKvgGRTL 240
|
....*....
gi 1080238652 252 SAAPAGAPD 260
Cdd:NF000106 241 QIRPAHAAE 249
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
298-471 |
3.56e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANFRIDGASARRVPDAFASWAFQNPEHQFtRAT 369
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPekgeilfeRQSIKKDLCTYQKQLCFVGHRSGINPYLTL-REN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDSAlagtdpHGPLGADELRKLREalCPRALD-PVSpfVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSR 448
Cdd:PRK13540 95 CLYDIHFS------PGAVGITELCRLFS--LEHLIDyPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 1080238652 449 IVLDALAEYAGAGGTVVFTCHDR 471
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQD 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
314-471 |
3.59e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 314 LVGANGAGKSTLLAVL-------SGQMKAGANFRI----------DGASARR-VPDAFA------------SWAFQNPEH 363
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMagvdkefEGEARPAPGIKVgylpqepqldPEKTVREnVEEGVAevkaaldrfneiYAAYAEPDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 QFTR-----ATVAAEIDSAlagtdphgplGADEL-RKLR---EAL-CPRALDPVSpfVLSGGQKRRlgiflaVAANRRL- 432
Cdd:PRK11819 118 DFDAlaaeqGELQEIIDAA----------DAWDLdSQLEiamDALrCPPWDAKVT--KLSGGERRR------VALCRLLl 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 433 -----LLLDEPLAHLDSPSsriVL---DALAEYAgagGTVVFTCHDR 471
Cdd:PRK11819 180 ekpdmLLLDEPTNHLDAES---VAwleQFLHDYP---GTVVAVTHDR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
282-336 |
3.63e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 3.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAG 336
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiyTRDAG 59
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
157-438 |
4.24e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGsva 236
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVI-RDG--- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 237 ahgapegiavKGIAT-SAAPAGAPDASTPGTGapdR------PDLESEADAVPLLA--LTGTHVARGGERILDGADLTLE 307
Cdd:PRK13549 220 ----------RHIGTrPAAGMTEDDIITMMVG---ReltalyPREPHTIGEVILEVrnLTAWDPVNPHIKRVDDVSFSLR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 308 RGEIHALVGANGAGKSTLLAVLSG--QMKAGANFRIDG--ASARRVPDAFASWAFQNPE--------------------- 362
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGayPGRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEdrkrdgivpvmgvgknitlaa 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 -HQFTRATV---AAEIDSALagtdphgplgaDELRKLRealcpraLDPVSPFV----LSGG--QKRRLGIFLavAANRRL 432
Cdd:PRK13549 367 lDRFTGGSRiddAAELKTIL-----------ESIQRLK-------VKTASPELaiarLSGGnqQKAVLAKCL--LLNPKI 426
|
....*.
gi 1080238652 433 LLLDEP 438
Cdd:PRK13549 427 LILDEP 432
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
298-498 |
4.69e-08 |
|
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: 54.47 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKaganfrIDGASARRV---------------PDAFAS 355
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEIL------LDGVDIRDLnlrwlrsqiglvsqePVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 WAFQN--------PEHQFTRATVAAEIDSALAGtDPHGplgadelrkLREALCPRAldpvspFVLSGGQKRRLGIFLAVA 427
Cdd:cd03249 92 TIAENirygkpdaTDEEVEEAAKKANIHDFIMS-LPDG---------YDTLVGERG------SQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 428 ANRRLLLLDEPLAHLDSPSSRIVLDALaEYAGAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
50-239 |
5.35e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.39 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGLIPshipidHAGFVHIvdaDGTE-RPVDGDR----VTFVGQDPSTQVLTLRvvDDVSMAle 124
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALLGFLP------YQGSLKI---NGIElRELDPESwrkhLSWVGQNPQLPHGTLR--DNVLLG-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 125 fslvEAGIVAKQSAEALSELGLSELAEKDPWAL-----------SGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:PRK11174 447 ----NPDASDEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 194 SLFAAIRDLRApGRVILLIEHDLRPFDGWvDTVTILDaDGSVAAHG 239
Cdd:PRK11174 523 LVMQALNAASR-RQTTLMVTHQLEDLAQW-DQIWVMQ-DGQIVQQG 565
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
294-493 |
5.38e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRvpdaFASWAFQNPEHQFTR-ATVA 371
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQH----YASKEVARRIGLLAQnATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 AEI---DSALAGTDPHGPLGAdELRKLREALCPRALDPV--------SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:PRK10253 94 GDItvqELVARGRYPHQPLFT-RWRKEDEEAVTKAMQATgithladqSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 441 HLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGyTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-188 |
6.75e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.20 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDGDRVTFVGQDpSTQVLTLRVVDDV 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-----SGSLTLNGQDHTTTPPSRRPVSMLFQE-NNLFSHLTVAQNI 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 120 SMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
41-218 |
7.75e-08 |
|
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: 53.13 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDAD-GTERPVDGDRVTFVGQDPS-TQVLTlrvv 116
Cdd:TIGR01189 19 LSFTLnaGEALQVTGPNGIGKTTLLRILAGLLRPD-----SGEVRWNGTPlAEQRDEPHENILYLGHLPGlKPELS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 ddVSMALEFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGA-VARAPeVMIFDEPAAHVDEDGRRSL 195
Cdd:TIGR01189 90 --ALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLwLSRRP-LWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|...
gi 1080238652 196 FAAIRDLRAPGRVILLIEHDLRP 218
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQDLG 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-214 |
7.81e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 53.27 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVD-ADGTERPVDGDRVTFVGQDPSTQ 109
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-----AGRVLLNGgPLDFQRDSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 110 VlTLRVVDDVSMALEFSLVEagivakQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDE 189
Cdd:cd03231 86 T-TLSVLENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*
gi 1080238652 190 DGRRSLFAAIRDLRAPGRVILLIEH 214
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
39-490 |
8.68e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPShipidhagfvhivdaDGTERPVDGDRVT-------------FVGQD 105
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP---------------DSGTLEIGGNPCArltpakahqlgiyLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 106 PSTqVLTLRVVDDVSmaleFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:PRK15439 95 PLL-FPNLSVKENIL----FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 186 HVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPEGIAVKGIATSAAPAgapdasTPG 265
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVM-RDGTIALSGKTADLSTDDIIQAITPA------ARE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 266 TGAPDRPDLeseadavpLLALTGTH-VARGGERILDGADLTLE----------RGEIHALVGANGAGKSTLLAVLSGQMK 334
Cdd:PRK15439 243 KSLSASQKL--------WLELPGNRrQQAAGAPVLTVEDLTGEgfrnislevrAGEILGLAGVVGAGRTELAETLYGLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 335 A-GANFRIDGA--SARRVPDAFASWAFQNPEHQ-----FTRATVAAEIDSALAGTDPHGPLGADE---LRKLREAL---C 400
Cdd:PRK15439 315 ArGGRIMLNGKeiNALSTAQRLARGLVYLPEDRqssglYLDAPLAWNVCALTHNRRGFWIKPAREnavLERYRRALnikF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 401 PRALDPVSpfVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADR 480
Cdd:PRK15439 395 NHAEQAAR--TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADR 472
|
490
....*....|
gi 1080238652 481 ASIVAEGKVA 490
Cdd:PRK15439 473 VLVMHQGEIS 482
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
294-504 |
9.02e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.73 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGANFrIDGASA-------RRVPDAFASWAFqnpehq 364
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKptEGQIF-IDGEDVthrsiqqRDICMVFQSYAL------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 365 FTRATVAAEIDSALAGTDphgpLGADELRK-LREALCPRALDPVSP-FV--LSGGQKRRLGIFLAVAANRRLLLLDEPLA 440
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLG----VPKEERKQrVKEALELVDLAGFEDrYVdqISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 441 HLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASPES 504
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-217 |
9.19e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRHADGrwapdmVDLSFDFGTINAITGPVGCGKTSLAhliaglipshipidhagfvhivdadgterpvdgdrv 99
Cdd:cd03238 1 LTVSGANVHNLQN------LDVSIPLNVLVVVTGVSGSGKSTLV------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 tfvgQDPSTQVLTLRVVDDVSMALEFSLVEAGivakqSAEALSELGLSELAEKDPWA-LSGGQRQRMAIAGAVARAPE-- 176
Cdd:cd03238 39 ----NEGLYASGKARLISFLPKFSRNKLIFID-----QLQFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgt 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 177 VMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLR 217
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
283-493 |
1.20e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 283 LLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK---AGANFRIDGASARRV-PDAFAS--- 355
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyevTGGTVEFKGKDLLELsPEDRAGegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 356 -WAFQNP------EHQFTRATVAAEIdSALAGTDPHGPLG-AD------ELRKLREALCPRALDpvspFVLSGGQKRRLG 421
Cdd:PRK09580 81 fMAFQYPveipgvSNQFFLQTALNAV-RSYRGQEPLDRFDfQDlmeekiALLKMPEDLLTRSVN----VGFSGGEKKRND 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 422 IFLAVAANRRLLLLDEPLAHLDSPSSRIV---LDALAEyaGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRD--GKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-215 |
1.25e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 30 ADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIpidhaGFVHIVDADGTERPVDGDR--VTFVGQDPs 107
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS-----GTLLFEGEDISTLKPEIYRqqVSYCAQTP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 108 tqVLTLRVVDDvSMALEFSLVEAGIVAKQSAEALSELGLSE-LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAH 186
Cdd:PRK10247 91 --TLFGDTVYD-NLIFPWQIRNQQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|
gi 1080238652 187 VDEDGRRSLFAAI-RDLRAPGRVILLIEHD 215
Cdd:PRK10247 168 LDESNKHNVNEIIhRYVREQNIAVLWVTHD 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
124-215 |
1.31e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 124 EFSLVEAGIVAKQ----SAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAI 199
Cdd:PRK10535 108 EVPAVYAGLERKQrllrAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL 187
|
90
....*....|....*.
gi 1080238652 200 RDLRAPGRVILLIEHD 215
Cdd:PRK10535 188 HQLRDRGHTVIIVTHD 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
313-490 |
1.32e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 313 ALVGANGAGKSTLLAVLSGQMK--AGANFR-------------IDGASARRVPDAFASWAFQNPEHQFTRATVaaeidsa 377
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQpsSGTVFRsakvrmavfsqhhVDGLDLSSNPLLYMMRCFPGVPEQKLRAHL------- 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 378 lagtdphGPLGadelrkLREALcprALDPVspFVLSGGQKRRLGiFLAVAANR-RLLLLDEPLAHLDSPSSRIVLDALAE 456
Cdd:PLN03073 612 -------GSFG------VTGNL---ALQPM--YTLSGGQKSRVA-FAKITFKKpHILLLDEPSNHLDLDAVEALIQGLVL 672
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 457 YAGAggtVVFTCHDRRVARTWADRASIVAEGKVA 490
Cdd:PLN03073 673 FQGG---VLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
298-475 |
1.49e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.90 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGASARRVPDAfASWAFQNPE----HQFTR----- 367
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTSGDVIFNGQPMSKLSSA-AKAELRNQKlgfiYQFHHllpdf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 -ATVAAEIDSALAGTDPhgplgADELRKLREALCPRALDPVS---PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:PRK11629 103 tALENVAMPLLIGKKKP-----AEINSRALEMLAAVGLEHRAnhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 444 SPSSRIVLDALAEYAGAGGT--VVFTcHDRRVAR 475
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTafLVVT-HDLQLAK 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
157-263 |
1.69e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVA 236
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM-HQGEIS 482
|
90 100
....*....|....*....|....*..
gi 1080238652 237 AHGAPEGIAVKGIATSAAPAGAPDAST 263
Cdd:PRK15439 483 GALTGAAINVDTIMRLAFGEHQAQEAS 509
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
36-196 |
1.69e-07 |
|
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: 55.30 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 36 PDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAG-LIPSHIPIDHAGfvhivdadgterpvdgdRVTFVGQDPSTQVLT 112
Cdd:TIGR01271 440 PVLKNISFKLekGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSG-----------------RISFSPQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRvvDDVSMALEFSLVEAGIVAKqsAEALSElGLSELAEKDPW-------ALSGGQRQRMAIAGAVARAPEVMIFDEPAA 185
Cdd:TIGR01271 503 IK--DNIIFGLSYDEYRYTSVIK--ACQLEE-DIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|.
gi 1080238652 186 HVDEDGRRSLF 196
Cdd:TIGR01271 578 HLDVVTEKEIF 588
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
290-474 |
1.91e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARG-GERIL-DGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIdGASARrvpdafASWAFQNPEHQFT 366
Cdd:PRK11819 329 NLSKSfGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPdSGTIKI-GETVK------LAYVDQSRDALDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 367 RATVAAEIDSalagtdphgplGADELRKLREALCPRALdpVSPF------------VLSGGQKRR--LGIFLAVAANrrL 432
Cdd:PRK11819 402 NKTVWEEISG-----------GLDIIKVGNREIPSRAY--VGRFnfkggdqqkkvgVLSGGERNRlhLAKTLKQGGN--V 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAgagGTVVFTCHDR----RVA 474
Cdd:PRK11819 467 LLLDEPTNDLDVETLRALEEALLEFP---GCAVVISHDRwfldRIA 509
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-235 |
2.11e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPG-RVILLIEHDLRPFDGWVDTVTILDADGSV 235
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
293-456 |
2.19e-07 |
|
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: 52.61 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGASARRVPdaFASW------AFQNPeHQF 365
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDIS--RKSLrsmigvVLQDT-FLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 366 TR------------ATVAAEIDSALAgtdphgpLGADEL-RKLrealcPRALDPV---SPFVLSGGQKRRLGIFLAVAAN 429
Cdd:cd03254 90 SGtimenirlgrpnATDEEVIEAAKE-------AGAHDFiMKL-----PNGYDTVlgeNGGNLSQGERQLLAIARAMLRD 157
|
170 180
....*....|....*....|....*..
gi 1080238652 430 RRLLLLDEPLAHLDSPSSRIVLDALAE 456
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEK 184
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
309-469 |
2.35e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 309 GEIHALVGANGAGKSTLLAVLSGQMKAG---ANFRIDGASARRvpDAFA---SWAFQNPEHQ-------------FTRAT 369
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyieGDIRISGFPKKQ--ETFArisGYCEQNDIHSpqvtvresliysaFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 370 VAAEIDSALAGTDPHGPLGadELRKLREALCprALDPVSPfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRI 449
Cdd:PLN03140 984 KEVSKEEKMMFVDEVMELV--ELDNLKDAIV--GLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180
....*....|....*....|
gi 1080238652 450 VLDALAEYAGAGGTVVFTCH 469
Cdd:PLN03140 1058 VMRTVRNTVDTGRTVVCTIH 1077
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
36-216 |
2.39e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 36 PDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAglipshipidhagfvHIVDADGTERPVDGDR------------VTF 101
Cdd:TIGR00958 495 PVLKGLTFTLhpGEVVALVGPSGSGKSTVAALLQ---------------NLYQPTGGQVLLDGVPlvqydhhylhrqVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 102 VGQDPstQVLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGL------SELAEKDPwALSGGQRQRMAIAGAVARAP 175
Cdd:TIGR00958 560 VGQEP--VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEfpngydTEVGEKGS-QLSGGQKQRIAIARALVRKP 636
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 176 EVMIFDEPAAHVDEDGRRSLFAairDLRAPGRVILLIEHDL 216
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRL 674
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
300-480 |
2.43e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 300 DGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--------GANFRIDGASARRVPDAFASWAFQNPEHQFT-RATV 370
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAtdgevawlGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNpRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIDSALAGTDPHgpLGADELRK------LREALCPRALDPVsPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD- 443
Cdd:PRK15079 118 GEIIAEPLRTYHPK--LSRQEVKDrvkammLKVGLLPNLINRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDv 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080238652 444 SPSSRIV--LDALAEYAGAggTVVFTCHDRRVARTWADR 480
Cdd:PRK15079 195 SIQAQVVnlLQQLQREMGL--SLIFIAHDLAVVKHISDR 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
157-216 |
2.44e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.25 E-value: 2.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDL 216
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRL 539
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
50-195 |
2.72e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.87 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGLI-PShipidhAGFVHIVDadgteRPVD-GD------RVTFVGQDPSTqvlTLRVVDDVSM 121
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIePT------SGELLIDD-----HPLHfGDysyrsqRIRMIFQDPST---SLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 122 ALEFSL-----VEAGIVAKQSAEALSELGL-SELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:PRK15112 109 ILDFPLrlntdLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-498 |
2.79e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.06 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGASArrvpdafASWAFQNPEHQFTRATV 370
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqQGEI------LLNGQPI-------ADYSEAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIDSA-------LAGtdphgPLGADElrKLREALC----------PRALD--------PvspfvLSGGQKRRLGIFLA 425
Cdd:PRK11160 422 RVHLFSAtlrdnllLAA-----PNASDE--ALIEVLQqvgleklledDKGLNawlgeggrQ-----LSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAgAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGPAADL 498
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
303-493 |
2.84e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.49 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGANFrIDGASARRVPDA-------FASWAFqnpehqFTRATVAAE 373
Cdd:PRK11000 23 NLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDITSGDLF-IGEKRMNDVPPAergvgmvFQSYAL------YPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 374 IDSA--LAGTDphgplgADELRK----LREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP-- 445
Cdd:PRK11000 96 MSFGlkLAGAK------KEEINQrvnqVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlr 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080238652 446 -SSRIVLDALAEYAGAggTVVFTCHDRRVARTWADRASIVAEGKVAWSG 493
Cdd:PRK11000 170 vQMRIEISRLHKRLGR--TMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
280-474 |
2.91e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 280 AVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGA-NFRIDGASARRVPDA-FASWA 357
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESgQIQIDGKTATRGDRSrFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 358 FQNPEHQFTRATVA-AEIDSALAGTD----PHGPLGADELRKLREALCPRaldpvspfvLSGGQKRRLGIFLAVAANRRL 432
Cdd:PRK13543 88 GHLPGLKADLSTLEnLHFLCGLHGRRakqmPGSALAIVGLAGYEDTLVRQ---------LSAGQKKRLALARLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1080238652 433 LLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVA 474
Cdd:PRK13543 159 WLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
265-489 |
2.94e-07 |
|
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: 52.09 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 265 GTGAPDrpDLESEadaVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRID 342
Cdd:cd03248 1 GSLAPD--HLKGI---VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyQPQGG-QVLLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 343 GA-----------------------SARRVPDAFASWAFQNPEHQFTRATVAAEIDSALAGTdPHGP-LGADELRKLrea 398
Cdd:cd03248 75 GKpisqyehkylhskvslvgqepvlFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISEL-ASGYdTEVGEKGSQ--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 399 lcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARtwA 478
Cdd:cd03248 151 -------------LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER--A 215
|
250
....*....|.
gi 1080238652 479 DRASIVAEGKV 489
Cdd:cd03248 216 DQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
295-498 |
2.99e-07 |
|
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: 53.98 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMKAGANF--RIDGASARRV-------PDAFASWAF 358
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffqarSGEILLNGFSlkDIDRHTLRQFinylpqePYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QNPEHQFTRATVAAEIDSALAgtdphgplgADELRKLREALcPRALD---PVSPFVLSGGQKRRLGIFLAVAANRRLLLL 435
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWAACE---------IAEIKDDIENM-PLGYQtelSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 436 DEPLAHLDSPSSRIVLDALAEYAGAggTVVFTCHDRRVARTwADRASIVAEGKVAWSGPAADL 498
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
46-242 |
3.31e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 46 GTINAITGPVGCGKTSLAHLIAGLIPSHIPIDhaGFVHIvdaDGteRPVDGDRVT----FVGQD----PSTQVL------ 111
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGVKGS--GSVLL---NG--MPIDAKEMRaisaYVQQDdlfiPTLTVRehlmfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 -TLRVVDDVSMALEFSLVEagivakqsaEALSELGLSELA------EKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPA 184
Cdd:TIGR00955 124 aHLRMPRRVTKKEKRERVD---------EVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 185 AHVDEDGRRSLFAAIRDLRAPGRVILLIEHD-----LRPFDGwvdtvTILDADGSVAAHGAPE 242
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsselFELFDK-----IILMAEGRVAYLGSPD 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
282-520 |
4.28e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVA--RGGE--RILDGADLTLERGEIHALVGANGAGKS-TLLAVL-----------SGQMK-AGAN-FRIDG 343
Cdd:PRK15134 4 PLLAIENLSVAfrQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIRfHGESlLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 344 ASARRVPDAFASWAFQ------NPEHqftraTVAAEIDSALAgtdPHGPLGADELRKlrEALcpRALDPVS--------- 408
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQepmvslNPLH-----TLEKQLYEVLS---LHRGMRREAARG--EIL--NCLDRVGirqaakrlt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 409 --PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGA-GGTVVFTCHDRRVARTWADRASIVA 485
Cdd:PRK15134 152 dyPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1080238652 486 EGKVAWSGPAADLPASPE---------SSRRDRPLPAAGARTSL 520
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPThpytqkllnSEPSGDPVPLPEPASPL 275
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
303-470 |
5.84e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLSG--QMKAGaNFRIDG----ASARRVPDAFASWAFQNpEHQFTRATVAaeids 376
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGlyQPQSG-EILLDGkpvtAEQPEDYRKLFSAVFTD-FHLFDQLLGP----- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 377 alAGTDPHGPLGADELRKLREALCPRALD-PVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRI----VL 451
Cdd:PRK10522 416 --EGKPANPALVEKWLERLKMAHKLELEDgRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREfyqvLL 493
|
170
....*....|....*....
gi 1080238652 452 DALAEyagAGGTVVFTCHD 470
Cdd:PRK10522 494 PLLQE---MGKTIFAISHD 509
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
41-203 |
6.77e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.78 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 41 LSFDFGtINAITGPVGCGKTSLAHLI-----------AGLIPSHIPIDHA-GFVHIV-DADGT----ERPvDGDRVTFVG 103
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEAIryalygkarsrSKLRSDLINVGSEeASVELEfEHGGKryriERR-QGEFAEFLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 104 QDPST------QVLTLRVVDDVSMALE--FSLVEAGIVAKQSAEALSELGLSELAEKDPWA-LSGGQRQRMAIAGAVAra 174
Cdd:COG0419 97 AKPSErkealkRLLGLEIYEELKERLKelEEALESALEELAELQKLKQEILAQLSGLDPIEtLSGGERLRLALADLLS-- 174
|
170 180
....*....|....*....|....*....
gi 1080238652 175 pevMIFDEpaAHVDEDGRRSLFAAIRDLR 203
Cdd:COG0419 175 ---LILDF--GSLDEERLERLLDALEELA 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
293-478 |
6.87e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 293 RGGERILDGADLTLERGEIHALVGANGAGKSTLL----AVLSGQMKAGAnfRIDGASARrvpdafaswafqnpehqFTRA 368
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdaigLALGGAQSATR--RRSGVKAG-----------------CIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 369 TVAAEIDSALAGtdphgplgadelrklrealcpraldpvspfvLSGGQKRRLGIFLAVA----ANRRLLLLDEPLAHLDS 444
Cdd:cd03227 66 AVSAELIFTRLQ-------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....
gi 1080238652 445 PSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWA 478
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELAD 148
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
40-239 |
8.38e-07 |
|
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: 50.00 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAG-LIPSHIPIDHAGFvHIVDADGTERpvdgDRVTFVGQDPSTQVLTLRvv 116
Cdd:cd03247 20 NLSLELkqGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGV-PVSDLEKALS----SLISVLNQRPYLFDTTLR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 ddvsmalefslveagivakqsaealSELGLSelaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLF 196
Cdd:cd03247 93 -------------------------NNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1080238652 197 AAIRDLrAPGRVILLIEHDLRPFDgWVDTVTILDaDGSVAAHG 239
Cdd:cd03247 139 SLIFEV-LKDKTLIWITHHLTGIE-HMDKILFLE-NGKIIMQG 178
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
156-241 |
8.43e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.73 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 156 ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSV 235
Cdd:PRK13537 138 ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEE-GRK 216
|
....*.
gi 1080238652 236 AAHGAP 241
Cdd:PRK13537 217 IAEGAP 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
304-479 |
8.93e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 304 LTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDAFAS------------WAFQNPeHQFTRATVa 371
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigMVFQKP-NPFPKSIY- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 aeiDSALAGTDPHGPLG-ADEL--RKLREAlcprAL-DPV------SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAH 441
Cdd:PRK14243 109 ---DNIAYGARINGYKGdMDELveRSLRQA----ALwDEVkdklkqSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080238652 442 LDsPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWAD 479
Cdd:PRK14243 182 LD-PISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
40-242 |
9.57e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.76 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPShipidhagfvhivdadgterpvDGDRVTFVG-QDPSTQVLTLRVV 116
Cdd:PRK13536 59 GLSFTVasGECFGLLGPNGAGKSTIARMILGMTSP----------------------DAGKITVLGvPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVS----MALEFSLVEAGIV--------AKQSAEALSEL----GLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIF 180
Cdd:PRK13536 117 GVVPqfdnLDLEFTVRENLLVfgryfgmsTREIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 181 DEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILDAdGSVAAHGAPE 242
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA-GRKIAEGRPH 257
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
135-343 |
1.18e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 135 KQSAEA---LSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILL 211
Cdd:PRK10762 117 KMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVY 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 212 IEHDLRPFDGWVDTVTILdADGsvaahgapegiavKGIATSAAPAGAPDASTP---GTGAPDR-PDLESEADAVPLLA-- 285
Cdd:PRK10762 197 ISHRLKEIFEICDDVTVF-RDG-------------QFIAEREVADLTEDSLIEmmvGRKLEDQyPRLDKAPGEVRLKVdn 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 286 LTGTHVarggerilDGADLTLERGEIHALVGANGAGKSTLLAVLSGQM-KAGANFRIDG 343
Cdd:PRK10762 263 LSGPGV--------NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALpRTSGYVTLDG 313
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
139-241 |
1.27e-06 |
|
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: 50.18 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 139 EALSELGLSELAEKDPWAL-----------SGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRApGR 207
Cdd:cd03244 111 QALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DC 189
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1080238652 208 VILLIEHDLRpfdgwvdtvTILDAD-------GSVAAHGAP 241
Cdd:cd03244 190 TVLTIAHRLD---------TIIDSDrilvldkGRVVEFDSP 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
157-217 |
1.39e-06 |
|
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: 49.98 E-value: 1.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAH-----VDEdgrrsLFAAIRDLRAPGRVILLIEHDLR 217
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGlapliVEE-----IFEIIRRLNREGVTILLVEQNAR 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-215 |
1.48e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 47 TINAITGPVGCGKTSLAHLIAGLIP---SHIPIDHAGFVHIVDADGTERPVDGDRVTFVGQDPSTqVLTLRVVDDVSMAL 123
Cdd:PRK14246 37 SIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP-FPHLSIYDNIAYPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 124 E-FSLVEAGIVAKQSAEALSELGL-SELAEK--DPWA-LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAA 198
Cdd:PRK14246 116 KsHGIKEKREIKKIVEECLRKVGLwKEVYDRlnSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKL 195
|
170
....*....|....*..
gi 1080238652 199 IRDLRAPgRVILLIEHD 215
Cdd:PRK14246 196 ITELKNE-IAIVIVSHN 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
297-502 |
1.53e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.06 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKagANFRIdgaSARRVpdafaSWAFQN-----PEHQftRATVA 371
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK--DNWHV---TADRF-----RWNGIDllklsPRER--RKIIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 372 AEI----DSALAGTDPHGPLGadelRKLREALcP-----------------RAL---------DPVS-----PFVLSGGQ 416
Cdd:COG4170 89 REIamifQEPSSCLDPSAKIG----DQLIEAI-PswtfkgkwwqrfkwrkkRAIellhrvgikDHKDimnsyPHELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 417 KRRLGIFLAVAANRRLLLLDEPLAHLDSPS-SRI--VLDALAEYAGAggTVVFTCHD-RRVARtWADRASIVAEGKVAWS 492
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTqAQIfrLLARLNQLQGT--SILLISHDlESISQ-WADTITVLYCGQTVES 240
|
250
....*....|
gi 1080238652 493 GPAADLPASP 502
Cdd:COG4170 241 GPTEQILKSP 250
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
50-238 |
1.62e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.64 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGlipsHIPIDHaGFVHIvdaDGteRPVDG-------DRVTFVGQDPStqVLTLRVVDDVSMA 122
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMG----YYPLTE-GEIRL---DG--RPLSSlshsvlrQGVAMVQQDPV--VLADTFLANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 123 LEFSlveagivAKQSAEALSELGLSELAEKDPWA-----------LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:PRK10790 439 RDIS-------EEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 192 RRSLFAAIRDLRaPGRVILLIEHDLRpfdgwvdtvTILDADGSVAAH 238
Cdd:PRK10790 512 EQAIQQALAAVR-EHTTLVVIAHRLS---------TIVEADTILVLH 548
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
40-203 |
2.08e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhaGFVHIVDADGterpvdgdRVTFVGQDPSTQVLTLRvvD 117
Cdd:TIGR00954 470 SLSFEVpsGNNLLICGPNGCGKSSLFRILGELWPVY------GGRLTKPAKG--------KLFYVPQRPYMTLGTLR--D 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 118 DV--SMALEfSLVEAGIVAKQSAEALSELGLSELAEKD-------PWA--LSGGQRQRMAIAGAVARAPEVMIFDEPAAH 186
Cdd:TIGR00954 534 QIiyPDSSE-DMKRRGLSDKDLEQILDNVQLTHILEREggwsavqDWMdvLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170
....*....|....*..
gi 1080238652 187 VDEDGRRSLFAAIRDLR 203
Cdd:TIGR00954 613 VSVDVEGYMYRLCREFG 629
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
299-331 |
2.22e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.47 E-value: 2.22e-06
10 20 30
....*....|....*....|....*....|...
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSG 331
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG 70
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
50-217 |
2.49e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.39 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIVDADGTERPVDG------DRVTFVGQDpSTQVLTLRVVDDVSMAL 123
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGS-----SGEVSLVGQPLHQMDEEAraklraKHVGFVFQS-FMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 124 EFSLVEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD-EDGRRS---LFAAI 199
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrQTGDKIadlLFSLN 193
|
170
....*....|....*...
gi 1080238652 200 RDLrapGRVILLIEHDLR 217
Cdd:PRK10584 194 REH---GTTLILVTHDLQ 208
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
11-182 |
2.66e-06 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 51.11 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 11 ATRGTAPARLrvSGA-GVRHADGRWAPD----MVDLSF--DFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvh 83
Cdd:TIGR03797 439 DEAKTDPGKL--SGAiEVDRVTFRYRPDgpliLDDVSLqiEPGEFVAIVGPSGSGKSTLLRLLLGF-------------- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 84 ivdadgtERPVDGdRVTFVGQDPST-QVLTLR----VVDDVSMALEFSLVE-----AGIVAKQSAEALSELGLSELAEKD 153
Cdd:TIGR03797 503 -------ETPESG-SVFYDGQDLAGlDVQAVRrqlgVVLQNGRLMSGSIFEniaggAPLTLDEAWEAARMAGLAEDIRAM 574
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 154 PW-----------ALSGGQRQRMAIAGAVARAPEVMIFDE 182
Cdd:TIGR03797 575 PMgmhtvisegggTLSGGQRQRLLIARALVRKPRILLFDE 614
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
298-531 |
2.71e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAG-----------ANFRIDGASAR-----RVPDAFASWAFQNP 361
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSegdirfhdiplTKLQLDSWRSRlavvsQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EHQFTRATvAAEIDSALAGTDPHgplgaDELRKLrealcPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:PRK10789 410 ALGRPDAT-QQEIEHVARLASVH-----DDILRL-----PQGYDTEvgeRGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 439 LAHLDSPSSRIVLDALAEYaGAGGTVVFTCHdRRVARTWADRASIVAEGKVAWSGPAADLPASPESSR---RDRPLPAAg 515
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQW-GEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRdmyRYQQLEAA- 555
|
250
....*....|....*.
gi 1080238652 516 artsLDESPGTSESAA 531
Cdd:PRK10789 556 ----LDDAPEIREEAV 567
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-212 |
3.28e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.40 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 12 TRGTAPARLRVSGAGVRHAdgrwapdMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdaDG 89
Cdd:COG1129 249 AAAPGEVVLEVEGLSVGGV-------VRDVSFSVraGEILGIAGLVGAGRTELARALFGADPAD-----SGEIRL---DG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 90 teRPVDGD--------RVTFVGQDPSTQ--VLTLRVVDDVSMALEFSLVEAGIVAKQSAEALSELGLSELAEK--DPWA- 156
Cdd:COG1129 314 --KPVRIRsprdairaGIAYVPEDRKGEglVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKtpSPEQp 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 157 ---LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLI 212
Cdd:COG1129 392 vgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
35-229 |
3.37e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIdHAGFVHIVDADGTE------RPVDGDRVTFVGQDPST 108
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHV-TADRFRWNGIDLLKlsprerRKIIGREIAMIFQEPSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVltlrvvdDVSMALEFSLVEAgI-----------VAKQSAEALSELgLSELAEKD--------PWALSGGQRQRMAIAG 169
Cdd:COG4170 101 CL-------DPSAKIGDQLIEA-IpswtfkgkwwqRFKWRKKRAIEL-LHRVGIKDhkdimnsyPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 170 AVARAPEVMIFDEPAAHVDEDGRR---SLFAAIRDLRapGRVILLIEHDLRPFDGWVDTVTIL 229
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAqifRLLARLNQLQ--GTSILLISHDLESISQWADTITVL 232
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
50-232 |
3.39e-06 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 50.71 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGLipsHIPIDHAGFVHIVDADGTERPVDGDRVTFVGQDPSTQVLTLRvvDDVSMaLEFSLVE 129
Cdd:TIGR03796 509 ALVGGSGSGKSTIAKLVAGL---YQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVR--DNLTL-WDPTIPD 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 130 AGIV-AKQSAEALSELGL------SELAEkDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLfaaIRDL 202
Cdd:TIGR03796 583 ADLVrACKDAAIHDVITSrpggydAELAE-GGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII---DDNL 658
|
170 180 190
....*....|....*....|....*....|
gi 1080238652 203 RAPGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:TIGR03796 659 RRRGCTCIIVAHRLS---------TIRDCD 679
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-221 |
3.70e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAGLIPshipiDHAGFVHIVDADgterpvdgdrvtfvgqdpstqvltlrvvddvsmalefslve 129
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELG-----PPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 130 agivakQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRD------LR 203
Cdd:smart00382 40 ------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllKS 113
|
170
....*....|....*...
gi 1080238652 204 APGRVILLIEHDLRPFDG 221
Cdd:smart00382 114 EKNLTVILTTNDEKDLGP 131
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
50-239 |
3.96e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAG-LIPSHIPIDHAGFVHIvdADGTERPVDGdrvtfvgqdpstqvLTLRVVDDVSMALEFSlv 128
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRM--AVFSQHHVDG--------------LDLSSNPLLYMMRCFP-- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 129 eaGIVAKQSAEALSELGLS-ELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLfaaIRDLRAPGR 207
Cdd:PLN03073 601 --GVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL---IQGLVLFQG 675
|
170 180 190
....*....|....*....|....*....|...
gi 1080238652 208 VILLIEHDLRPFDGWVDTVTILdADGSVAA-HG 239
Cdd:PLN03073 676 GVLMVSHDEHLISGSVDELWVV-SEGKVTPfHG 707
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
39-188 |
4.29e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.00 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLI---AGLIPShipidhagfvhiVDADGTerpvdgdrVTFVGQD---PSTQVLT 112
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPE------------VTITGS--------IVYNGHNiysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 113 LRvvDDVSMALE------FSLVE--------AGIVAKQSAEALSELGLSELA----EKD-----PWALSGGQRQRMAIAG 169
Cdd:PRK14239 84 LR--KEIGMVFQqpnpfpMSIYEnvvyglrlKGIKDKQVLDEAVEKSLKGASiwdeVKDrlhdsALGLSGGQQQRVCIAR 161
|
170
....*....|....*....
gi 1080238652 170 AVARAPEVMIFDEPAAHVD 188
Cdd:PRK14239 162 VLATSPKIILLDEPTSALD 180
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
39-235 |
6.03e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHipidhAGFVHIvdadGTerpvdGDRVTFVGQDPSTQVLTLRVVDD 118
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD-----SGTVKL----GE-----TVKIGYFDQHQEELDPDKTVLDE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 VSMALEfslveagivAKQSAEALSELGL----SELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:COG0488 400 LRDGAP---------GGTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080238652 195 LFAAIRDLraPGrVILLIEHDlRPFDGWVDTVTILDADGSV 235
Cdd:COG0488 471 LEEALDDF--PG-TVLLVSHD-RYFLDRVATRILEFEDGGV 507
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
157-249 |
8.63e-06 |
|
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: 47.92 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRPFDGwVDTVTILDaDGSVA 236
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQ-NGQVV 216
|
90
....*....|....
gi 1080238652 237 AHGAP-EGIAVKGI 249
Cdd:cd03249 217 EQGTHdELMAQKGV 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
299-456 |
9.74e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQ-MKAGANFRIDGASARRVPDAFASwafQNPeHQFTRaTV 370
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEiLLDGHDLRDYTLASLRNQVALVS---QNV-HLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 AAEIdsALAGTDPHGPLGADELRKLREAL-----CPRALDPV---SPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHL 442
Cdd:PRK11176 434 ANNI--AYARTEQYSREQIEEAARMAYAMdfinkMDNGLDTVigeNGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170
....*....|....
gi 1080238652 443 DSPSSRIVLDALAE 456
Cdd:PRK11176 512 DTESERAIQAALDE 525
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
268-456 |
9.76e-06 |
|
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: 49.05 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 268 APDRPDLESEADAVpllALTGTHVARGGER-ILDGADLTLERGEIHALVGANGAGKSTLL-------AVLSGQMkaganf 339
Cdd:COG5265 345 APDAPPLVVGGGEV---RFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyDVTSGRI------ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 340 RIDG--------ASARR----VP-DA-------FASWAFQNP---EHQFTRATVAAEIDSALAGTdphgPLGADEL---R 393
Cdd:COG5265 416 LIDGqdirdvtqASLRAaigiVPqDTvlfndtiAYNIAYGRPdasEEEVEAAARAAQIHDFIESL----PDGYDTRvgeR 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 394 KLRealcpraldpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAE 456
Cdd:COG5265 492 GLK---------------LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
282-454 |
1.03e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.85 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLL------------AVLSGQMK-AGANF---RIDGAS 345
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmndlnpeVTITGSIVyNGHNIyspRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 346 ARR-------VPDAFASWAFQNPEHQF------TRATVAAEIDSALAGtdphgplgADELRKLREALCPRALDpvspfvL 412
Cdd:PRK14239 84 LRKeigmvfqQPNPFPMSIYENVVYGLrlkgikDKQVLDEAVEKSLKG--------ASIWDEVKDRLHDSALG------L 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1080238652 413 SGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDAL 454
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
282-489 |
1.03e-05 |
|
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: 46.66 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGgeriLDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA-GANFRIDGASARRVPdafaswafqn 360
Cdd:cd03215 3 PVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVTRRS---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 361 pehqfTRATVAAEIdsALAGTDPHgplgadelrklREALCPRAldPVS-----PFVLSGG--QKrrlgIFLA--VAANRR 431
Cdd:cd03215 69 -----PRDAIRAGI--AYVPEDRK-----------REGLVLDL--SVAenialSSLLSGGnqQK----VVLArwLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 432 LLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
279-471 |
1.11e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.40 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 279 DAVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK--AGANFRIDGASARRVPDAF--- 353
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISptSGTLLFEGEDISTLKPEIYrqq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 354 ASWAFQNPehqftratvaaeidsALAGTDPHGPL--------GADELRKLREALCPRALD------PVSPfvLSGGQKRR 419
Cdd:PRK10247 83 VSYCAQTP---------------TLFGDTVYDNLifpwqirnQQPDPAIFLDDLERFALPdtiltkNIAE--LSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 420 LGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDR 471
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNiAVLWVTHDK 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
292-502 |
1.14e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 292 ARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-----AGANFRIDGA--------SARRVPDAFASWAF 358
Cdd:PRK15093 16 SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvTADRMRFDDIdllrlsprERRKLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 359 QNPEHQFTRAT-VAAEIDSALAGTDPHGPLGADELRKLREAL---------CPRALDPVSPFVLSGGQKRRLGIFLAVAA 428
Cdd:PRK15093 96 QEPQSCLDPSErVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIellhrvgikDHKDAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 429 NRRLLLLDEPLAHLDSPSSRIVLDALAEY-AGAGGTVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADLPASP 502
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
48-188 |
1.22e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 48 INAITGPVGCGKTSLAHL---IAGLIPShIPIDHAGFVHIVDA-DGTERPVD-GDRVTFVGQDPSTqvLTLRVVDDVSMA 122
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCfnrLNDLIPG-FRVEGKVTFHGKNLyAPDVDPVEvRRRIGMVFQKPNP--FPKSIYDNIAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 123 LEFS--------LVEAGIvaKQSA------EALSELGLSelaekdpwaLSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:PRK14243 115 ARINgykgdmdeLVERSL--RQAAlwdevkDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-326 |
1.30e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 141 LSELGLSELA-EKDPWALSGGQRQRMAIAGAV-ARAPEVM-IFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLR 217
Cdd:TIGR00630 472 LIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 218 pfdgwvdtvTILDAD-------------GSVAAHGAPEGI-AVKGIATSAAPAGA-----PDASTPGTGApdrpdlesea 278
Cdd:TIGR00630 552 ---------TIRAADyvidigpgagehgGEVVASGTPEEIlANPDSLTGQYLSGRkkievPAERRPGNGK---------- 612
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1080238652 279 davpLLALTGTHvarggERILDGADLTLERGEIHALVGANGAGKSTLL 326
Cdd:TIGR00630 613 ----FLTLKGAR-----ENNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
35-229 |
1.31e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDhAGFVHIVDAD------GTERPVDGDRVTFVGQDPST 108
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVT-ADRMRFDDIDllrlspRERRKLVGHNVSMIFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 109 QVltlrvvdDVSMALEFSLVEA--------------GIVAKQSAEALSELGLSElaEKD-----PWALSGGQRQRMAIAG 169
Cdd:PRK15093 101 CL-------DPSERVGRQLMQNipgwtykgrwwqrfGWRKRRAIELLHRVGIKD--HKDamrsfPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 170 AVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTIL 229
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
156-242 |
1.32e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 156 ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPG-RVILLIEHDLRPFDGwVDTVTIL---DA 231
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFnnpDR 1436
|
90
....*....|..
gi 1080238652 232 DGS-VAAHGAPE 242
Cdd:PTZ00265 1437 TGSfVQAHGTHE 1448
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
297-526 |
1.44e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.81 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 297 RILDGADLTLERGEIHALVGANGAGKS-TLLAVLS-----GQMKA------GANF-RIDGASARRVPDAFASWAFQNPEH 363
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGlidypGRVMAeklefnGQDLqRISEKERRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 QFTRA-TVAAEIDSAL----AGTDPHGPLGADELRKLREALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:PRK11022 101 SLNPCyTVGFQIMEAIkvhqGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 439 LAHLDSPSSRIVLDALAEYAGAGG-TVVFTCHDRRVARTWADRASIVAEGKVAWSGPAADL---PASPESSRRDRPLPA- 513
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIfraPRHPYTQALLRALPEf 260
|
250
....*....|...
gi 1080238652 514 AGARTSLDESPGT 526
Cdd:PRK11022 261 AQDKARLASLPGV 273
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
278-506 |
1.48e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 47.10 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 278 ADAVPLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQmkaganFRIDGASARRVP 350
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGE------IRVGGEEIRLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 351 DAF-----ASWA------------FQNpehqF---TRATVAAEIDSAlagtdPHGPLG--ADELRKLREALcpraLDPVS 408
Cdd:COG4598 77 DRDgelvpADRRqlqrirtrlgmvFQS----FnlwSHMTVLENVIEA-----PVHVLGrpKAEAIERAEAL----LAKVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 409 --------PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADR 480
Cdd:COG4598 144 ladkrdayPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSH 223
|
250 260
....*....|....*....|....*.
gi 1080238652 481 ASIVAEGKVAWSGPAADLPASPESSR 506
Cdd:COG4598 224 VVFLHQGRIEEQGPPAEVFGNPKSER 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
50-216 |
1.49e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIAgLI--PSHIPIDHAGfVHIVDADGTERPVDGDRVTFVGQDPSTqvlTLRVVDDVSMALEFSL 127
Cdd:PRK11308 45 AVVGESGCGKSTLARLLT-MIetPTGGELYYQG-QDLLKADPEAQKLLRQKIQIVFQNPYG---SLNPRKKVGQILEEPL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 128 V-----EAGIVAKQSAEALSELGL-SELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRD 201
Cdd:PRK11308 120 LintslSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMD 199
|
170
....*....|....*.
gi 1080238652 202 LRAP-GRVILLIEHDL 216
Cdd:PRK11308 200 LQQElGLSYVFISHDL 215
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
406-470 |
1.52e-05 |
|
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: 1.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 406 PVSPFVLSGGQKRRLGIFLAVAANR---RLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHD 470
Cdd:pfam13304 231 ELPAFELSDGTKRLLALLAALLSALpkgGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-242 |
1.58e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 47.07 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 20 LRVSGAGVRhADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGlipshipidhagfvhivdadgtERPVDGDRV 99
Cdd:PRK13548 3 LEARNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----------------------ELSPDSGEV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 100 TFVGQD----PSTQVLTLRVVDDVSMALEFSL-----VEAGIVAKQS---------AEALSELGLSELAEKDPWALSGGQ 161
Cdd:PRK13548 60 RLNGRPladwSPAELARRRAVLPQHSSLSFPFtveevVAMGRAPHGLsraeddalvAAALAQVDLAHLAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 162 RQRMAIA------GAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL--RAPGRVIlLIEHDLRPFDGWVDTVTILdADG 233
Cdd:PRK13548 140 QQRVQLArvlaqlWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVI-VVLHDLNLAARYADRIVLL-HQG 217
|
....*....
gi 1080238652 234 SVAAHGAPE 242
Cdd:PRK13548 218 RLVADGTPA 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
46-214 |
1.59e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 46 GTINAITGPVGCGKTSLAHLIAGLIPSHipiDHAGFVHIVDADGTERPVDgdRVTFVGQD----PSTQVL-TLRVVDDVS 120
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGN---NFTGTILANNRKPTKQILK--RTGFVTQDdilyPHLTVReTLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 121 MALEFSLVEAGIVAKQsaeALSELGLSE-----LAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSL 195
Cdd:PLN03211 169 LPKSLTKQEKILVAES---VISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170
....*....|....*....
gi 1080238652 196 FAAIRDLRAPGRVILLIEH 214
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMH 264
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
290-474 |
1.88e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.70 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 290 HVARGGER--ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGqmkaganfrIDGASARRVPDAFASWAFQNPEHqftR 367
Cdd:PRK10584 15 SVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAG---------LDDGSSGEVSLVGQPLHQMDEEA---R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 368 ATVAA----------------------EIDSALAG-TDPHGPLGADELrkLREALCPRALDPVsPFVLSGGQKRRLGIFL 424
Cdd:PRK10584 83 AKLRAkhvgfvfqsfmliptlnalenvELPALLRGeSSRQSRNGAKAL--LEQLGLGKRLDHL-PAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1080238652 425 AVAANRRLLLLDEPLAHLDSPSSRIVLDAL----AEYAgagGTVVFTCHDRRVA 474
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHG---TTLILVTHDLQLA 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
298-450 |
1.91e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.18 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVL-------SGQMkaganfRIDGASARRVpdafaswafqnpEHQFTRATV 370
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQV------LLDGVPLVQY------------DHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 371 aaeidsALAGTDP------------HGPLGADELRKLREALCPRALDPVSPFV-------------LSGGQKRRLGIFLA 425
Cdd:TIGR00958 558 ------ALVGQEPvlfsgsvreniaYGLTDTPDEEIMAAAKAANAHDFIMEFPngydtevgekgsqLSGGQKQRIAIARA 631
|
170 180
....*....|....*....|....*
gi 1080238652 426 VAANRRLLLLDEPLAHLDSPSSRIV 450
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLL 656
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
157-216 |
1.97e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 1.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRA-PGRVILLIEHDL 216
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRL 640
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-216 |
1.99e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIaglipSHIPIDHAGFVHIVDADGTERPVDG--------DRVTFVG 103
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-----NRMNDKVSGYRYSGDVLLGGRSIFNyrdvlefrRRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 104 QDPSTqvLTLRVVDDVSMALE-FSLVEAGIVAKQSAEALSELGLSElAEKD-----PWALSGGQRQRMAIAGAVARAPEV 177
Cdd:PRK14271 108 QRPNP--FPMSIMDNVLAGVRaHKLVPRKEFRGVAQARLTEVGLWD-AVKDrlsdsPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 1080238652 178 MIFDEPAAHVDEDGRRSLFAAIRDLrAPGRVILLIEHDL 216
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNL 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
309-443 |
2.09e-05 |
|
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: 46.98 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 309 GEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDAFASWAFQNpehQFTR-------------------AT 369
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQN---YFTKllegdvkvivkpqyvdlipKA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 370 VAAEIDSALAGTDPHGPLG----ADELRKLREalcpRALDPvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLD 443
Cdd:cd03236 103 VKGKVGELLKKKDERGKLDelvdQLELRHVLD----RNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
128-216 |
2.11e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.47 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 128 VEAGIVAKQSAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGR 207
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
....*....
gi 1080238652 208 VILLIEHDL 216
Cdd:TIGR01257 2122 AVVLTSHSM 2130
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
299-503 |
2.15e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRID-GASARRVPDAfaSWAFQnpehqftrATVAAEIdsa 377
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVViRGSVAYVPQV--SWIFN--------ATVRENI--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 378 LAGTDPHG-----PLGADELRKLREALCPRALDPVSP--FVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIV 450
Cdd:PLN03232 700 LFGSDFESerywrAIDVTALQHDLDLLPGRDLTEIGErgVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 451 LDALAEYAGAGGTVVFTCHDRRVArTWADRASIVAEGKVAWSGPAADLPASPE 503
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
298-525 |
2.23e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 298 ILDGADLTLERGEIHALVGANGAGKSTLLAVLSGqmkaganfRIDGASarrvpdaFASWAFQN---PEHQFTRATVAAEI 374
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--------RIQGNN-------FTGTILANnrkPTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 375 DSALAgtdPHgpLGADE------LRKLREALCP----RALDPV---------------SPFV--LSGGQKRRLGIFLAVA 427
Cdd:PLN03211 148 DDILY---PH--LTVREtlvfcsLLRLPKSLTKqekiLVAESViselgltkcentiigNSFIrgISGGERKRVSIAHEML 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 428 ANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCH--DRRVARTWaDRASIVAEGKVAWSGPAADLPASPESS 505
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHqpSSRVYQMF-DSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
250 260
....*....|....*....|
gi 1080238652 506 RRDRPLPAAGARTSLDESPG 525
Cdd:PLN03211 302 GFSPSFPMNPADFLLDLANG 321
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
303-437 |
2.45e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.49 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLSG-QMKAGANFRIDGasaRRVPDafASWA---------FQNPeHQFTRatvaa 372
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGEILLDG---QPVTA--DNREayrqlfsavFSDF-HLFDR----- 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080238652 373 eidsaLAGtdPHGPLGADELRKLREALcprALDPVSPFV--------LSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:COG4615 421 -----LLG--LDGEADPARARELLERL---ELDHKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
157-216 |
2.50e-05 |
|
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: 46.36 E-value: 2.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPA-----AHVDEDGRrslfaAIRDLRAPGRV-ILLIEHDL 216
Cdd:TIGR03410 132 LSGGQQQQLAIARALVTRPKLLLLDEPTegiqpSIIKDIGR-----VIRRLRAEGGMaILLVEQYL 192
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
40-185 |
2.56e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.57 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDF--GTINAITGPVGCGKTSLahL-----IAGLIPShipidhagfvhiVDADGterpvdgdRVTFVGQD---PSTQ 109
Cdd:COG1117 29 DINLDIpeNKVTALIGPSGCGKSTL--LrclnrMNDLIPG------------ARVEG--------EILLDGEDiydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 110 VLTLR----------------VVDDVSMALEfslvEAGIVAKQSAEALSELGLSELA---E-KD-----PWALSGGQRQR 164
Cdd:COG1117 87 VVELRrrvgmvfqkpnpfpksIYDNVAYGLR----LHGIKSKSELDEIVEESLRKAAlwdEvKDrlkksALGLSGGQQQR 162
|
170 180
....*....|....*....|.
gi 1080238652 165 MAIAGAVARAPEVMIFDEPAA 185
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTS 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
31-244 |
2.59e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 31 DGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPSHIPIDHAGFVHIVDADGteRPVdgdrvtfvGQDPSTQV 110
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNG--EPL--------AAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 111 LTLRVV--DDVSMALEFSLVE------------AGIVAKQSAE----ALSELGLSELAEKDPWALSGGQRQRMAIAGAVA 172
Cdd:PRK13547 82 ARLRAVlpQAAQPAFAFSAREivllgrypharrAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 173 ---------RAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRV-ILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPE 242
Cdd:PRK13547 162 qlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAML-ADGAIVAHGAPA 240
|
..
gi 1080238652 243 GI 244
Cdd:PRK13547 241 DV 242
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
294-489 |
2.70e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 294 GGERILDGADLTLERGEIHALVGANGAgkstllAVLSGQMKAganfRIDGASARRVPDAFASW-----------AFQNPE 362
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALPA----HV*GPDAGRRPWRF*TWcanrralrrtiG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 363 HQFTRATVAAEIDSALAG-----TDPHGPLGADELRKlREALCPRALDPVSPFvlSGGQKRRLGIFLAVAANRRLLLLDE 437
Cdd:NF000106 94 R*GRRESFSGRENLYMIGr*ldlSRKDARARADELLE-RFSLTEAAGRAAAKY--SGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 438 PLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVARTWA------DRASIVAEGKV 489
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAheltviDRGRVIADGKV 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
295-331 |
2.88e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 2.88e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG 331
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG 46
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
32-188 |
3.04e-05 |
|
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: 47.43 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 32 GRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGFvhivDADGTERPVDGDRVTFVGQDP---S 107
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGF----SLKDIDRHTLRQFINYLPQEPyifS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 108 TQVLTLRVV--------DDVSMALEFSLVEAGIvakqsaEALSeLGL-SELAEkDPWALSGGQRQRMAIAGAVARAPEVM 178
Cdd:TIGR01193 562 GSILENLLLgakenvsqDEIWAACEIAEIKDDI------ENMP-LGYqTELSE-EGSSISGGQKQRIALARALLTDSKVL 633
|
170
....*....|
gi 1080238652 179 IFDEPAAHVD 188
Cdd:TIGR01193 634 ILDESTSNLD 643
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-216 |
3.25e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 19 RLRV---SGAGVRhadgrwapdmvDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPS---HIPIDH------------ 78
Cdd:PRK10762 257 RLKVdnlSGPGVN-----------DVSFTLrkGEILGVSGLMGAGRTELMKVLYGALPRtsgYVTLDGhevvtrspqdgl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 79 -AGFVHIVDadgtERPVDGdrvtfvgqdpstQVLTLRVVDDVSM-ALE-FSLVEAGIVAKQSAEALSE-LGLSELaeKDP 154
Cdd:PRK10762 326 aNGIVYISE----DRKRDG------------LVLGMSVKENMSLtALRyFSRAGGSLKHADEQQAVSDfIRLFNI--KTP 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 155 WA------LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:PRK10762 388 SMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEM 455
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
40-229 |
3.35e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDFGTINAITGPVGCGKTSLahliaglipshipIDHAGFVHIVDADGTERPVDGDRVTFVGQdpstqvltlrvvddV 119
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTI-------------LDAIGLALGGAQSATRRRSGVKAGCIVAA--------------V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 120 SMALEFSLVEagivakqsaealselglselaekdpwaLSGGQRQRMAIA-----GAVARAPEVmIFDEPAAHVDEDGRRS 194
Cdd:cd03227 68 SAELIFTRLQ---------------------------LSGGEKELSALAlilalASLKPRPLY-ILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*
gi 1080238652 195 LFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTIL 229
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-248 |
3.82e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 36 PDMVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshiPIDHAGFVhivdadgterpVDGdRVTFVGQdpSTQVLTL 113
Cdd:PLN03130 631 PTLSNINLDVpvGSLVAIVGSTGEGKTSLISAMLGELP---PRSDASVV-----------IRG-TVAYVPQ--VSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 114 RVVDDVSMALEF--SLVEAGIVAKQSAEALSEL---GLSELAEKDPwALSGGQRQRMAIAGAVARAPEVMIFDEPA---- 184
Cdd:PLN03130 694 TVRDNILFGSPFdpERYERAIDVTALQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLsald 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 185 AHVdedGRRSLFAAIRD-LRAPGRVilLIEHDLRpFDGWVDTVtILDADGSVAAHGAPEGIAVKG 248
Cdd:PLN03130 773 AHV---GRQVFDKCIKDeLRGKTRV--LVTNQLH-FLSQVDRI-ILVHEGMIKEEGTYEELSNNG 830
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
37-220 |
3.88e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 37 DMVDLSFDF---------------GTINAITGPVGCGKTSLAHLIAGLI-PSHIPIDHAGfvhivdadgteRPVDGDRVT 100
Cdd:PRK13540 3 DVIELDFDYhdqpllqqisfhlpaGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEILFER-----------QSIKKDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 101 ------FVGQDPSTQ-VLTLRvvDDVSMALEFSLVEAGIvakqsAEALSELGLSELAEKDPWALSGGQRQRMAIAGAVAR 173
Cdd:PRK13540 72 yqkqlcFVGHRSGINpYLTLR--ENCLYDIHFSPGAVGI-----TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 174 APEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFD 220
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLN 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-216 |
4.46e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 15 TAPARLRVSGAGVRHADGRWAPDMVDLSFDFGTINAITGPVGCGKTSLAHLIAGLipshipidhagfvhivdadgteRPV 94
Cdd:COG3845 253 PGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL----------------------RPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 95 DGDRVTFVGQD----PSTQVLTLRVV---DD---VSMALEFSLVEAGIVAKQSAEALSELGL------SELAEK------ 152
Cdd:COG3845 311 ASGSIRLDGEDitglSPRERRRLGVAyipEDrlgRGLVPDMSVAENLILGRYRRPPFSRGGFldrkaiRAFAEElieefd 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 153 ----DPWA----LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:COG3845 391 vrtpGPDTparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDL 462
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
138-188 |
4.85e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 4.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1080238652 138 AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:NF033858 379 AEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-249 |
5.16e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPshiPIDHAGfvhiVDADGTerpvdgdrVTFVGQDPSTQVLTLRvvDD 118
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELS---HAETSS----VVIRGS--------VAYVPQVSWIFNATVR--EN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 VSMALEFSLVEAGIVAKQSA-----EALSELGLSELAEKDPwALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRR 193
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTAlqhdlDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080238652 194 SLF-AAIRD-LRAPGRVILLIEHDLRPFdgwVDTVtILDADGSVAAHGAPEGIAVKGI 249
Cdd:PLN03232 778 QVFdSCMKDeLKGKTRVLVTNQLHFLPL---MDRI-ILVSEGMIKEEGTFAELSKSGS 831
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
299-452 |
5.19e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKA--GANFRIDGASARrVPDAfaSWAFQnpehqftrATVAaeiDS 376
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASVVIRGTVAY-VPQV--SWIFN--------ATVR---DN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 377 ALAGT--DPHGPLGADELRKLREALcprALDPVSPFV--------LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPS 446
Cdd:PLN03130 699 ILFGSpfDPERYERAIDVTALQHDL---DLLPGGDLTeigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
....*.
gi 1080238652 447 SRIVLD 452
Cdd:PLN03130 776 GRQVFD 781
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
157-216 |
5.35e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 5.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDL 216
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-218 |
5.87e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 38 MVDLSFDF--GTINAITGPVGCGKTSLAHLIAGLI-PSHIPIdhagFVHIVDADGTERPVdgdrVTFVGQDPSTQvLTLR 114
Cdd:PRK13541 16 LFDLSITFlpSAITYIKGANGCGKSSLLRMIAGIMqPSSGNI----YYKNCNINNIAKPY----CTYIGHNLGLK-LEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 115 VVDDVSMALEFSLVEAGIVAkqsaeALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRS 194
Cdd:PRK13541 87 VFENLKFWSEIYNSAETLYA-----AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|....
gi 1080238652 195 LFAAIRDLRAPGRVILLIEHDLRP 218
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSHLESS 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-254 |
6.00e-05 |
|
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: 46.86 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 33 RWAPDM------VDLSFDFGTINAITGPVGCGKTSLAhliaglipshipidhAGFVHIVDADGTERPVDG---------- 96
Cdd:TIGR00957 1293 RYREDLdlvlrhINVTIHGGEKVGIVGRTGAGKSSLT---------------LGLFRINESAEGEIIIDGlniakiglhd 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 97 --DRVTFVGQDPSTQVLTLRV---------VDDVSMALEFSLVEaGIVAKQSAEALSELglSELAEKdpwaLSGGQRQRM 165
Cdd:TIGR00957 1358 lrFKITIIPQDPVLFSGSLRMnldpfsqysDEEVWWALELAHLK-TFVSALPDKLDHEC--AEGGEN----LSVGQRQLV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 166 AIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDlRAPGRVILLIEHDLRPFDGWVdTVTILDaDGSVAAHGAP-EGI 244
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLD-KGEVAEFGAPsNLL 1507
|
250
....*....|
gi 1080238652 245 AVKGIATSAA 254
Cdd:TIGR00957 1508 QQRGIFYSMA 1517
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
409-502 |
6.51e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 409 PFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGT-VVFTCHDRRVARTWADRASIVAEG 487
Cdd:PRK11144 126 PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQG 205
|
90
....*....|....*
gi 1080238652 488 KVAWSGPAADLPASP 502
Cdd:PRK11144 206 KVKAFGPLEEVWASS 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
305-443 |
7.06e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 305 TLERGEIHALVGANGAGKSTLLAVLSGQMKAGANFRIDGASARRVPDAFASWAFQNpehqFTRATVAAEIDSA------- 377
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQN----YFKKLYNGEIKVVhkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 378 -------------LAGTDPHGPLgaDELRK---LREALcPRALDpvspfVLSGGQKRRLGIFLAVAANRRLLLLDEPLAH 441
Cdd:PRK13409 171 lipkvfkgkvrelLKKVDERGKL--DEVVErlgLENIL-DRDIS-----ELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
..
gi 1080238652 442 LD 443
Cdd:PRK13409 243 LD 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
157-232 |
7.39e-05 |
|
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: 46.35 E-value: 7.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLrAPGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLS---------TIVDAD 560
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-215 |
1.05e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 135 KQSAEALSELGLSELA-EKDPWALSGGQRQRMAIA---GAvarapEVM----IFDEPAAHVDEDGRRSLFAAIRDLRAPG 206
Cdd:PRK00635 454 KSRLSILIDLGLPYLTpERALATLSGGEQERTALAkhlGA-----ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQG 528
|
....*....
gi 1080238652 207 RVILLIEHD 215
Cdd:PRK00635 529 NTVLLVEHD 537
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
299-489 |
1.06e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 299 LDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMK-AGANFRIDGasarrvpdafaswafqnpehQFTRATVAAEIDSA 377
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSpTVGKVDRNG--------------------EVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 378 LAGTD--PHGPLGADELRKLREALCPRALD----------PVSPFvlSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSP 445
Cdd:PRK13546 100 LTGIEniEFKMLCMGFKRKEIKAMTPKIIEfselgefiyqPVKKY--SSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080238652 446 SSRIVLDALAEYAGAGGTVVFTCHDRRVARTWADRASIVAEGKV 489
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
309-487 |
1.09e-04 |
|
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: 46.16 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 309 GEIHALVGANGAGKSTLLAVLSGQMKAGANfriDGASARRVPDAFASWAFQNPEH--QFTratvaaEIDSALAGTDpHGP 386
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSG---DATVAGKSILTNISDVHQNMGYcpQFD------AIDDLLTGRE-HLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 387 L-------GADELRKLR----EALCPRALDPVSPFVLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALA 455
Cdd:TIGR01257 2035 LyarlrgvPAEEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190
....*....|....*....|....*....|..
gi 1080238652 456 EYAGAGGTVVFTCHDRRVARTWADRASIVAEG 487
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
50-239 |
1.12e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.59 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 50 AITGPVGCGKTSLAHLIA-------GLIP-SHIPIDHAgfvhivdADGTERpvdgDRVTFVGQDPSTQVLTLRvvDDVSM 121
Cdd:PRK11160 370 ALLGRTGCGKSTLLQLLTrawdpqqGEILlNGQPIADY-------SEAALR----QAISVVSQRVHLFSATLR--DNLLL 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 122 ALEFSLVEagivakQSAEALSELGLSELAEKDP----W------ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDG 191
Cdd:PRK11160 437 AAPNASDE------ALIEVLQQVGLEKLLEDDKglnaWlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1080238652 192 RRSLFAAIRDLrAPGRVILLIEHDLRPFDGwVDTVTILDaDGSVAAHG 239
Cdd:PRK11160 511 ERQILELLAEH-AQNKTVLMITHRLTGLEQ-FDRICVMD-NGQIIEQG 555
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
282-331 |
1.33e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.33 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1080238652 282 PLLALTGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLLAVLSG 331
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG 52
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
305-470 |
1.37e-04 |
|
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: 45.16 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 305 TLERGEIHALVGANGAGKSTLLAVLSGQMKagANF-RIDG-ASARRVPDAFASWAFQN---------------PEH---- 363
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELK--PNLgDYDEePSWDEVLKRFRGTELQDyfkklangeikvahkPQYvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 364 -QFTRATVAaeidSALAGTDPHGPLgaDELRK---LREALcPRALDpvspfVLSGGQKRRLGIFLAVAANRRLLLLDEPL 439
Cdd:COG1245 173 pKVFKGTVR----ELLEKVDERGKL--DELAEklgLENIL-DRDIS-----ELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|..
gi 1080238652 440 AHLDSpSSRI-VLDALAEYAGAGGTVVFTCHD 470
Cdd:COG1245 241 SYLDI-YQRLnVARLIRELAEEGKYVLVVEHD 271
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-215 |
1.54e-04 |
|
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: 43.75 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 40 DLSFDFGT-INAITGPVGCGKTSLAHLI-AGLIPSHIPidhagfvhivdadgTERPVDGDRVTFVGQDPSTQV-LTLRVV 116
Cdd:cd03240 15 RSEIEFFSpLTLIVGQNGAGKTTIIEALkYALTGELPP--------------NSKGGAHDPKLIREGEVRAQVkLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 117 DDVSMAL--EFSLVEAGIVAKQSaealselGLSELAEKDPWALSGGQRQ------RMAIAGAVARAPEVMIFDEPAAHVD 188
Cdd:cd03240 81 NGKKYTItrSLAILENVIFCHQG-------ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180
....*....|....*....|....*....
gi 1080238652 189 EDGRRSLFAAIRDLRAPGRV--ILLIEHD 215
Cdd:cd03240 154 EENIEESLAEIIEERKSQKNfqLIVITHD 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
139-244 |
2.08e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.01 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 139 EALSELGLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLR 217
Cdd:PRK10575 130 EAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDIN 209
|
90 100
....*....|....*....|....*..
gi 1080238652 218 PFDGWVDTVTILDAdGSVAAHGAPEGI 244
Cdd:PRK10575 210 MAARYCDYLVALRG-GEMIAQGTPAEL 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
156-232 |
2.57e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 2.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 156 ALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRApGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLS---------TVRNAD 537
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
39-232 |
3.30e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.02 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLA--------------------------------HLIAGLIPShIPIDHagfvhivd 86
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarqflgqmdkpdvDSIEGLSPA-IAIDQ-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 87 adgterpvdgdrvTFVGQDPSTQVLTLRVVDDvSMALEFSLVeaGIVAKqsAEALSELGLSELA-EKDPWALSGGQRQRM 165
Cdd:cd03270 85 -------------KTTSRNPRSTVGTVTEIYD-YLRLLFARV--GIRER--LGFLVDVGLGYLTlSRSAPTLSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 166 AIAGAV-ARAPEVM-IFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRpfdgwvdtvTILDAD 232
Cdd:cd03270 147 RLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED---------TIRAAD 206
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-326 |
3.91e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 136 QSAEALSELGLSELAEKDP-WALSGGQRQRMAIA---GAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILL 211
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 212 IEHDLRPFDgWVDTVTIL-----DADGSVAAHGAPEGIAVKGiaTSAAPAGAPDASTPgtgaPDRPDLESEADAVPLLAl 286
Cdd:PRK00635 868 IEHNMHVVK-VADYVLELgpeggNLGGYLLASCSPEELIHLH--TPTAKALRPYLSSP----QELPYLPDPSPKPPVPA- 939
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080238652 287 tGTHVARGGERILDGADLTLERGEIHALVGANGAGKSTLL 326
Cdd:PRK00635 940 -DITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLV 978
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
303-455 |
4.04e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.38 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 303 DLTLERGEIHALVGANGAGKSTLLAVLsGQMKAGANFRIDGASARRvpDAFASWAFQNPEHQFTRATVAAEIDSALAGT- 381
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDAL-RFLSDAARGGLQDALARR--GGLEELLWRGPRTITEPIRLELEFAEEDERDl 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 382 ----DPHGPLGADELRKLREALCPRALDPVSPFVLSGGQKRRL-GIFLAVAANRRllLLDEPLAHLDSPSSRIVLDALA 455
Cdd:COG4637 92 ryelELGLPEPGGRPEVKEERLWLKRGSGGRPFLDFRPKGRAVgGEPERLDSPES--LLSQLGDPERFPELRALREALR 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
306-488 |
5.40e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 306 LERGEIHALVGANGAGKSTLLAVLSGQMKaganfridgasarrvpdafaswafqnpehqftratvaaeidsalagtdPHG 385
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLI------------------------------------------------PNG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 386 plGADELRKLREALCPRALDpvspfvLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVV 465
Cdd:cd03222 54 --DNDEWDGITPVYKPQYID------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|....
gi 1080238652 466 FTC-HDRRVARTWADRAsIVAEGK 488
Cdd:cd03222 126 LVVeHDLAVLDYLSDRI-HVFEGE 148
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
295-465 |
5.96e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 43.26 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 295 GERILDGADLTLERGEIHALVGANGAGKSTLLAVLSGQMKAGANfRIDGASARRVpdAFASW-------------AFQNP 361
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-RIARPAGARV--LFLPQrpylplgtlrealLYPAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 362 EHQFTRATVAAeidsalagtdphgplgadELRKLR-EALCPRaLDPVSPF--VLSGGQKRRLGIFLAVAANRRLLLLDEP 438
Cdd:COG4178 452 AEAFSDAELRE------------------ALEAVGlGHLAER-LDEEADWdqVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180
....*....|....*....|....*..
gi 1080238652 439 LAHLDSPSSRIVLDALAEyAGAGGTVV 465
Cdd:COG4178 513 TSALDEENEAALYQLLRE-ELPGTTVI 538
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-216 |
7.05e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 35 APDMVDLSFDFGTINAITGPVGCGKT--SLAhlIAGLI--PSHIPIDHAGFvhivdaDGTE---------RPVDGDRVTF 101
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLIdyPGRVMAEKLEF------NGQDlqrisekerRNLVGAEVAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 102 VGQDPSTQVltlrvvdDVSMALEFSLVEAGIV--------AKQSA-EALSELGLSELAEK---DPWALSGGQRQRMAIAG 169
Cdd:PRK11022 94 IFQDPMTSL-------NPCYTVGFQIMEAIKVhqggnkktRRQRAiDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1080238652 170 AVARAPEVMIFDEPAAHVDEdgrrSLFAAIRDL-----RAPGRVILLIEHDL 216
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDV----TIQAQIIELllelqQKENMALVLITHDL 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-242 |
8.05e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.84 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 30 ADGRWAPdmvdLSFDF--GTINAITGPVGCGKTSLAHLIAGLIPshipidHAGFVHIVDADGTERPVDG---DRVTFVGQ 104
Cdd:PRK03695 8 VSTRLGP----LSAEVraGEILHLVGPNGAGKSTLLARMAGLLP------GSGSIQFAGQPLEAWSAAElarHRAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 105 DPSTQVLtlrvvdDVSMALEFSLvEAGIVAKQSAEALSE----LGLSELAEKDPWALSGGQRQRMAIAGA---VARA--P 175
Cdd:PRK03695 78 QTPPFAM------PVFQYLTLHQ-PDKTRTEAVASALNEvaeaLGLDDKLGRSVNQLSGGEWQRVRLAAVvlqVWPDinP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080238652 176 E--VMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVAAHGAPE 242
Cdd:PRK03695 151 AgqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLL-KQGKLLASGRRD 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
39-215 |
8.55e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.79 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKTSLAHLIAGlipshipidhagfvhivdadgTERPVDGdRVTFVGQDpSTQVLTLRVVDD 118
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCG---------------------DPRATSG-RIVFDGKD-ITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 119 V------------SMALEFSLVEAGIVAK-----QSAEALSEL--GLSELAEKDPWALSGGQRQRMAIAGAVARAPEVMI 179
Cdd:PRK11614 81 AvaivpegrrvfsRMTVEENLAMGGFFAErdqfqERIKWVYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1080238652 180 FDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHD 215
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQN 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
39-239 |
1.23e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 39 VDLSFDFGTINAITGPVGCGKtSLAHLIA-GLIPSHIPiDHAGFVHivdADGTE---RPVDGDRVTFVGQDPSTQ---VL 111
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGK-SLTCAAAlGILPAGVR-QTAGRVL---LDGKPvapCALRGRKIATIMQNPRSAfnpLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 112 TLRvvddvSMALEfSLVEAGIVA--KQSAEALSELGLSE---LAEKDPWALSGGQRQRMAIAGAV-ARAPeVMIFDEPAA 185
Cdd:PRK10418 97 TMH-----THARE-TCLALGKPAddATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALlCEAP-FIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080238652 186 HVDEDGRR---SLFAAIRDLRAPGrvILLIEHDLRPFDGWVDTVTILDaDGSVAAHG 239
Cdd:PRK10418 170 DLDVVAQArilDLLESIVQKRALG--MLLVTHDMGVVARLADDVAVMS-HGRIVEQG 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-249 |
1.25e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVILLIEHDLRPFDGWVDTVTILdADGSVA 236
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL-RDGQWI 213
|
90
....*....|...
gi 1080238652 237 AHGAPEGIAVKGI 249
Cdd:PRK10982 214 ATQPLAGLTMDKI 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
154-244 |
1.30e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.63 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 154 PWALSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDL-RAPGRVILLIEHDLRPFDGWVDTVTILDAd 232
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYA- 237
|
90
....*....|..
gi 1080238652 233 GSVAAHGAPEGI 244
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-245 |
2.62e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 122 ALEFSLVEAGIVAKqsAEALSELGLSELAEKDP-WALSGGQRQRMAIA---GAVARAPEVMIFDEPAAHVDEDGRRSLFA 197
Cdd:TIGR00630 796 AYEFFEAVPSISRK--LQTLCDVGLGYIRLGQPaTTLSGGEAQRIKLAkelSKRSTGRTLYILDEPTTGLHFDDIKKLLE 873
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 198 AIRDLRAPGRVILLIEH------------DLRPFDGwvdtvtilDADGSVAAHGAPEGIA 245
Cdd:TIGR00630 874 VLQRLVDKGNTVVVIEHnldviktadyiiDLGPEGG--------DGGGTVVASGTPEEVA 925
|
|
| CbiQ |
pfam02361 |
Cobalt transport protein; This family consists of various cobalt transport proteins Most of ... |
566-732 |
3.11e-03 |
|
Cobalt transport protein; This family consists of various cobalt transport proteins Most of which are found in Cobalamin (Vitamin B12) biosynthesis operons. In Salmonella the cbiN cbiQ (product CbiQ in this family) and cbiO are likely to form an active cobalt transport system.
Pssm-ID: 396782 Cd Length: 215 Bit Score: 39.62 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 566 VVAFLALAAIAERDVRATAGKVLLVLLIGVFFGLLGWRSE----FYGGGD--ASEAVRHGIHHGLLLMAVFAGTVLVSAC 639
Cdd:pfam02361 39 LLLLLLLLVILPRFWASFLRLPLLFLLLGFIILLFLFSTEgqfvFAGGGFsiTSDGLLRGLLLALRILTLLSALLFLALT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 640 MRVEELFDAMVqRLRVPYTWCTIAISGVSIAAFLRSEIPQLTWAIRLRSMRPERSFRSGfIRATtpARIAFPLFVSAVRC 719
Cdd:pfam02361 119 TPPIELTSSLR-RLGVPLELAEILLLAYRFIPLLLEEAQRIRQAQKLRGGDSGLGIRRS-YRSL--GLLIAPLFIRALKR 194
|
170
....*....|...
gi 1080238652 720 AEKLSLTLAMRNF 732
Cdd:pfam02361 195 AERVAIAMEARGY 207
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-191 |
3.79e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 15 TAPARLRVSG-AGVRHADGRWAPdmVDLSFDFGTINAITGPVGCGKTSLAHLIAGLIPShipidHAGFVHIvdadGTERP 93
Cdd:PRK13543 7 TAPPLLAAHAlAFSRNEEPVFGP--LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHV-----ESGQIQI----DGKTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 94 VDGDRVTFVGQdpSTQVLTLRVVDDVSMALEFSLVEAGIVAKQS-AEALSELGLSELAEKDPWALSGGQRQRMAIAGAVA 172
Cdd:PRK13543 76 TRGDRSRFMAY--LGHLPGLKADLSTLENLHFLCGLHGRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*....
gi 1080238652 173 RAPEVMIFDEPAAHVDEDG 191
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLEG 172
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-327 |
4.30e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 135 KQSAEALSELGLSElaekDPWALSG----GQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRDLRAPGRVIL 210
Cdd:NF040905 118 RRARELLAKVGLDE----SPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 211 LIEHDLRPFDGWVDTVTILdADG----SVAAHGAP--EGIAVKGIAtsaapagapdastpGTGAPDR-PDLESEADAVpL 283
Cdd:NF040905 194 IISHKLNEIRRVADSITVL-RDGrtieTLDCRADEvtEDRIIRGMV--------------GRDLEDRyPERTPKIGEV-V 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1080238652 284 LAL---TGTHVARGGERILDGADLTLERGEIHALVGANGAGKsTLLA 327
Cdd:NF040905 258 FEVknwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELA 303
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
412-450 |
5.06e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 5.06e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1080238652 412 LSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIV 450
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-450 |
5.10e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 5.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1080238652 407 VSPF--VLSGGQKRRLGIFLAVAANRRLLLLDEPLAHLDSPSSRIV 450
Cdd:PTZ00265 1352 VGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
407-475 |
5.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080238652 407 VSPFVLSGG---QkrrlgIFLAV-------AANRRL-LLLDEPLAHLDSPSSRIVLDALAEYAGAGGTVVFTCHDRRVAR 475
Cdd:COG4717 554 RPVEELSRGtreQ-----LYLALrlalaelLAGEPLpLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVEL 628
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
157-220 |
7.54e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 7.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080238652 157 LSGGQRQRMAIAGAVARAPEVMIFDEPAAHVDEDGRRSLFAAIRD-LRAPGRVILLIEHDLRPFD 220
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPlLQEMGKTIFAISHDDHYFI 514
|
|
| |
