|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-298 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 545.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 4 QREKLIEVKNVKQHFDVSGG-------VVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENV 76
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGlfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 77 HGKkSRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAkSKKERMDRVHELLNTVGLNKEHANRFPHEFSG 156
Cdd:COG4608 83 TGL-SGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLA-SKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELT 236
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 237 TSEELYANPVHPYTKSLLSAIPLPDPdyERNRKRIVYD---------PSqhdyG---------------SEVPTMREIRP 292
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDP--ERRRERIVLEgdvpsplnpPS----GcrfhtrcpyaqdrcaTEEPPLREVGP 314
|
....*.
gi 506991877 293 GHFVLC 298
Cdd:COG4608 315 GHQVAC 320
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-298 |
1.22e-165 |
|
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: 462.99 E-value: 1.22e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDA---TAGEVLFDGENVHgKKSRAE 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL-KLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 LKKF-NRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAkSKKERMDRVHELLNTVGLN--KEHANRFPHEFSGGQRQR 161
Cdd:COG0444 80 LRKIrGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGL-SKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 242 YANPVHPYTKSLLSAIPLPDPDYERnRKRIVYD-PSQHDYGS-----------------EVPTMREIRPGHFVLC 298
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRR-LIPIPGEpPSLLNPPSgcrfhprcpyamdrcreEEPPLREVGPGHRVAC 312
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-263 |
2.49e-159 |
|
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: 454.36 E-value: 2.49e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREKLIEVKNVKQHFDVSG-GVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgK 79
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT-K 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 80 KSRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAkSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQR 159
Cdd:COG1123 332 LSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLL-SRAERRERVAELLERVGLPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSE 239
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|....
gi 506991877 240 ELYANPVHPYTKSLLSAIPLPDPD 263
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPSLDPA 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-261 |
1.23e-143 |
|
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: 415.24 E-value: 1.23e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGV-------VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLyDATAGEVLFDGENVHGKk 80
Cdd:COG4172 275 LLEARDLKVWFPIKRGLfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGL- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 SRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQ 160
Cdd:COG4172 353 SRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
250 260
....*....|....*....|.
gi 506991877 241 LYANPVHPYTKSLLSAIPLPD 261
Cdd:COG4172 513 VFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-269 |
5.92e-138 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 393.30 E-value: 5.92e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREKLIEVKNVKQHFDVSGG---------VVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLF 71
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 72 DGENVHgKKSRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANRFP 151
Cdd:PRK15079 81 LGKDLL-GMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 152 HEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQ 231
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 506991877 232 IVELTTSEELYANPVHPYTKSLLSAIPLPDPDYERNRK 269
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKT 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-234 |
5.71e-129 |
|
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: 366.45 E-value: 5.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKK 87
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLL-KLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-267 |
9.68e-125 |
|
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: 356.81 E-value: 9.68e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkk 87
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAkskkERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP----DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVH 247
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250 260
....*....|....*....|
gi 506991877 248 PYTKSLLSAIplpdPDYERN 267
Cdd:COG1124 233 PYTRELLAAS----LAFERA 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-272 |
1.24e-117 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 341.56 E-value: 1.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGV------VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKS 81
Cdd:PRK11308 5 LLQAIDLKKHYPVKRGLfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHgLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQR 161
Cdd:PRK11308 84 PEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLIN-TSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
250 260 270
....*....|....*....|....*....|.
gi 506991877 242 YANPVHPYTKSLLSAIPLPDPDyeRNRKRIV 272
Cdd:PRK11308 243 FNNPRHPYTQALLSATPRLNPD--DRRERIK 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-303 |
7.65e-105 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 319.11 E-value: 7.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGGV-------VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHg 78
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 79 KKSRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKERmDRVHELLNTVGLNKEHANRFPHEFSGGQ 158
Cdd:PRK10261 390 TLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAA-ARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTS 238
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 239 EELYANPVHPYTKSLLSAIPLPDPDYERNRKRIVYD--PSQ-HDYGSEVP--TMREIRPGHFVLCSEAEY 303
Cdd:PRK10261 549 RAVFENPQHPYTRKLMAAVPVADPSRQRPQRVLLSDdlPSNiHLRGEEVAavSLQCVGPGHYVAQPQSEY 618
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-263 |
2.69e-100 |
|
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: 304.30 E-value: 2.69e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATA----GEVLFDGENVHGKkS 81
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGL-S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKF-NRKMQMIFQDPYASLNPRMTVGDIIAEGIDIH-GLakSKKERMDRVHELLNTVGLN--KEHANRFPHEFSGG 157
Cdd:COG4172 83 ERELRRIrGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHrGL--SGAAARARALELLERVGIPdpERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTT 237
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260
....*....|....*....|....*.
gi 506991877 238 SEELYANPVHPYTKSLLSAIPLPDPD 263
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-255 |
1.29e-85 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 266.57 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 4 QREKLIEVKNVKQHFDVSGGVVK-------AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYdATAGEVLFDGENV 76
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 77 HGKkSRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSG 156
Cdd:PRK15134 350 HNL-NRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELT 236
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
250
....*....|....*....
gi 506991877 237 TSEELYANPVHPYTKSLLS 255
Cdd:PRK15134 509 DCERVFAAPQQEYTRQLLA 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-270 |
9.31e-83 |
|
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: 258.68 E-value: 9.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATA---GEVLFDGENVhgkkSR 82
Cdd:COG1123 2 TPLLEVRDL--SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDL----LE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 83 AELKKFNRKMQMIFQDPYASLNPrMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRI 162
Cdd:COG1123 76 LSEALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGL--SRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELY 242
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
250 260
....*....|....*....|....*...
gi 506991877 243 ANPvhpytkSLLSAIPLPDPDYERNRKR 270
Cdd:COG1123 232 AAP------QALAAVPRLGAARGRAAPA 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-256 |
2.18e-81 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 247.06 E-value: 2.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGG-----VVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGK- 79
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 80 -KSRAelkkfnRKMQMIFQDPYASLNPRMTVGDIIAEGIdIHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQ 158
Cdd:COG4167 82 yKYRC------KHIRMIFQDPNTSLNPRLNIGQILEEPL-RLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTS 238
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*...
gi 506991877 239 EELYANPVHPYTKSLLSA 256
Cdd:COG4167 235 AEVFANPQHEVTKRLIES 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
8-262 |
9.31e-81 |
|
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: 245.49 E-value: 9.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDvSGGVVKA------VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKS 81
Cdd:TIGR02769 2 LLEVRDVTHTYR-TGGLFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY-QLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDiHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQR 161
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250 260
....*....|....*....|.
gi 506991877 242 YANPvHPYTKSLLSAIPLPDP 262
Cdd:TIGR02769 239 LSFK-HPAGRNLQSAVLPEHP 258
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-268 |
1.42e-76 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 234.97 E-value: 1.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKA-----VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSR 82
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGKHqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 83 AELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDiHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRI 162
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELY 242
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250 260
....*....|....*....|....*.
gi 506991877 243 ANPvHPYTKSLLSAIPLPDPDYERNR 268
Cdd:PRK10419 241 TFS-SPAGRVLQNAVLPAFPVRRRTT 265
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-262 |
4.37e-75 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 233.43 E-value: 4.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKKF 88
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:COG1135 81 RRKIGMIFQH--FNLLSSRTVAENVALPLEIAGV--PKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHP 248
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250
....*....|....
gi 506991877 249 YTKSLLSAIPLPDP 262
Cdd:COG1135 236 LTRRFLPTVLNDEL 249
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-249 |
1.70e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 232.68 E-value: 1.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGkksraeLKK 87
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------LPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:COG3842 75 EKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGV--PKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHD----LSMvkyiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVGTPEEIYE 225
|
....*.
gi 506991877 244 NPVHPY 249
Cdd:COG3842 226 RPATRF 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-265 |
2.95e-74 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 231.15 E-value: 2.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDA---TAGEVLFDGENV- 76
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 77 -----HGKKSRAElkkfnrKMQMIFQDPYASLNPRMTVGDIIAEGIDIH-GLakSKKERMDRVHELLNTVGL--NKEHAN 148
Cdd:PRK09473 85 nlpekELNKLRAE------QISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGM--SKAEAFEESVRMLDAVKMpeARKRMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 149 RFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:PRK09473 157 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 506991877 229 RGQIVELTTSEELYANPVHPYTKSLLSAIPLPDPDYE 265
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGE 273
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-245 |
6.81e-72 |
|
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: 221.69 E-value: 6.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKK 87
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL-TLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDpYASLNPRmTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:cd03258 80 ARRRIGMIFQH-FNLLSSR-TVFENVALPLEIAGV--PKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-234 |
3.41e-68 |
|
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: 211.95 E-value: 3.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKksraelkkf 88
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03293 72 GPDRGYVFQQD--ALLPWLTVLDNVALGLELQGV--PKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVM--YRGQIVE 234
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-258 |
4.33e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 215.38 E-value: 4.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD----ATAGEVLFDGENVHGKKSRA 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGlAKSKKERMDRVHELLNTVGLnKEHANR---FPHEFSGGQRQ 160
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQ-GGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*...
gi 506991877 241 LYANPVHPYTKSLLSAIP 258
Cdd:PRK11022 241 IFRAPRHPYTQALLRALP 258
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-268 |
2.57e-67 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 213.89 E-value: 2.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKKF 88
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-TALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpYASLNPRmTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:PRK11153 81 RRQIGMIFQH-FNLLSSR-TVFDNVALPLELAG--TPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHP 248
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
250 260
....*....|....*....|.
gi 506991877 249 YTKSLL-SAIPLPDPDYERNR 268
Cdd:PRK11153 236 LTREFIqSTLHLDLPEDYLAR 256
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-249 |
3.60e-67 |
|
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: 210.96 E-value: 3.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 2 TKQREKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKS 81
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKFNRK-MQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQ 160
Cdd:cd03294 93 RKELRELRRKkISMVFQS-FA-LLPHRTVLENVAFGLEVQGV--PRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
....*....
gi 506991877 241 LYANPVHPY 249
Cdd:cd03294 248 ILTNPANDY 256
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-254 |
1.23e-66 |
|
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: 208.68 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 4 QREKLIEVKNVKQHFdvsGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRA 83
Cdd:COG1127 1 MSEPMIEVRNLTKSF---GDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT-GLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKFNRKMQMIFQDP--YASlnprMTVGDIIAEGIDIHGlAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQR 161
Cdd:COG1127 76 ELYELRRRIGMLFQGGalFDS----LTVFENVAFPLREHT-DLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 506991877 242 YANPvHPYTKSLL 254
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-258 |
2.39e-65 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 216.26 E-value: 2.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVH-------- 77
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 78 -GKKSRAELKKF-NRKMQMIFQDPYASLNPRMTVGDIIAEGIDIH-GLakSKKERMDRVHELLNTVGLNKEHA--NRFPH 152
Cdd:PRK10261 90 lSEQSAAQMRHVrGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHqGA--SREEAMVEAKRMLDQVRIPEAQTilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 EFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260
....*....|....*....|....*.
gi 506991877 233 VELTTSEELYANPVHPYTKSLLSAIP 258
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-263 |
9.59e-65 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 212.26 E-value: 9.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDA-----TAGEVLFDGENV-HGKKS 81
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLlHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKFNRkMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVhELLNTVGLnKEHANR---FPHEFSGGQ 158
Cdd:PRK15134 85 TLRGVRGNK-IAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEIL-NCLDRVGI-RQAAKRltdYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTS 238
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260
....*....|....*....|....*
gi 506991877 239 EELYANPVHPYTKSLLSAIPLPDPD 263
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-252 |
1.01e-64 |
|
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: 203.50 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvsGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKF 88
Cdd:cd03261 1 IELRGLTKSFG--GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS-GLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHGlAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03261 76 RRRMGMLFQS--GALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPvHP 248
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DP 230
|
....
gi 506991877 249 YTKS 252
Cdd:cd03261 231 LVRQ 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-246 |
1.91e-64 |
|
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: 202.85 E-value: 1.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvsGGVvkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGkksraeLKKF 88
Cdd:cd03300 1 IELENVSKFYG--GFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN------LPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03300 71 KRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
3.27e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 203.01 E-value: 3.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTkQREKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKk 80
Cdd:COG1116 1 MS-AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 sraelkkfNRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQ 160
Cdd:COG1116 79 --------GPDRGVVFQEP--ALLPWLTVLDNVALGLELRGV--PKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDV----SIQaqvvNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYR--GQIVE 234
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-232 |
2.78e-63 |
|
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: 199.25 E-value: 2.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKF 88
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 -NRKMQMIFQDPYasLNPRMTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:cd03255 80 rRRHIGFVFQSFN--LLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQI 232
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-257 |
3.40e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 199.84 E-value: 3.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsrAELKK 87
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK--KDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQdpyaSLN--PRMTVGDIIAEGIdIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIA 165
Cdd:COG1126 75 LRRKVGMVFQ----QFNlfPHLTVLENVTLAP-IKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|..
gi 506991877 246 VHPYTKSLLSAI 257
Cdd:COG1126 228 QHERTRAFLSKV 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-256 |
4.65e-63 |
|
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: 199.45 E-value: 4.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI----REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEgidIHGLAKSKKERMD-RVHELLNTVGLN-KEHANRFPHEFSGGQRQRIGIAR 166
Cdd:cd03295 74 RRKIGYVIQQ--IGLFPHMTVEENIAL---VPKLLKWPKEKIReRADELLALVGLDpAEFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
250
....*....|
gi 506991877 247 HPYTKSLLSA 256
Cdd:cd03295 229 NDFVAEFVGA 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-234 |
7.25e-63 |
|
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: 198.13 E-value: 7.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGkksraeLKKF 88
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03259 71 RRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGV--PKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-256 |
4.15e-61 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 195.39 E-value: 4.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGGV-----VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkk 80
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 sRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHgLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQ 160
Cdd:PRK15112 79 -FGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLN-TDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*.
gi 506991877 241 LYANPVHPYTKSLLSA 256
Cdd:PRK15112 237 VLASPLHELTKRLIAG 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-254 |
6.80e-61 |
|
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: 194.09 E-value: 6.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelkkf 88
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAK--SKKERMDRVHELLNTVGLNKeHANRFPHEFSGGQRQRIGIAR 166
Cdd:cd03296 73 ERNVGFVFQH-YA-LFRHMTVFDNVAFGLRVKPRSErpPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
....*...
gi 506991877 247 HPYTKSLL 254
Cdd:cd03296 230 SPFVYSFL 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-254 |
9.37e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 196.91 E-value: 9.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGE----NVHGKKsrae 84
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 lkkfnRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGI 164
Cdd:COG1118 75 -----RRVGFVFQH-YA-LFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 165 ARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
250
....*....|
gi 506991877 245 PVHPYTKSLL 254
Cdd:COG1118 225 PATPFVARFL 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
8-258 |
9.83e-61 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 196.28 E-value: 9.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD----ATAGEVLFDGENVHGKKSRA 83
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLA----KSKKERMDRVHELLNTVGLnKEHA---NRFPHEFSG 156
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKgkwwQRFKWRKKRAIELLHRVGI-KDHKdimNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELT 236
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260
....*....|....*....|..
gi 506991877 237 TSEELYANPVHPYTKSLLSAIP 258
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMP 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-234 |
3.26e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 191.80 E-value: 3.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKST-----TGrtiirLYDATAGEVLFDGENVHgKK 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnilGG-----LDRPTSGEVLIDGQDIS-SL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 SRAELKKF-NRKMQMIFQDPYasLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQR 159
Cdd:COG1136 76 SERELARLrRRHIGFVFQFFN--LLPELTALENVALPLLLAGV--SRKERRERARELLERVGL-GDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVE 234
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-241 |
5.73e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 188.73 E-value: 5.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAELKkf 88
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:COG1131 73 -RRIGYVPQEP--ALYPDLTVRENLRFFARLYGL--PRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
23-259 |
1.82e-58 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 191.60 E-value: 1.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 23 GVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKKFNR-KMQMIFQDpyA 101
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI-MKQSPVELREVRRkKIGMVFQQ--F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 SLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPI 181
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGW--PEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 182 SALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSLLSAIPL 259
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDL 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-244 |
3.29e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 187.19 E-value: 3.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFDvsGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELK 86
Cdd:COG3638 1 PMLELRNLSKRYP--GGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV-TALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNRKMQMIFQDPYasLNPRMTV---------GDiiaegidiHGLAKS------KKERmDRVHELLNTVGLnKEHANRFP 151
Cdd:COG3638 77 RLRRRIGMIFQQFN--LVPRLSVltnvlagrlGR--------TSTWRSllglfpPEDR-ERALEALERVGL-ADKAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 152 HEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQ 231
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
250 260
....*....|....*....|.
gi 506991877 232 IV------ELTTS--EELYAN 244
Cdd:COG3638 225 VVfdgppaELTDAvlREIYGG 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-247 |
1.42e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 188.74 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkf 88
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:COG3839 75 -RNIAMVFQS-YA-LYPHMTVYENIAFPLKLRKV--PKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHD----LSMvkyiSDRIGVMYRGQIVELTTSEELYAN 244
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDR 224
|
...
gi 506991877 245 PVH 247
Cdd:COG3839 225 PAN 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-241 |
2.03e-57 |
|
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: 184.69 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqhfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDA-----TAGEVLFDGENVHGKK-SR 82
Cdd:cd03260 1 IELRDL----NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 83 AELKkfnRKMQMIFQDPyaslNP-RMTVGDIIAEGIDIHGLaKSKKERMDRVHELLNTVGLNKEHANR-FPHEFSGGQRQ 160
Cdd:cd03260 77 LELR---RRVGMVFQKP----NPfPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 506991877 241 L 241
Cdd:cd03260 227 I 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-245 |
3.46e-57 |
|
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: 184.07 E-value: 3.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:COG1122 1 IELENL--SFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI----TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYASL-NPrmTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:COG1122 74 RRKVGLVFQNPDDQLfAP--TVEEDVAFGPENLGL--PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-231 |
6.30e-55 |
|
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: 176.61 E-value: 6.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKKF 88
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGDIIAEGIdihglakskkermdrvhellntvglnkehanrfphefSGGQRQRIGIARAL 168
Cdd:cd03229 75 RRRIGMVFQDF--ALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQ 231
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-258 |
1.74e-53 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 177.69 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRL----YDATAGEVLFDGENVHGKKSRA 83
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDihglAKSKKER-MDRVH-------ELLNTVGLnKEHAN---RFPH 152
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIP----GWTYKGRwWQRFGwrkrraiELLHRVGI-KDHKDamrSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 EFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260
....*....|....*....|....*.
gi 506991877 233 VELTTSEELYANPVHPYTKSLLSAIP 258
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-242 |
5.22e-53 |
|
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: 173.52 E-value: 5.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKF 88
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN-KLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGDIIAEG-IDIHGLAKS-----KKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRI 162
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLENVLSGrLGRRSTWRSlfglfPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV------ELT 236
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVfdgppaELT 233
|
....*...
gi 506991877 237 TS--EELY 242
Cdd:cd03256 234 DEvlDEIY 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-231 |
7.80e-53 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 172.27 E-value: 7.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsraeLKKFN 89
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 90 RKMQMIFQDPYASL-NPrmTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03225 75 RKVGLVFQNPDDQFfGP--TVEEEVAFGLENLGL--PEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQ 231
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-232 |
5.83e-52 |
|
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: 170.02 E-value: 5.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsrAELKKF 88
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK--KNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEG-IDIHGlaKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:cd03262 75 RQKVGMVFQQ--FNLFPHLTVLENITLApIKVKG--MSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-235 |
7.22e-52 |
|
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: 169.74 E-value: 7.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKKF 88
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV------TDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03301 71 DRDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVPKDEIDE--RVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVEL 235
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-247 |
2.48e-51 |
|
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: 169.84 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkk 87
Cdd:COG1120 1 MLEAENL--SVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYASLNprMTVGDIIAEGIDIH--GLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIA 165
Cdd:COG1120 73 LARRIAYVPQEPPAPFG--LTVRELVALGRYPHlgLFGRPSAEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV------ELTTSE 239
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaqgppeEVLTPE 229
|
250
....*....|.
gi 506991877 240 ---ELYANPVH 247
Cdd:COG1120 230 lleEVYGVEAR 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-234 |
7.15e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 167.54 E-value: 7.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKF 88
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:COG2884 78 RRRIGVVFQD--FRLLPDRTVYENVALPLRVTG--KSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKeKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-300 |
2.15e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 171.17 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSggvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKK 87
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAKSkkERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:PRK11607 89 YQRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPKA--EIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 168 LAVEPEFIIADEPISALDVSI----QAQVVNLLKKLqkekGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 244 NPVHPYTKSLLSAIPLPDPDY-ERNRKRIVYD------PSQHDYGSE----VPTMREIRPGHFVLCSE 300
Cdd:PRK11607 240 HPTTRYSAEFIGSVNVFEGVLkERQEDGLVIDspglvhPLKVDADASvvdnVPVHVALRPEKIMLCEE 307
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-243 |
6.45e-50 |
|
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: 165.93 E-value: 6.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKK 87
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI-TKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDpyASLNPRMTV------GDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQR 161
Cdd:TIGR02315 77 LRRRIGMIFQH--YNLIERLTVlenvlhGRLGYKPTWRSLLGRFSEEDKERALSALERVGL-ADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
..
gi 506991877 242 YA 243
Cdd:TIGR02315 234 DD 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-180 |
1.47e-49 |
|
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: 161.66 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKksraELKKFNRKMQMIFQDPyaSLNPRM 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD----ERKSLRKEIGYVFQDP--QLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 108 TVGDIIAEGIDIHGLAKS-KKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEP 180
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKReKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-251 |
3.98e-49 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 164.05 E-value: 3.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREKL---IEVKNvkqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-----ATAGEVLFD 72
Cdd:COG1117 1 MTAPASTLepkIEVRN----LNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 73 GENVHGKK-SRAELKkfnRKMQMIFQDPyaslNP-RMTVGDIIAEGIDIHGLaKSKKERMDRVHELLNTVGLNKEHANRF 150
Cdd:COG1117 77 GEDIYDPDvDVVELR---RRVGMVFQKP----NPfPKSIYDNVAYGLRLHGI-KSKSELDEIVEESLRKAALWDEVKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 151 ---PHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVM 227
Cdd:COG1117 149 kksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|....
gi 506991877 228 YRGQIVELTTSEELYANPVHPYTK 251
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-245 |
1.62e-48 |
|
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: 161.84 E-value: 1.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelKKF 88
Cdd:cd03219 1 LEVRGLTKRF---GGL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGD--IIA------EGIDIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQ 160
Cdd:cd03219 74 RLGIGRTFQIP--RLFPELTVLEnvMVAaqartgSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 506991877 241 LYANP 245
Cdd:cd03219 230 VRNNP 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-250 |
3.33e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 165.12 E-value: 3.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREK--LIEVKNVKQHFDVSggvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHG 78
Cdd:PRK09452 5 NKQPSSLspLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 79 KKsrAElkkfNRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQ 158
Cdd:PRK09452 81 VP--AE----NRHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKTPAAEITP--RVMEALRMVQL-EEFAQRKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHD----LSMvkyiSDRIGVMYRGQIVE 234
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQ 225
|
250
....*....|....*.
gi 506991877 235 LTTSEELYANPVHPYT 250
Cdd:PRK09452 226 DGTPREIYEEPKNLFV 241
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-245 |
6.98e-48 |
|
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: 163.05 E-value: 6.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 43 LVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKKFNRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGL 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 123 AKSkkERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKE 202
Cdd:TIGR01187 73 PRA--EIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 506991877 203 KGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-254 |
1.03e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 159.87 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsrAELKK 87
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK--VDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYasLNPRMTVGDIIAEG-IDIHGLAKSKKERMDRvhELLNTVGLnKEHANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK09493 75 IRQEAGMVFQQFY--LFPHLTALENVMFGpLRVRGASKEEAEKQAR--ELLAKVGL-AERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
....*...
gi 506991877 247 HPYTKSLL 254
Cdd:PRK09493 229 SQRLQEFL 236
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-256 |
6.70e-46 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 155.63 E-value: 6.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDA----TAGEVLFDGENVHGKKSRAelkkfnRKMQMIFQDPYASL 103
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRG------RKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 NPRMTVGDIIAEGidihGLAKSKKERMDRVHELLNTVGLNKEH--ANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPI 181
Cdd:PRK10418 93 NPLHTMHTHARET----CLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 182 SALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSLLSA 256
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-232 |
8.31e-46 |
|
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: 152.94 E-value: 8.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKkf 88
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVK-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDPyaSLNPRMTVGDIIaegidihglakskkermdrvhellntvglnkehanrfphEFSGGQRQRIGIARAL 168
Cdd:cd03230 73 -RRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-245 |
9.81e-46 |
|
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: 155.20 E-value: 9.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelkK 87
Cdd:COG0411 4 LLEVRGLTKRF---GGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRK-MQMIFQDPyaSLNPRMTVGD-------------IIAEGIDIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHE 153
Cdd:COG0411 76 IARLgIARTFQNP--RLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGL-ADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 154 FSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
250
....*....|..
gi 506991877 234 ELTTSEELYANP 245
Cdd:COG0411 233 AEGTPAEVRADP 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-257 |
6.68e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 157.12 E-value: 6.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELK 86
Cdd:PRK10070 23 KYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNRK-MQMIFQDpyASLNPRMTVGDIIAEGIDIHGLAKSkkERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIA 165
Cdd:PRK10070 102 EVRRKkIAMVFQS--FALMPHMTVLDNTAFGMELAGINAE--ERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK10070 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
250
....*....|..
gi 506991877 246 VHPYTKSLLSAI 257
Cdd:PRK10070 257 ANDYVRTFFRGV 268
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-244 |
1.40e-44 |
|
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: 151.93 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksrAELKK 87
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-----KEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYasLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARA 167
Cdd:COG4555 72 ARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL--FDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-245 |
1.54e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 155.24 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelkkf 88
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIhgLAKSKKERMD----RVHELLNTVGLnkEH-ANRFPHEFSGGQRQRIG 163
Cdd:PRK10851 73 DRKVGFVFQH-YA-LFRHMTVFDNIAFGLTV--LPRRERPNAAaikaKVTQLLEMVQL--AHlADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 164 IARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
..
gi 506991877 244 NP 245
Cdd:PRK10851 227 EP 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-249 |
1.59e-43 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 158.07 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL----RQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPY---ASL--NprMTVGDiiaEGIDihglakskkerMDRVHELLNTVGLNkEHANRFPH----------- 152
Cdd:COG2274 548 RRQIGVVLQDVFlfsGTIreN--ITLGD---PDAT-----------DEEIIEAARLAGLH-DFIEALPMgydtvvgeggs 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 EFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYRGQI 232
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIR-LADRIIVLDKGRI 687
|
250
....*....|....*..
gi 506991877 233 VELTTSEELYANPVHPY 249
Cdd:COG2274 688 VEDGTHEELLARKGLYA 704
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-246 |
2.29e-43 |
|
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: 148.64 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKKFNRKMQMIFQDpYAsLNPRMTV 109
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI------TNLPPEKRDISYVPQN-YA-LFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDIHGLAKSKKERmdRVHELlnTVGLNKEHA-NRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSI 188
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIER--KVLEI--AEMLGIDHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 189 QAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-245 |
2.79e-43 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 151.80 E-value: 2.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQreKLIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKK 80
Cdd:PRK11432 1 MTQK--NFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--TH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 SRAElkkfNRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNKeHANRFPHEFSGGQRQ 160
Cdd:PRK11432 73 RSIQ----QRDICMVFQS-YA-LFPHMSLGENVGYGLKMLGV--PKEERKQRVKEALELVDLAG-FEDRYVDQISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
....*
gi 506991877 241 LYANP 245
Cdd:PRK11432 224 LYRQP 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-234 |
6.58e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 147.47 E-value: 6.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqhfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEV-----LFDGENVHGKKSRA 83
Cdd:PRK11124 3 IQLNGI----NCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKkfnRKMQMIFQDpYaSLNPRMTVGD-IIAEGIDIHGLakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRI 162
Cdd:PRK11124 79 ELR---RNVGMVFQQ-Y-NLWPHLTVQQnLIEAPCRVLGL--SKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-234 |
1.62e-42 |
|
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: 145.96 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKK 87
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLS-KLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 F-NRKMQMIFQdpYASLNPRMTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLNKEhANRFPHEFSGGQRQRIGIAR 166
Cdd:TIGR02211 80 LrNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGK--KSVKEAKERAYEMLEKVGLEHR-INHRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYIsDRIGVMYRGQIVE 234
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-245 |
2.51e-42 |
|
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: 147.21 E-value: 2.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTtgrtIIRLYDA----TAGEVLFDGENVHGKKSRaELKKFNRKMQMIFQDPYA 101
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKST----LIQHLNGllkpTSGTVTIDGRDITAKKKK-KLKDLRKKVGLVFQFPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 SLNpRMTVGDIIAEGIdiHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPI 181
Cdd:TIGR04521 94 QLF-EETVYKDIAFGP--KNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 182 SALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-257 |
8.58e-42 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 144.97 E-value: 8.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 23 GVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKK----SRAELKKFNR-KMQMIFQ 97
Cdd:TIGR02323 14 GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlSEAERRRLMRtEWGFVHQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 98 DPYASLNPRMTVGDIIAEGIDIHGLAKSKKERmDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIA 177
Cdd:TIGR02323 94 NPRDGLRMRVSAGANIGERLMAIGARHYGNIR-ATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 178 DEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSLLSAI 257
Cdd:TIGR02323 173 DEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-232 |
1.22e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYAslnPRMTVGDIIAEGIDIhglaKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:COG4619 73 RRQVAYVPQEPAL---WGGTVRDNLPFPFQL----RERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-257 |
3.05e-41 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 143.91 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvHGKKSRAELKK 87
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQM------IFQDPYASLNPRMTVGDIIAEGI---------DIHGLAKSKKERM----DRVHELlntvglnkehan 148
Cdd:PRK11701 81 AERRRLLrtewgfVHQHPRDGLRMQVSAGGNIGERLmavgarhygDIRATAGDWLERVeidaARIDDL------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 149 rfPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:PRK11701 149 --PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260
....*....|....*....|....*....
gi 506991877 229 RGQIVELTTSEELYANPVHPYTKSLLSAI 257
Cdd:PRK11701 227 QGRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-241 |
4.20e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.92 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqhfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSR-Ae 84
Cdd:COG1121 4 MPAIELENL----TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRiG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 lkkfnrkmqmifqdpY----ASLNPR--MTVGDIIAEGIDIH-GLAK--SKKERmDRVHELLNTVGLnKEHANRFPHEFS 155
Cdd:COG1121 79 ---------------YvpqrAEVDWDfpITVRDVVLMGRYGRrGLFRrpSRADR-EAVDEALERVGL-EDLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 156 GGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVEL 235
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHG 220
|
....*.
gi 506991877 236 TTSEEL 241
Cdd:COG1121 221 PPEEVL 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-234 |
4.72e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 143.46 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKS-RAelkk 87
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAdRG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fnrkmqMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAKSkkERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:COG4525 80 ------VVFQK-DA-LLPWLNVLDNVAFGLRLRGVPKA--ERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVM--YRGQIVE 234
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-243 |
6.12e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 143.72 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDvSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDG-----ENVHGKK 80
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 sraelkkfnRKMQMIFQDPYASLnPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQ 160
Cdd:PRK13650 81 ---------HKIGMVFQNPDNQF-VGATVEDDVAFGLENKGI--PHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKyISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
...
gi 506991877 241 LYA 243
Cdd:PRK13650 227 LFS 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-231 |
7.38e-41 |
|
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: 139.83 E-value: 7.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL----RDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPY---ASlnprmtvgdiIAEGIdihglakskkermdrvhellntvglnkehanrfpheFSGGQRQRIGIA 165
Cdd:cd03228 75 RKNIAYVPQDPFlfsGT----------IRENI------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYRGQ 231
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-251 |
1.24e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 141.69 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqhfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGE--NVHGKKSRAELK 86
Cdd:COG4161 3 IQLKNI----NCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNRKMQMIFQDpYaSLNPRMTVGD-IIAEGIDIHGLakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIA 165
Cdd:COG4161 79 LLRQKVGMVFQQ-Y-NLWPHLTVMEnLIEAPCKVLGL--SKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELyanp 245
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF---- 228
|
....*.
gi 506991877 246 VHPYTK 251
Cdd:COG4161 229 TQPQTE 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-243 |
1.58e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGEnvhgKKSRAEL 85
Cdd:PRK13635 3 EEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM----VLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFNRKMQMIFQdpyaslNPR-----MTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQ 160
Cdd:PRK13635 77 WDVRRQVGMVFQ------NPDnqfvgATVQDDVAFGLENIGV--PREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEE 240
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE 226
|
...
gi 506991877 241 LYA 243
Cdd:PRK13635 227 IFK 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-224 |
3.02e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 139.98 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVKqhfdVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSR----AEL 85
Cdd:cd03235 1 EVEDLT----VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyvPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFNRKMqmifqdpyaslnpRMTVGDIIAEGIDIH--GLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIG 163
Cdd:cd03235 77 RSIDRDF-------------PISVRDVVLMGLYGHkgLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 164 IARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRI 224
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-251 |
3.04e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 141.20 E-value: 3.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-----ATAGEVLFDGENVHgkksRA 83
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIF----KM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKFNRKMQMIFQDPYASlnPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANRF---PHEFSGGQRQ 160
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|.
gi 506991877 241 LYANPVHPYTK 251
Cdd:PRK14247 232 VFTNPRHELTE 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-233 |
3.74e-40 |
|
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: 139.74 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIyRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDpyASLNPRMTV 109
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDIHglakSKKERMDRVHELLNTVGLNKEhANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQ 189
Cdd:cd03297 93 RENLAFGLKRK----RNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 506991877 190 AQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-256 |
1.18e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 139.55 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREKLIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKK 80
Cdd:COG4598 1 MTDTAPPALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 SR---------AELKKFNRKMQMIFQdpyaSLN--PRMTVGDIIAEGiDIHGLAKSKKERMDRVHELLNTVGL-NKEHAn 148
Cdd:COG4598 77 DRdgelvpadrRQLQRIRTRLGMVFQ----SFNlwSHMTVLENVIEA-PVHVLGRPKAEAIERAEALLAKVGLaDKRDA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 149 rFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:COG4598 151 -YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLH 228
|
250 260
....*....|....*....|....*...
gi 506991877 229 RGQIVELTTSEELYANPVHPYTKSLLSA 256
Cdd:COG4598 229 QGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-234 |
1.20e-39 |
|
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: 138.12 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKKF 88
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY------QKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVgdiiAEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03268 71 LRRIGALIEAP--GFYPNLTA----RENLRLLARLLGIRKK--RIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-233 |
2.11e-39 |
|
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: 136.41 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKfn 89
Cdd:cd03214 1 EVENL--SVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-SLSPKELAR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 90 rkmqmifqdpyaslnpRMTVgdiiaegidihglakskkermdrVHELLNTVGLnkEH-ANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03214 74 ----------------KIAY-----------------------VPQALELLGL--AHlADRPFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-241 |
5.47e-39 |
|
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: 136.73 E-value: 5.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksRAELKKF 88
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-----VREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03265 72 RRRIGIVFQDL--SVDDELTGWENLYIHARLYGV--PGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-231 |
5.47e-39 |
|
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: 134.68 E-value: 5.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksRAELKKFN 89
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 90 RKMQMIFQdpyaslnprmtvgdiiaegidihglakskkermdrvhellntvglnkehanrfpheFSGGQRQRIGIARALA 169
Cdd:cd00267 73 RRIGYVPQ--------------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 170 VEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQ 231
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-241 |
1.86e-38 |
|
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: 142.25 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 4 QREKLIEVKNVKQHF-DVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGE--VLFDGENVHGKK 80
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 SRAELK-KFNRKMQMIFQDpyASLNPRMTVGDIIAEGIdihGLAKSKK-ERMDRVHeLLNTVGLNKEHA----NRFPHEF 154
Cdd:TIGR03269 355 PGPDGRgRAKRYIGILHQE--YDLYPHRTVLDNLTEAI---GLELPDElARMKAVI-TLKMVGFDEEKAeeilDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*..
gi 506991877 235 LTTSEEL 241
Cdd:TIGR03269 509 IGDPEEI 515
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-233 |
2.12e-38 |
|
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: 133.32 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGEnvhgkksraelkkf 88
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nrkmqmifqdPYASLNPRmtvgDIIAEGIdihglakskkeRMdrVHELlntvglnkehanrfphefSGGQRQRIGIARAL 168
Cdd:cd03216 63 ----------EVSFASPR----DARRAGI-----------AM--VYQL------------------SVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-233 |
2.30e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 137.16 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 -----NRkmqmifqdpyaSLNPRMTVGDII---AEgidIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQ 160
Cdd:COG4152 74 gylpeER-----------GLYPKMKVGEQLvylAR---LKGL--SKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 161 RIGIARALAVEPEFIIADEPISALD-VSiqaqvVNLLKKL---QKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-243 |
2.41e-38 |
|
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: 135.44 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGkksrAELKKF 88
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD----YTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYaslnprmTVGDIIAEGIdIHGLAKSKKERMDRVHELLNTvglnKEHANRFPHEF-----------SGG 157
Cdd:cd03251 75 RRQIGLVSQDVF-------LFNDTVAENI-AYGRPGATREEVEEAARAANA----HEFIMELPEGYdtvigergvklSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTT 237
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
....*.
gi 506991877 238 SEELYA 243
Cdd:cd03251 220 HEELLA 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-232 |
3.45e-38 |
|
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: 134.46 E-value: 3.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAeLKKF 88
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-IPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLNKEHaNRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03292 77 RRKIGVVFQD--FRLLPDRNVYENVAFALEVTG--VPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKeKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-244 |
8.39e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 141.07 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:COG1132 340 IEFENV--SFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----RDLTLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPY---ASL-------NPRMTVGDII--AEGIDIHglakskkermDRVHEL---LNTV----GLNkehanr 149
Cdd:COG1132 413 RRQIGVVPQDTFlfsGTIrenirygRPDATDEEVEeaAKAAQAH----------EFIEALpdgYDTVvgerGVN------ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 150 fpheFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYR 229
Cdd:COG1132 477 ----LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIR-NADRILVLDD 549
|
250
....*....|....*
gi 506991877 230 GQIVELTTSEELYAN 244
Cdd:COG1132 550 GRIVEQGTHEELLAR 564
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-255 |
1.52e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.11 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKF 88
Cdd:PRK11264 4 IEVKNLVKKF--HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQ----MIFQDpyASLNPRMTVGDIIAEG-IDIHGLAKSkkERMDRVHELLNTVGLN-KEhaNRFPHEFSGGQRQRI 162
Cdd:PRK11264 80 IRQLRqhvgFVFQN--FNLFPHRTVLENIIEGpVIVKGEPKE--EATARARELLAKVGLAgKE--TSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELY 242
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|...
gi 506991877 243 ANPVHPYTKSLLS 255
Cdd:PRK11264 233 ADPQQPRTRQFLE 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-245 |
2.63e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.13 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksraELKKF 88
Cdd:PRK11650 4 LKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN------ELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAKSkkERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:PRK11650 75 DRDIAMVFQN-YA-LYPHMSVRENMAYGLKIRGMPKA--EIEERVAEAARILELE-PLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-244 |
6.73e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.25 E-value: 6.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsrAELKKFNRKMQMIFQDPYASLNP 105
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK--VKLSDIRKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RmTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNKE-HANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISAL 184
Cdd:PRK13637 99 E-TIEKDIAFGPINLGL--SEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 185 DVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-255 |
1.31e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.50 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvSGGVVKAVNdisFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-----ATAGEVLFDGENVHGKKSRA 83
Cdd:PRK14267 5 IETVNLRVYYG-SNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 elKKFNRKMQMIFQdpYASLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANR---FPHEFSGGQRQ 160
Cdd:PRK14267 81 --IEVRREVGMVFQ--YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
250
....*....|....*
gi 506991877 241 LYANPVHPYTKSLLS 255
Cdd:PRK14267 235 VFENPEHELTEKYVT 249
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-255 |
1.07e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 129.13 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-----ATAGEVLFDGENVHGKKS-RAELKKfnrKMQMIFQDP 99
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTdTVDLRK---EIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 100 yaslNP-RMTVGDIIAEGIDIHGLakSKKERMDR-VHELLNTVGLNKEHANRFpHE----FSGGQRQRIGIARALAVEPE 173
Cdd:PRK14239 96 ----NPfPMSIYENVVYGLRLKGI--KDKQVLDEaVEKSLKGASIWDEVKDRL-HDsalgLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSL 253
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDY 246
|
..
gi 506991877 254 LS 255
Cdd:PRK14239 247 IS 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-240 |
1.21e-35 |
|
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: 128.32 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 1 MTKQREKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHG-- 78
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 79 KKSRAELKkfNRKMQMIFQdpyaS--LNPRMT----VGdIIAEgidihgLAkSKKERMDRVHELLNTVGLnKEHANRFPH 152
Cdd:COG4181 81 EDARARLR--ARHVGFVFQ----SfqLLPTLTalenVM-LPLE------LA-GRRDARARARALLERVGL-GHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 EFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQI 232
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
....*...
gi 506991877 233 VELTTSEE 240
Cdd:COG4181 225 VEDTAATA 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-244 |
1.29e-35 |
|
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: 134.89 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:COG4988 337 IELEDV--SFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL----SDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYasLnPRMTVGDIIAegidihgLAKSKKERmDRVHELLNTVGLNkEHANRFPH-------E----FSGG 157
Cdd:COG4988 410 RRQIAWVPQNPY--L-FAGTIRENLR-------LGRPDASD-EELEAALEAAGLD-EFVAALPDgldtplgEggrgLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYRGQIVELTT 237
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
....*..
gi 506991877 238 SEELYAN 244
Cdd:COG4988 555 HEELLAK 561
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-244 |
4.66e-35 |
|
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: 126.89 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksRAELKKF 88
Cdd:cd03249 1 IEFKNVSFRYP-SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR----DLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDP--YAslnprMTVGDIIAegidiHGLAKSKKERMDRV------HELLNTvglnkehanrFPHEF------ 154
Cdd:cd03249 76 RSQIGLVSQEPvlFD-----GTIAENIR-----YGKPDATDEEVEEAakkaniHDFIMS----------LPDGYdtlvge 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 -----SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkeKGLTYLFIAHDLSMVKYiSDRIGVMYR 229
Cdd:cd03249 136 rgsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQN 212
|
250
....*....|....*
gi 506991877 230 GQIVELTTSEELYAN 244
Cdd:cd03249 213 GQVVEQGTHDELMAQ 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-241 |
8.73e-35 |
|
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: 125.70 E-value: 8.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksRAELKKF 88
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----RTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVgdiiAEGIDIHGLAK--SKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIAR 166
Cdd:cd03263 74 RQSLGYCPQF--DALFDELTV----REHLRFYARLKglPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-233 |
1.71e-34 |
|
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: 124.68 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelkkfnRKMQMIFQDPYASLNp 105
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR-------KSIGYVMQDVDYQLF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAEGIDIHGLAKSKKErmdrvhELLNTVGLNKEHaNRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:cd03226 86 TDSVREELLLGLKELDAGNEQAE------TVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506991877 186 VSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03226 159 YKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-233 |
1.75e-34 |
|
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: 124.79 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAELKk 87
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fnRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHGLAksKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARA 167
Cdd:cd03266 78 --RRLGFVSDS--TGLYDRLTARENLEYFAGLYGLK--GDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-256 |
2.47e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.87 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvHGKKSRAElkkfnRKMQMIFQDpyASLNPRMTVG 110
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAE-----RPVSMLFQE--NNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 111 DIIAEGIDiHGLAKSKKERmDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQA 190
Cdd:COG3840 90 QNIGLGLR-PGLKLTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 191 QVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSLLSA 256
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-233 |
2.50e-34 |
|
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: 124.32 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksraelkKF 88
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----------DI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03269 67 AARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGL--KKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 169 AVEPEFIIADEPISALDvsiqaqVVN--LLKKL---QKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03269 144 IHDPELLILDEPFSGLD------PVNveLLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
30-236 |
2.80e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.93 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQdpYASLNPRMTV 109
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLNKEHANRfPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQ 189
Cdd:PRK11629 105 LENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506991877 190 AQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGvMYRGQIV-ELT 236
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTaELS 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-251 |
2.83e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 125.53 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSggvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATA-----GEVLFDGENVHGKksRA 83
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYER--RV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKFNRKMQMIFQDPyaSLNPrMTVGDIIAEGIDIHGLaKSKKERMDRVHELLNTVGLNKEHANRFPH---EFSGGQRQ 160
Cdd:PRK14258 82 NLNRLRRQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGW-RPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYR-----GQIVEL 235
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEF 237
|
250
....*....|....*.
gi 506991877 236 TTSEELYANPVHPYTK 251
Cdd:PRK14258 238 GLTKKIFNSPHDSRTR 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-255 |
3.23e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.47 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVH-GKKSRAELKKFNRK--------MQMIFQdpYA 101
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlVRDKDGQLKVADKNqlrllrtrLTMVFQ--HF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 SLNPRMTVGDIIAEG-IDIHGLakSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEP 180
Cdd:PRK10619 102 NLWSHMTVLENVMEApIQVLGL--SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 181 ISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSLLS 255
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-284 |
3.23e-34 |
|
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: 124.50 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGEnvhgkksraELKKFNRKMQMIFQDpyASLNPRM 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---------QITEPGPDRMVVFQN--YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 108 TVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVS 187
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 188 IQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVM------YRGQIVElttseelyanpvhpytksllsaIPLPD 261
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE----------------------VPFPR 206
|
250 260
....*....|....*....|...
gi 506991877 262 PdyeRNRKRIVYDPSQHDYGSEV 284
Cdd:TIGR01184 207 P---RDRLEVVEDPSYYDLRNEA 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-245 |
5.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.19 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKK 87
Cdd:PRK13639 1 ILETRDL--KYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI--KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYASL-NPrmTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK13639 76 VRKTVGIVFQNPDDQLfAP--TVEEDVAFGPLNLGLSKEEVEK--RVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-244 |
7.29e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 7.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 2 TKQREKLIEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkS 81
Cdd:PRK13632 1 IKNKSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKFNRKMQMIFQdpyaslNPR-----MTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRFPHEFSG 156
Cdd:PRK13632 75 KENLKEIRKKIGIIFQ------NPDnqfigATVEDDIAFGLENKKV--PPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVkYISDRIGVMYRGQIVELT 236
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQG 224
|
....*...
gi 506991877 237 TSEELYAN 244
Cdd:PRK13632 225 KPKEILNN 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-241 |
1.12e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 123.10 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKf 88
Cdd:cd03254 3 IEFENV--NFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nrKMQMIFQDPYaslnprmTVGDIIAEGIDIHGLakskKERMDRVHELLNTVGLN----------KEHANRFPHEFSGGQ 158
Cdd:cd03254 78 --MIGVVLQDTF-------LFSGTIMENIRLGRP----NATDEEVIEAAKEAGAHdfimklpngyDTVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTS 238
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
...
gi 506991877 239 EEL 241
Cdd:cd03254 222 DEL 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-243 |
1.56e-33 |
|
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: 123.11 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03253 1 IEFENV--TFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDP------------YAslNPRMTVGDII--AEGIDIHGLAKSKKERMDRVhellntVGlnkEHANRFphef 154
Cdd:cd03253 74 RRAIGVVPQDTvlfndtigynirYG--RPDATDEEVIeaAKAAQIHDKIMRFPDGYDTI------VG---ERGLKL---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVkYISDRIGVMYRGQIVE 234
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTI-VNADKIIVLKDGRIVE 215
|
....*....
gi 506991877 235 LTTSEELYA 243
Cdd:cd03253 216 RGTHEELLA 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-245 |
2.25e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.18 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFdvsGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRael 85
Cdd:PRK11300 3 QPLLSVSGLMMRF---GGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 kKFNRK-MQMIFQDpyASLNPRMTVGD--IIAE------GIdIHGLAK------SKKERMDRVHELLNTVGLnKEHANRF 150
Cdd:PRK11300 76 -QIARMgVVRTFQH--VRLFREMTVIEnlLVAQhqqlktGL-FSGLLKtpafrrAESEALDRAATWLERVGL-LEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 151 PHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRG 230
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250
....*....|....*
gi 506991877 231 QIVELTTSEELYANP 245
Cdd:PRK11300 231 TPLANGTPEEIRNNP 245
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-245 |
2.67e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 128.35 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKkf 88
Cdd:COG4987 334 LELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR-DLDEDDLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDPY---ASL-------NPRMTVGDIIA--EGIDIHGLAKSKKERmdrvhelLNT-VGlnkEHANRFphefS 155
Cdd:COG4987 409 -RRIAVVPQRPHlfdTTLrenlrlaRPDATDEELWAalERVGLGDWLAALPDG-------LDTwLG---EGGRRL----S 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 156 GGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLtyLFIAHDLSMVKYIsDRIGVMYRGQIVEL 235
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRIVEQ 550
|
250
....*....|
gi 506991877 236 TTSEELYANP 245
Cdd:COG4987 551 GTHEELLAQN 560
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-245 |
3.20e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 125.53 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 12 KNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksraELKKFNRK 91
Cdd:PRK11000 7 RNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN------DVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 92 MQMIFQDpYAsLNPRMTVGDIIAEGIDIHGLAKSK-KERMDRVHELLNTVGLnkehANRFPHEFSGGQRQRIGIARALAV 170
Cdd:PRK11000 77 VGMVFQS-YA-LYPHLSVAENMSFGLKLAGAKKEEiNQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 171 EPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-249 |
4.76e-33 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 124.84 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDpyASLNPRMTV 109
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDiHGLAKSKKERMDRVHELLNTvglnkEH-ANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSI 188
Cdd:TIGR02142 93 RGNLRYGMK-RARPSERRISFERVIELLGI-----GHlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 189 QAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPY 249
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-244 |
5.48e-33 |
|
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: 121.00 E-value: 5.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelKKF 88
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH---ERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLAKsKKERMDRVHEL---LntvglnKEHANRFPHEFSGGQRQRIGIA 165
Cdd:cd03224 74 RAGIGYVPEGR--RIFPELTVEENLLLGAYARRRAK-RKARLERVYELfprL------KERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-246 |
5.81e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.60 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTI--IRLYDATAGEVL-FDGENVhGKKSRAEL 85
Cdd:PRK13640 6 VEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSKItVDGITL-TAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKfnrKMQMIFQDPYASLnPRMTVGDIIAEGIDIHGLAKSKKERMdrVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIA 165
Cdd:PRK13640 83 RE---KVGIVFQNPDNQF-VGATVGDDVAFGLENRAVPRPEMIKI--VRDVLADVGM-LDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKyISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
|
.
gi 506991877 246 V 246
Cdd:PRK13640 235 E 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-234 |
6.22e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 6.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKk 87
Cdd:COG1129 4 LLEMRGISKSF---GGV-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fnRKMQMIFQDPyaSLNPRMTVgdiiAEGIDI------HGLAKSKKERmDRVHELLNTVGLNkEHANRFPHEFSGGQRQR 161
Cdd:COG1129 79 --AGIAIIHQEL--NLVPNLSV----AENIFLgreprrGGLIDWRAMR-RRARELLARLGLD-IDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-243 |
3.03e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.97 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsraeLK 86
Cdd:PRK13642 3 KILEVENLVFKYEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN----VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNRKMQMIFQDPYASLnPRMTVGDIIAEGIDIHGLAKskKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK13642 78 NLRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGIPR--EEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-233 |
3.47e-32 |
|
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: 118.85 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvsGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKkf 88
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDPADLR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDP---YASLNPRMTVGDIIAEgidihglakskKERMDRVHELLntvGLNkEHANRFPHEF----------- 154
Cdd:cd03245 78 -RNIGYVPQDVtlfYGTLRDNITLGAPLAD-----------DERILRAAELA---GVT-DFVNKHPNGLdlqigergrgl 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYRGQIV 233
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-243 |
4.64e-32 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 125.21 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsraeL 85
Cdd:TIGR02203 328 RGDVEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT----L 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFNRKMQMIFQDPyaslnprMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTvglnKEHANRFPHEF----------- 154
Cdd:TIGR02203 402 ASLRRQVALVSQDV-------VLFNDTIANNIAYGRTEQADRAEIERALAAAYA----QDFVDKLPLGLdtpigengvll 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVE 234
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
....*....
gi 506991877 235 LTTSEELYA 243
Cdd:TIGR02203 548 RGTHNELLA 556
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-233 |
1.19e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 117.29 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvsGGvvKAVNDISFDIYRGeTFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKkf 88
Cdd:cd03264 1 LQLENLTKRYG--KK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:cd03264 72 -RRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKA--RVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
25-243 |
1.70e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 123.66 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 25 VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRKMQMIFQDP---YA 101
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL----RQLDPAELRARMALVPQDPvlfAA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 SL--NPRMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNT-VGlnkEHANRFphefSGGQRQRIGIARALAVEPEFIIAD 178
Cdd:TIGR02204 429 SVmeNIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTyLG---ERGVTL----SGGQRQRIAIARAILKDAPILLLD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 179 EPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR02204 502 EATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-244 |
3.43e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNV--KQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRA 83
Cdd:PRK13633 2 NEMIKCKNVsyKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKfnrKMQMIFQDPYASLnprmtVGDIIAEGIDI--HGLAKSKKERMDRVHELLNTVGLN--KEHAnrfPHEFSGGQR 159
Cdd:PRK13633 82 DIRN---KAGMVFQNPDNQI-----VATIVEEDVAFgpENLGIPPEEIRERVDESLKKVGMYeyRRHA---PHLLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSE 239
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPK 229
|
....*
gi 506991877 240 ELYAN 244
Cdd:PRK13633 230 EIFKE 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-245 |
5.15e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.81 E-value: 5.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDPYASLNP 105
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RmTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK13634 101 E-TVEKDICFGPMNFGV--SEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 186 VSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-243 |
8.86e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.19 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDPYASLNP 105
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAE----GIDIhglakskKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPI 181
Cdd:PRK13646 101 DTVEREIIFGpknfKMNL-------DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 182 SALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-249 |
8.95e-31 |
|
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: 115.70 E-value: 8.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVKQHFDVSggvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKK-- 87
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 -FNRKMQMIFqdpyaslnPRMTVGDIIAEGIDihGLAKSKKERMDRVHELLNTVglnKEHANRFPHEFSGGQRQRIGIAR 166
Cdd:TIGR03410 78 aYVPQGREIF--------PRLTVEENLLTGLA--ALPRRSRKIPDEIYELFPVL---KEMLGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
...
gi 506991877 247 HPY 249
Cdd:TIGR03410 225 RRY 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-243 |
1.06e-30 |
|
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: 115.66 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRKMQMIFQ--------- 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL----ALADPAWLRRQVGVVLQenvlfnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 98 -DPYASLNPRMTVGDII--AEGIDIHGLAKSKKERMDR-VHEllNTVGLnkehanrfphefSGGQRQRIGIARALAVEPE 173
Cdd:cd03252 93 rDNIALADPGMSMERVIeaAKLAGAHDFISELPEGYDTiVGE--QGAGL------------SGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLQkeKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-213 |
1.39e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.50 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTtgrtiirLYDATAG----------EVLFDGENVHGKKSRAelkkfnRKMQMIFQ 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKST-------LLAAIAGtlspafsasgEVLLNGRRLTALPAEQ------RRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 98 DPYasLNPRMTVGDIIAegidiHGLAKS--KKERMDRVHELLNTVGLNKeHANRFPHEFSGGQRQRIGIARALAVEPEFI 175
Cdd:COG4136 84 DDL--LFPHLSVGENLA-----FALPPTigRAQRRARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 506991877 176 IADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHD 213
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-245 |
1.40e-30 |
|
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: 115.08 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSraelkk 87
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fNRKMQM----------IFqdpyaslnPRMTVGDIIAEGIDIHGLAKSKKERMDRVHEL---LntvglnKEHANRFPHEF 154
Cdd:COG0410 73 -HRIARLgigyvpegrrIF--------PSLTVEENLLLGAYARRDRAEVRADLERVYELfprL------KERRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
250
....*....|.
gi 506991877 235 LTTSEELYANP 245
Cdd:COG0410 217 EGTAAELLADP 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-251 |
1.64e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.53 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKS--RAELKKFNRKMQMIFQDPYASlnP 105
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPF--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAEGIDIHGLaKSKKERMDRVHELLNTVGLNKEHANRF---PHEFSGGQRQRIGIARALAVEPEFIIADEPIS 182
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGI-KEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 183 ALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTK 251
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-232 |
5.32e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.39 E-value: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 11 VKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLfdgenvhgkKSRAELKKFNR 90
Cdd:PRK11247 15 LNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---------AGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 91 KMQMIFQDpyASLNPRMTVgdiiaegIDIHGLAKSKKERmDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAV 170
Cdd:PRK11247 82 DTRLMFQD--ARLLPWKKV-------IDNVGLGLKGQWR-DAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 171 EPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-242 |
6.46e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAEL 85
Cdd:PRK13648 5 NSIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI----TDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFNRKMQMIFQDPYASLnprmtVGDII----AEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQRQR 161
Cdd:PRK13648 79 EKLRKHIGIVFQNPDNQF-----VGSIVkydvAFGLENHAVPYDEMHR--RVSEALKQVDM-LERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEEL 241
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
.
gi 506991877 242 Y 242
Cdd:PRK13648 230 F 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-243 |
6.89e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 118.97 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKF 88
Cdd:PRK11176 342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMI--FQD------PYASlNPRMTVGDIIAEGIDIHglAKSKKERMDRVhelLNTV-GLNKEhanrfphEFSGGQR 159
Cdd:PRK11176 420 ALVSQNVhlFNDtianniAYAR-TEQYSREQIEEAARMAY--AMDFINKMDNG---LDTViGENGV-------LLSGGQR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDV----SIQAQvvnlLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVEL 235
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVER 559
|
....*...
gi 506991877 236 TTSEELYA 243
Cdd:PRK11176 560 GTHAELLA 567
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-246 |
9.51e-30 |
|
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: 113.02 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRkMQMIFQDPYASLNP 105
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPMHKRAR-LGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLnkEH-ANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISAL 184
Cdd:cd03218 89 KLTVEENILAVLEIRG--LSKKEREEKLEELLEEFHI--THlRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 185 D-VSIQaQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:cd03218 165 DpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
27-214 |
1.19e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 113.26 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKsrAElkkfnrkMQMIFQDpyASLNPR 106
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG--AE-------RGVVFQN--EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 MTVGDIIAEGIDIHGLAKSkkERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDV 186
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVEKM--QRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*...
gi 506991877 187 SIQAQVVNLLKKLQKEKGLTYLFIAHDL 214
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-243 |
1.66e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.75 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 5 REKLIEVKNVK---QHFDVS---GGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHG 78
Cdd:PRK13657 322 PPGAIDLGRVKgavEFDDVSfsyDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 79 KkSRAELKkfnRKMQMIFQDPY---ASLNPRMTVGDIIAEGIDIHGLAKSKK--ERMDRVHELLNT-VGlnkEHANRFph 152
Cdd:PRK13657 402 V-TRASLR---RNIAVVFQDAGlfnRSIEDNIRVGRPDATDEEMRAAAERAQahDFIERKPDGYDTvVG---ERGRQL-- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 efSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkeKGLTYLFIAHDLSMVKYiSDRIGVMYRGQI 232
Cdd:PRK13657 473 --SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
250
....*....|.
gi 506991877 233 VELTTSEELYA 243
Cdd:PRK13657 548 VESGSFDELVA 558
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-233 |
2.92e-29 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 117.66 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKkf 88
Cdd:TIGR03375 464 IEFRNVS--FAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-QIDPADLR-- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQDP---YASLNPRMTVGDIIAEgidihglakskKERMDRVHELlntVGLN---KEHANRFPH-------EFS 155
Cdd:TIGR03375 539 -RNIGYVPQDPrlfYGTLRDNIALGAPYAD-----------DEEILRAAEL---AGVTefvRRHPDGLDMqigergrSLS 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 156 GGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYRGQIV 233
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIV 678
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-245 |
3.59e-29 |
|
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: 114.04 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIY-RGETfGLVGESGCGKSTTGRTI----------IRLydatAGEVLFDGEN-----VHgkksraelkkfNRKMQ 93
Cdd:COG4148 17 DVDFTLPgRGVT-ALFGPSGSGKTTLLRAIaglerpdsgrIRL----GGEVLQDSARgiflpPH-----------RRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 94 MIFQDpyASLNPRMTVGDIIAEGIDiHGLAKSKKERMDRVHELLntvGLnkEH-ANRFPHEFSGGQRQRIGIARALAVEP 172
Cdd:COG4148 81 YVFQE--ARLFPHLSVRGNLLYGRK-RAPRAERRISFDEVVELL---GI--GHlLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 173 EFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-232 |
9.49e-29 |
|
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: 109.95 E-value: 9.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGkksraeLKKFNRKMQMIFQDpyASLNPRMTVGD 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG------LAPYQRPVSMLFQE--NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 112 IIAEGIdiHGLAKSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQ 191
Cdd:TIGR01277 90 NIGLGL--HPGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506991877 192 VVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-240 |
1.06e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFdvsGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAEL 85
Cdd:COG3845 3 PPALELRGITKRF---GGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KkfnRKMQMIFQDPyaSLNPRMTVgdiiAEGIdIHGLAKSKKERMD------RVHELLNTVGLNKEhANRFPHEFSGGQR 159
Cdd:COG3845 79 A---LGIGMVHQHF--MLVPNLTV----AENI-VLGLEPTKGGRLDrkaaraRIRELSERYGLDVD-PDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDvsiQAQVVNL---LKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV-EL 235
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLT---PQEADELfeiLRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVgTV 223
|
....*
gi 506991877 236 TTSEE 240
Cdd:COG3845 224 DTAET 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-243 |
1.07e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKK 87
Cdd:PRK13636 5 ILKVEEL--NYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI--DYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYASLNPRMTVGDIiaeGIDIHGLAKSKKERMDRVHELLNTVGLnkEHANRFP-HEFSGGQRQRIGIAR 166
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDV---SFGAVNLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-245 |
1.16e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKK 87
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FnrkMQMIFQDPYASL-NPrmTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK13652 79 F---VGLVFQNPDDQIfSP--TVEQDIAFGPINLGLDEETVAH--RVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-224 |
1.28e-28 |
|
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: 109.83 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFD---VSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAE 84
Cdd:COG4778 4 LLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 lkkfNRKMQMIFQDP--YAS--LN--PRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQ 158
Cdd:COG4778 84 ----PREILALRRRTigYVSqfLRviPRVSALDVVAEPLLERGV--DREEARARARELLARLNLPERLWDLPPATFSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRI 224
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRV 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-245 |
1.59e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.59 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRKMQMIFQDPyasLNPRMTV 109
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL----VQYDHHYLHRQVALVGQEP---VLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAegidiHGLAKSKKERM----------DRVHELLNTVGLN-KEHANrfphEFSGGQRQRIGIARALAVEPEFIIAD 178
Cdd:TIGR00958 572 RENIA-----YGLTDTPDEEImaaakaanahDFIMEFPNGYDTEvGEKGS----QLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 179 EPISALDVSIQAqvvnLLKKLQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYANP 245
Cdd:TIGR00958 643 EATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-262 |
3.57e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKST------------TGRTIIRLYDATAGevlfdgenvhgKKSRAELKKFNRKMQ 93
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTmiqltngliiseTGQTIVGDYAIPAN-----------LKKIKEVKRLRKEIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 94 MIFQDPYASLNpRMTVGDIIAEGiDIHgLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPE 173
Cdd:PRK13645 94 LVFQFPEYQLF-QETIEKDIAFG-PVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANpvhpytKSL 253
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QEL 244
|
....*....
gi 506991877 254 LSAIPLPDP 262
Cdd:PRK13645 245 LTKIEIDPP 253
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
9-243 |
3.78e-28 |
|
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: 114.45 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL----AIADPAWL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQ----------DPYASLNPRMTVGDIIAegidIHGLAKSKkERMDRVHELLNTVgLNKEHANrfpheFSGGQ 158
Cdd:TIGR01846 530 RRQMGVVLQenvlfsrsirDNIALCNPGAPFEHVIH----AAKLAGAH-DFISELPQGYNTE-VGEKGAN-----LSGGQ 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkeKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTS 238
Cdd:TIGR01846 599 RQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC--RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRH 675
|
....*
gi 506991877 239 EELYA 243
Cdd:TIGR01846 676 EELLA 680
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-266 |
4.86e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.42 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 43 LVGESGCGKSTTGRTIIRLYDATAG-----EVLFDGENVHGKKSRAElkkFNRKMQMIFQDPyaslNP-RMTVGDIIAEG 116
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLE---FRRRVGMLFQRP----NPfPMSIMDNVLAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 117 IDIHGLAkSKKERMDRVHELLNTVGLNKEHANRF---PHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVV 193
Cdd:PRK14271 125 VRAHKLV-PRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 194 NLLKKLQKEkgLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPVHPYTKSLLSAIPLPDPDYER 266
Cdd:PRK14271 204 EFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDAKR 274
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-245 |
5.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDPYASLNP 105
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAEGIDihgLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK13641 101 NTVLKDVEFGPKN---FGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 186 VSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
28-243 |
6.89e-28 |
|
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: 113.50 E-value: 6.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGEnvhgkkSRAELKK--FNRKMQMIFQDpyASL-- 103
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGI------PREEIPRevLANSVAMVDQD--IFLfe 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 ----------NPRMTVGDIIAEGID--IHGLAKSKKERMDrvHELLNTvGLNkehanrfpheFSGGQRQRIGIARALAVE 171
Cdd:TIGR03796 567 gtvrdnltlwDPTIPDADLVRACKDaaIHDVITSRPGGYD--AELAEG-GAN----------LSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 172 PEFIIADEPISALDVSIQAQVVNLLKKlqkeKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWA 700
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-260 |
7.76e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.70 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 3 KQREKLIEVKNVKqhfdVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSR 82
Cdd:PRK11831 2 QSVANLVDMRGVS----FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PAMSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 83 AELKKFNRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHG-----LAKSKkermdrVHELLNTVGLnKEHANRFPHEFSGG 157
Cdd:PRK11831 77 SRLYTVRKRMSMLFQS--GALFTDMNVFDNVAYPLREHTqlpapLLHST------VMMKLEAVGL-RGAAKLMPSELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTT 237
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250 260
....*....|....*....|....*.
gi 506991877 238 SEELYANPvHPYTKSLLSAI---PLP 260
Cdd:PRK11831 228 AQALQANP-DPRVRQFLDGIadgPVP 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-246 |
2.29e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.57 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 38 GETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkFNRKMQMIFQD-PYASlnpRMTVGDIIAEG 116
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA----FARKVAYLPQQlPAAE---GMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 117 -IDIHG-LAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVN 194
Cdd:PRK10575 110 rYPWHGaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506991877 195 LLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV 246
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
9-243 |
2.37e-27 |
|
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: 111.97 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkF 88
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA----V 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQdpyaslNPRMTVGDI---IAEGIDIhglakskkeRMDRVHELLNTVGLnKEHANRFP---H--------EF 154
Cdd:TIGR03797 526 RRQLGVVLQ------NGRLMSGSIfenIAGGAPL---------TLDEAWEAARMAGL-AEDIRAMPmgmHtvisegggTL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkekgLTYLFIAHDLSMVKYiSDRIGVMYRGQIVE 234
Cdd:TIGR03797 590 SGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQ 664
|
....*....
gi 506991877 235 LTTSEELYA 243
Cdd:TIGR03797 665 QGTYDELMA 673
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-241 |
2.67e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.71 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaELKKf 88
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSR-ELAK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nrKMQMIFQDPyaSLNPRMTVGDIIAEGIDIHG---LAKSKKERMDRVHELLNTVGLnkehANRFPHEFSGGQRQRIGIA 165
Cdd:COG4604 76 --RLAILRQEN--HINSRLTVRELVAFGRFPYSkgrLTAEDREIIDEAIAYLDLEDL----ADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-245 |
4.43e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.01 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDV-SGGVVKAVNDISFDIYRGETFGLVGESGCGKST----------TGRTIIRLYDATAGE--VLFDGE 74
Cdd:PRK13631 21 ILRVKNLYCVFDEkQENELVALNNISYTFEKNKIYFIIGNSGSGKSTlvthfnglikSKYGTIQVGDIYIGDkkNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 75 NVHGKKSRAELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIdihGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEF 154
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPV---ALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKlQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 506991877 235 LTTSEELYANP 245
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
30-213 |
4.50e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 104.87 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAELKKfnrkmQMIFQDPYASLNPRMTV 109
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRR-----RLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 gdiiAEGIDIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQ 189
Cdd:COG4133 93 ----RENLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 506991877 190 AQVVNLLKKLQKEKGLTyLFIAHD 213
Cdd:COG4133 168 ALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-234 |
5.29e-27 |
|
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: 105.27 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03244 3 IEFKNVS--LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI----SKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYaslnprmTVGDIIAEGIDIHGLAKSkkermDRVHELLNTVGLnKEHANRFPHE-----------FSGG 157
Cdd:cd03244 77 RSRISIIPQDPV-------LFSGTIRSNLDPFGEYSD-----EELWQALERVGL-KEFVESLPGGldtvveeggenLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKklQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVE 234
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
26-245 |
5.77e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.50 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENV-----HGkksRAelkkfnrKMQMIF--QD 98
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmHK---RA-------RLGIGYlpQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 99 PyaSLNPRMTVGD---IIAEgidIHGLakSKKERMDRVHELLNTVGLnkEH-ANRFPHEFSGGQRQRIGIARALAVEPEF 174
Cdd:COG1137 87 A--SIFRKLTVEDnilAVLE---LRKL--SKKEREERLEELLEEFGI--THlRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 175 IIADEPISALD---VS-IQAQVVNLlkklqKEKGLTYLFIAHD----LSmvkyISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:COG1137 158 ILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVLITDHNvretLG----ICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-233 |
5.97e-27 |
|
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: 104.88 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKKFNRKMQMIFQDpyASLNPRMTV 109
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV------TAAPPADRPVSMLFQE--NNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDiHGLaKSKKERMDRVHELLNTVGL-NKEhaNRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSI 188
Cdd:cd03298 88 EQNVGLGLS-PGL-KLTAEDRQAIEVALARVGLaGLE--KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506991877 189 QAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-233 |
8.94e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.05 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvHGKKSRAElkkfnRKMQMIFQDpyASLNPRMTVGD 111
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSR-----RPVSMLFQE--NNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 112 IIAEGIDiHGLAKSKKERmDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQ 191
Cdd:PRK10771 91 NIGLGLN-PGLKLNAAQR-EKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506991877 192 VVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-234 |
1.22e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 104.76 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTI--IRLYDATAGEVLFDGENVHGKKS--RAEL 85
Cdd:COG0396 2 EIKNL--HVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdeRARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFnrkmqMIFQDPYASlnPRMTVGDIIAEGID-IHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHE-FSGGQRQRIG 163
Cdd:COG0396 78 GIF-----LAFQYPVEI--PGVSVSNFLRTALNaRRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 164 IARALAVEPEFIIADEPISALDV-SIQAqVVNLLKKLqKEKGLTYLFIAHDLSMVKYIS-DRIGVMYRGQIVE 234
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKL-RSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVK 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-233 |
3.43e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.03 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaELKKFNRKMQMIFQDPYASLNp 105
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR-EVPFLRRQIGMIFQDHHLLMD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 rMTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK10908 94 -RTVYDNVAIPLIIAGASGDDIRR--RVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506991877 186 VSIQAQVVNLLKKLQKeKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK10908 170 DALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-242 |
4.26e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDPYASLNP 105
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIiAEGIDIHGLAKSKKERMdrVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK13643 100 ETVLKDV-AFGPQNFGIPKEKAEKI--AAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 186 VSIQAQVVNLLKKLQkEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELY 242
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
27-255 |
6.59e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.32 E-value: 6.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-----ATAGEVLFDGENVHGkkSRAELKKFNRKMQMIFQDPya 101
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA--PDVDPVEVRRRIGMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 slNP-RMTVGDIIAEGIDIHGLAKSKKERMDR----------VHELLNTVGLNkehanrfpheFSGGQRQRIGIARALAV 170
Cdd:PRK14243 101 --NPfPKSIYDNIAYGARINGYKGDMDELVERslrqaalwdeVKDKLKQSGLS----------LSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 171 EPEFIIADEPISALDVSIQAQVVNLLKKLQKEkgLTYLFIAHDLSMVKYISDRI----------GVMYrGQIVELTTSEE 240
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTaffnveltegGGRY-GYLVEFDRTEK 245
|
250
....*....|....*
gi 506991877 241 LYANPVHPYTKSLLS 255
Cdd:PRK14243 246 IFNSPQQQATRDYVS 260
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-232 |
6.71e-26 |
|
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: 101.35 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqhfdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAEL 85
Cdd:cd03215 2 EPVLEVRGL--------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KK---F---NRKMQMIFQDpyaslnprMTVGDiiaegidihglakskkermdrvhellNTVglnkehanrFPHEFSGGQR 159
Cdd:cd03215 74 RAgiaYvpeDRKREGLVLD--------LSVAE--------------------------NIA---------LSSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-233 |
1.70e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 106.35 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAeLKK 87
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA-LAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRK-MQMIFQDPYasLNPRMTVgdiiAEGIDIHGL--AKSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGI 164
Cdd:PRK10535 83 LRREhFGFIFQRYH--LLSHLTA----AQNVEVPAVyaGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 165 ARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQkEKGLTYLFIAHDlSMVKYISDRIGVMYRGQIV 233
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-233 |
1.78e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.52 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFNRKMQMIFQDPYASLNP 105
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RmTVGDIIAEGIDIHGLAKSKKERMDRvhELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK13649 101 E-TVLKDVAFGPQNFGVSQEEAEALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506991877 186 VSIQAQVVNLLKKLQkEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK13649 178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-240 |
2.83e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 16 QHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRaelkKFNRKMQMI 95
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR----QLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 96 FQDPyasLNPR-MTVGDIIAEG----IDIHG-LAKSKKERMDRVHELLNTVGLnkehANRFPHEFSGGQRQRIGIARALA 169
Cdd:PRK11231 82 PQHH---LTPEgITVRELVAYGrspwLSLWGrLSAEDNARVNQAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 170 VEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
8-224 |
2.85e-25 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 100.93 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHF---DVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAE 84
Cdd:TIGR02324 1 LLEVEDLSKTFtlhQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 LKKFN--RKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKKErmDRVHELLNTVGLNKEHANRFPHEFSGGQRQRI 162
Cdd:TIGR02324 81 PREVLevRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAAR--ARARELLARLNIPERLWHLPPATFSGGEQQRV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRI 224
Cdd:TIGR02324 159 NIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRV 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-232 |
3.72e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqhfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkF 88
Cdd:PRK09536 4 IDVSDL----SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLNPRMTVGDIIAEGIDIHGLAKSKKERMDR--VHELLNTVGLNKeHANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK09536 76 SRRVASVPQD--TSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRaaVERAMERTGVAQ-FADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-240 |
4.07e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.00 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKkSRAELKK 87
Cdd:PRK13548 2 MLEARNL--SVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW-SPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fNRKM--QmifqdpYASLNPRMTVGDIIAEGIDIHGLAKSKKERMdrVHELLNTVGLnkEH-ANRFPHEFSGGQRQRIGI 164
Cdd:PRK13548 77 -RRAVlpQ------HSSLSFPFTVEEVVAMGRAPHGLSRAEDDAL--VAAALAQVDL--AHlAGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 165 ARALA------VEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTS 238
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
..
gi 506991877 239 EE 240
Cdd:PRK13548 226 AE 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-233 |
4.77e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvSGGV--VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKK--SRAe 84
Cdd:COG1101 2 LELKNLSKTFN-PGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeyKRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 lkkfnrkmQMI---FQDPYASLNPRMTvgdiIAEGIDI-------HGLAKS-KKERMDRVHELLNTVGLNKEhaNRFPHE 153
Cdd:COG1101 80 --------KYIgrvFQDPMMGTAPSMT----IEENLALayrrgkrRGLRRGlTKKRRELFRELLATLGLGLE--NRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 154 ---FSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLS-MVKYiSDRIGVMYR 229
Cdd:COG1101 146 vglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDY-GNRLIMMHE 224
|
....
gi 506991877 230 GQIV 233
Cdd:COG1101 225 GRII 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-239 |
6.67e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSraelKKFNRKMQMIFQDpyASLNPRMTV 109
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQN--ATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDIHG--LAKSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVS 187
Cdd:PRK10253 99 QELVARGRYPHQplFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 188 IQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV------ELTTSE 239
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVaqgapkEIVTAE 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-234 |
8.79e-25 |
|
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: 98.15 E-value: 8.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAELKKf 88
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nrKMQMIFQDPYAslnprmtvgdiiaegidihgLAKSkkermdrvheLLNTVGLnkehanrfphEFSGGQRQRIGIARAL 168
Cdd:cd03247 76 --LISVLNQRPYL--------------------FDTT----------LRNNLGR----------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYIsDRIGVMYRGQIVE 234
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-233 |
1.47e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDV-SGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKK 87
Cdd:PRK13651 3 IKVKNIVKIFNKkLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 F--------------------NRKMQMIFQDPYASLNPRMTVGDIIAEGIDihgLAKSKKERMDRVHELLNTVGLNKEHA 147
Cdd:PRK13651 83 VleklviqktrfkkikkikeiRRRVGVVFQFAEYQLFEQTIEKDIIFGPVS---MGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 148 NRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVM 227
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
....*.
gi 506991877 228 YRGQIV 233
Cdd:PRK13651 239 KDGKII 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-234 |
1.53e-24 |
|
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: 98.76 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSG------------------GVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVl 70
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 71 fdgeNVHGKKSrAELkkfnrkmqmifqDPYASLNPRMTVGDIIAEGIDIHGLakSKKERMDRVHELLNTVGLnKEHANRF 150
Cdd:cd03220 80 ----TVRGRVS-SLL------------GLGGGFNPELTGRENIYLNGRLLGL--SRKEIDEKIDEIIEFSEL-GDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 151 PHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRG 230
Cdd:cd03220 140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
....
gi 506991877 231 QIVE 234
Cdd:cd03220 219 KIRF 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-232 |
2.14e-24 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKqhFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI----SQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDpyASLnprmtVGDIIAEGIdihglakskkermdrvhellntvglnkehanrfpheFSGGQRQRIGIARAL 168
Cdd:cd03246 75 GDHVGYLPQD--DEL-----FSGSIAENI------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKyISDRIGVMYRGQI 232
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-271 |
2.22e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.70 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTI--IRLYDATAGEVLFDGENVHGKKSRA 83
Cdd:PRK13549 3 EYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKfnrKMQMIFQDpyASLNPRMTVGDIIAEGIDIHglaksKKERMD------RVHELLNTVGLNKEHANRFpHEFSGG 157
Cdd:PRK13549 79 TERA---GIAIIHQE--LALVKELSVLENIFLGNEIT-----PGGIMDydamylRAQKLLAQLKLDINPATPV-GNLGLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV---- 233
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIgtrp 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 506991877 234 --ELTTSE-----------ELYANPVHPYTKSLLSA--IPLPDPDyERNRKRI 271
Cdd:PRK13549 227 aaGMTEDDiitmmvgreltALYPREPHTIGEVILEVrnLTAWDPV-NPHIKRV 278
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-213 |
2.28e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 98.31 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVH--GKKSRA 83
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKfnRKMQMIFQDpyaslnpRMTVGDIIA-EGIDIHGLAKSKKERMDRVH--ELLNTVGLNKEhANRFPHEFSGGQRQ 160
Cdd:PRK10584 84 KLRA--KHVGFVFQS-------FMLIPTLNAlENVELPALLRGESSRQSRNGakALLEQLGLGKR-LDHLPAQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506991877 161 RIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHD 213
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-239 |
3.65e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqhfdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAEL 85
Cdd:COG1129 254 EVVLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KK---F---NRKMQMIFQDpyaslnprMTVGDIIA----EGIDIHGLAKSKKERM--DRVHELLN--TVGLNKEHANrfp 151
Cdd:COG1129 326 RAgiaYvpeDRKGEGLVLD--------LSIRENITlaslDRLSRGGLLDRRRERAlaEEYIKRLRikTPSPEQPVGN--- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 152 heFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQ 231
Cdd:COG1129 395 --LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
....*....
gi 506991877 232 IV-ELTTSE 239
Cdd:COG1129 472 IVgELDREE 480
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-259 |
3.79e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAEL 85
Cdd:PRK13647 2 DNIIEVEDL--HFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKfnrKMQMIFQDPYASLNPrMTVGDIIAEGIDIHGLAKSKKERmdRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIA 165
Cdd:PRK13647 78 RS---KVGLVFQDPDDQVFS-STVWDDVAFGPVNMGLDKDEVER--RVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIV-----ELTTSEE 240
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLaegdkSLLTDED 229
|
250 260
....*....|....*....|....*....
gi 506991877 241 LYAN-----PV-----HPYTKSLLSAIPL 259
Cdd:PRK13647 230 IVEQaglrlPLvaqifEDLPELGQSKLPL 258
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-243 |
5.65e-24 |
|
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: 101.82 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 29 NDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKkfnRKMQMIFQDP--------- 99
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQASLR---AAIGIVPQDTvlfndtiay 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 100 ---YAslNPRMTVGDII--AEGIDIHGLAKSKKERMD-RVHELlntvGLnkehanrfphEFSGGQRQRIGIARALAVEPE 173
Cdd:COG5265 451 niaYG--RPDASEEEVEaaARAAQIHDFIESLPDGYDtRVGER----GL----------KLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506991877 174 FIIADEPISALDV----SIQAQvvnlLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:COG5265 515 ILIFDEATSALDSrterAIQAA----LREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLA 581
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-243 |
6.86e-24 |
|
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: 101.66 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 5 REKLIEVKNVKQHFDVS-------GGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGenvh 77
Cdd:TIGR01842 304 RDPAMPLPEPEGHLSVEnvtivppGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 78 gkksrAELKKFNRKmqmifqdpyaSLNPRmtVG----DI------IAEGIDIHG-LAKSKK----ERMDRVHELLNtvgl 142
Cdd:TIGR01842 380 -----ADLKQWDRE----------TFGKH--IGylpqDVelfpgtVAENIARFGeNADPEKiieaAKLAGVHELIL---- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 143 nkehanRFPHEF-----------SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKeKGLTYLFIA 211
Cdd:TIGR01842 439 ------RLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVIT 511
|
250 260 270
....*....|....*....|....*....|..
gi 506991877 212 HDLSMVKYIsDRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR01842 512 HRPSLLGCV-DKILVLQDGRIARFGERDEVLA 542
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-247 |
9.75e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 97.08 E-value: 9.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqhfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEV--LFD----GENVhgkks 81
Cdd:COG1119 3 LLELRNV----TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGerrgGEDV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 rAELKK----FNRKMQMIFQdpyaslnPRMTVGDIIAEGI-DIHGLAKSKKERM-DRVHELLNTVGLnKEHANRFPHEFS 155
Cdd:COG1119 74 -WELRKriglVSPALQLRFP-------RDETVLDVVLSGFfDSIGLYREPTDEQrERARELLELLGL-AHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 156 GGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLS-MVKYISDRI-----GVMYR 229
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLllkdgRVVAA 224
|
250 260
....*....|....*....|.
gi 506991877 230 GQIVELTTSE---ELYANPVH 247
Cdd:COG1119 225 GPKEEVLTSEnlsEAFGLPVE 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
27-245 |
1.41e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKFnrkMQMIFQDPYASLNPR 106
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL---VGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 mTVGDIIAEGIDihGLAKSKKERMDRVHELLNTVGLNKeHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDV 186
Cdd:PRK13644 94 -TVEEDLAFGPE--NLCLPPIEIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 187 SIQAQVVNLLKKLQkEKGLTYLFIAHDLSMVkYISDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK13644 170 DSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-232 |
2.59e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 95.62 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRKMQMIFQDPyaSLNPRmTV 109
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI----SQYEHKYLHSKVSLVGQEP--VLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAegidiHGLAKSKkerMDRVHELLNtvglnKEHANRFPHEF---------------SGGQRQRIGIARALAVEPEF 174
Cdd:cd03248 105 QDNIA-----YGLQSCS---FECVKEAAQ-----KAHAHSFISELasgydtevgekgsqlSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 175 IIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQI 232
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-233 |
5.05e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDV-------SGGV----------VKAVNDISFDIYRGETFGLVGESGCGKSTT-----GrtIIRlydATA 66
Cdd:COG4586 2 IEVENLSKTYRVyekepglKGALkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltG--ILV---PTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 67 GEVLFDGENVHgkKSRAELKK-----FNRKMQMIFqD--PYASLnprmtvgDIIAEgidIHGLAKSK-KERMDRVHELLN 138
Cdd:COG4586 77 GEVRVLGYVPF--KRRKEFARrigvvFGQRSQLWW-DlpAIDSF-------RLLKA---IYRIPDAEyKKRLDELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 139 TvglnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVK 218
Cdd:COG4586 144 L----GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIE 219
|
250
....*....|....*
gi 506991877 219 YISDRIGVMYRGQIV 233
Cdd:COG4586 220 ALCDRVIVIDHGRII 234
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-241 |
5.54e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 94.53 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 33 FDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvhGKKSRAELKKFNRKMQMIFQDP----YASLNPRMT 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS--PGKGWRHIGYVPQRHEFAWDFPisvaHTVMSGRTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 109 VgdiiaegidIHGLAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSI 188
Cdd:TIGR03771 79 H---------IGWLRRPCVADFAAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506991877 189 QAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIgVMYRGQIVELTTSEEL 241
Cdd:TIGR03771 149 QELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-241 |
9.50e-23 |
|
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: 97.97 E-value: 9.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLY--DATAGEVLFDGENVHGKKSRAEL 85
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKfnrKMQMIFQDpyASLNPRMTVGDIIAEG--IDIHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQRQRIG 163
Cdd:TIGR02633 77 RA---GIVIIHQE--LTLVPELSVAENIFLGneITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 164 IARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-233 |
1.20e-22 |
|
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: 97.90 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGenvhgkksrAELKKFNRkmqmifqdpyASLNPRm 107
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---------ADLSQWDR----------EELGRH- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 108 tVG----DI------IAEGIDIHGLAKSKK----ERMDRVHELLNtvglnkehanRFPHEF-----------SGGQRQRI 162
Cdd:COG4618 408 -IGylpqDVelfdgtIAENIARFGDADPEKvvaaAKLAGVHEMIL----------RLPDGYdtrigeggarlSGGQRQRI 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKyISDRIGVMYRGQIV 233
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLA-AVDKLLVLRDGRVQ 545
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-233 |
1.32e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.94 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGG-----------------VVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLF 71
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 72 DGeNVHGKKSRAELKK----FNRKMQMIFQDPyaslnprmtVGDIIAEGIDIHGLAKSK-KERMDRVHELLNTVGLNKEH 146
Cdd:cd03267 81 AG-LVPWKRRKKFLRRigvvFGQKTQLWWDLP---------VIDSFYLLAAIYDLPPARfKKRLDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 147 ANRFPHefsgGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGV 226
Cdd:cd03267 151 VRQLSL----GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLV 226
|
....*..
gi 506991877 227 MYRGQIV 233
Cdd:cd03267 227 IDKGRLL 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-219 |
1.48e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.18 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFDVSGGVvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDgeNVHGKKSrAELK 86
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKD-INLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNRKMQMIFQDP-----------------------------------YASLNPRMT-----VGDI--IAEGIDIHGLAK 124
Cdd:PTZ00265 457 WWRSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNScrakcAGDLndMSNTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 125 SKKE-------------RMDRVHELLNT--------VGLNKEhanrfphEFSGGQRQRIGIARALAVEPEFIIADEPISA 183
Cdd:PTZ00265 537 MRKNyqtikdsevvdvsKKVLIHDFVSAlpdkyetlVGSNAS-------KLSGGQKQRISIARAIIRNPKILILDEATSS 609
|
250 260 270
....*....|....*....|....*....|....*.
gi 506991877 184 LDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKY 219
Cdd:PTZ00265 610 LDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-244 |
3.96e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.43 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvhgkksraeLKK 87
Cdd:PRK11160 338 SLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP---------IAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRkmqmifqdpyASLNPRMTVgdiIAEGIDIHG--------LAKSKK--ERMdrvHELLNTVGLNKEHANRFP------ 151
Cdd:PRK11160 407 YSE----------AALRQAISV---VSQRVHLFSatlrdnllLAAPNAsdEAL---IEVLQQVGLEKLLEDDKGlnawlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 152 ---HEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDL----SMvkyisDRI 224
Cdd:PRK11160 471 eggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLtgleQF-----DRI 543
|
250 260
....*....|....*....|
gi 506991877 225 GVMYRGQIVELTTSEELYAN 244
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQ 563
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-234 |
4.15e-22 |
|
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: 91.43 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRL--YDATAGEVLFDGENVHGKK--SRAE 84
Cdd:cd03217 1 LEIKDL--HVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpeERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 LKKFnrkmqMIFQDPyaslnprmtvgdiiaegIDIHGLakskkermdRVHELLNTVGLNkehanrfpheFSGGQRQRIGI 164
Cdd:cd03217 77 LGIF-----LAFQYP-----------------PEIPGV---------KNADFLRYVNEG----------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 165 ARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYI-SDRIGVMYRGQIVE 234
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-243 |
4.46e-22 |
|
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: 96.02 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVsggvVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTI--IRLYDATAGEVL---------------- 70
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 71 FDGEN--VHGKK-----------SRAELKKFNRKMQMIFQDPYAsLNPRMTVGDIIAEGIdiHGLAKSKKERMDRVHELL 137
Cdd:TIGR03269 77 KVGEPcpVCGGTlepeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEAL--EEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 138 NTVGLnkEHanRFPH---EFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDL 214
Cdd:TIGR03269 154 EMVQL--SH--RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 506991877 215 SMVKYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-241 |
4.72e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqHFDVSGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKkSRAEL 85
Cdd:COG3845 255 EVVLEVENL--SVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL-SPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 kkfnRKMQM--IFQDPYAS-LNPRMTVGD-IIAEGIDIHGLAKSKKERMDRVHEllNTVGLNKEHANRFPHE------FS 155
Cdd:COG3845 331 ----RRLGVayIPEDRLGRgLVPDMSVAEnLILGRYRRPPFSRGGFLDRKAIRA--FAEELIEEFDVRTPGPdtparsLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 156 GGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVEL 235
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
....*.
gi 506991877 236 TTSEEL 241
Cdd:COG3845 484 VPAAEA 489
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-243 |
1.25e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKKFNRKMQMIFQDPyaslNPRMTVG 110
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKRGLLALRQQVATVFQDP----EQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 111 DIIAE-GIDIHGLAKSKKERMDRVHELLNTVglnkeHANRFPHE----FSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK13638 94 DIDSDiAFSLRNLGVPEAEITRRVDEALTLV-----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 186 VSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-241 |
2.78e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKF------NRKMQMIFQDPYASL 103
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvylpeDRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 NP-RMTVGDIiaegidihGL-AKSKKER--MDRVHELLntvGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADE 179
Cdd:PRK15439 361 NVcALTHNRR--------GFwIKPARENavLERYRRAL---NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 180 PISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-240 |
6.03e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 21 SGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVlfdgeNVHGKKSraelkkfnrkmQMIfqDPY 100
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRVS-----------ALL--ELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 101 ASLNPRMTVGD-IIAEGIdIHGLAKSK-KERMDRVhellntvglnkehanrfpHEFSG--------------GQRQRIGI 164
Cdd:COG1134 97 AGFHPELTGREnIYLNGR-LLGLSRKEiDEKFDEI------------------VEFAElgdfidqpvktyssGMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 165 ARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE 240
Cdd:COG1134 158 AVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
26-241 |
9.10e-21 |
|
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: 92.50 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKKFnrkMQMIFQDPYaslnp 105
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-DIDRHTLRQF---INYLPQEPY----- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 rMTVGDIIaEGIDIHGLAKSKKERMDRVHELLNTvglnKEHANRFPHEF-----------SGGQRQRIGIARALAVEPEF 174
Cdd:TIGR01193 559 -IFSGSIL-ENLLLGAKENVSQDEIWAACEIAEI----KDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 175 IIADEPISALDVSIQAQVVNLLKKLQKEkglTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEEL 241
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-257 |
9.88e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.70 E-value: 9.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 41 FGLvgeSGCGKST------------TGRtiIRLydatAGEVLFDGENvhgkksRAELKKFNRKMQMIFQDpyASLNPRMT 108
Cdd:PRK11144 30 FGR---SGAGKTSlinaisgltrpqKGR--IVL----NGRVLFDAEK------GICLPPEKRRIGYVFQD--ARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 109 VgdiiaEGIDIHGLAKSKKERMDRVHELLntvGLnkEHA-NRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVS 187
Cdd:PRK11144 93 V-----RGNLRYGMAKSMVAQFDKIVALL---GI--EPLlDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 188 IQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYANPV-HPY-TKSLLSAI 257
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPWlPKEEQSSI 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-234 |
1.88e-20 |
|
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: 87.47 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPyaslnprmtvgdiiaegIDIHGLAKSKKERMDR-----VHELLNTV--GLNkehanrfpheFSGGQRQR 161
Cdd:cd03369 81 RSSLTIIPQDP-----------------TLFSGTIRSNLDPFDEysdeeIYGALRVSegGLN----------LSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAqvvnLLKKLQKE--KGLTYLFIAHDL-SMVKYisDRIGVMYRGQIVE 234
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDA----LIQKTIREefTNSTILTIAHRLrTIIDY--DKILVMDAGEVKE 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-227 |
2.26e-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: 91.19 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGenvhgkksrAELKKFNRKmQMIFQDPYASLNP 105
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG---------VPLADADAD-SWRDQIAWVPQHP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIiAEGIdIHGLAKSKKERMDRV------HELLNTV--GLNKEHANRfPHEFSGGQRQRIGIARALAVEPEFIIA 177
Cdd:TIGR02857 406 FLFAGTI-AENI-RLARPDASDAEIREAleraglDEFVAALpqGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506991877 178 DEPISALDVSIQAQVVNLLKKLQkeKGLTYLFIAHDLSmVKYISDRIGVM 227
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-224 |
7.30e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.31 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 3 KQREKLIEVKNVkqHFDVSGGVVkaVNDISFDIYRGEtFGLV-GESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkks 81
Cdd:PRK10247 2 QENSPLLQLQNV--GYLAGDAKI--LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 rAELK--KFNRKMQMIFQDPyaslnprMTVGDIIAEGIDIHGLAKSKKERMDRVHELLNTVGLNKEHANRFPHEFSGGQR 159
Cdd:PRK10247 72 -STLKpeIYRQQVSYCAQTP-------TLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 160 QRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRI 224
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-234 |
1.03e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 25 VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELkkfNRKMQMIFQDpyASLN 104
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL---AAGVAIIYQE--LHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 105 PRMTVgdiiAEGIDI------HGLAKsKKERMDRVHELLNTVGLNKEHANRFPHeFSGGQRQRIGIARALAVEPEFIIAD 178
Cdd:PRK11288 92 PEMTV----AENLYLgqlphkGGIVN-RRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 179 EPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-233 |
4.52e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.15 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGE--NVHGKKSRA 83
Cdd:PRK09700 3 TPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKkfnrkMQMIFQDPYA----SLNPRMTVGDIIAE---GIDIHGLAKSKKermdRVHELLNTVGLnKEHANRFPHEFSG 156
Cdd:PRK09700 79 QLG-----IGIIYQELSVidelTVLENLYIGRHLTKkvcGVNIIDWREMRV----RAAMMLLRVGL-KVDLDEKVANLSI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKE-KGLTYlfIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVY--ISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-245 |
8.56e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksRAELKKFNRKMQMIFQDPYaslnpr 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLAVVSQTPF------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 mTVGDIIAEGIDIhGLAKSKKERMDRVHELLNTvglnKEHANRFPHEF-----------SGGQRQRIGIARALAVEPEFI 175
Cdd:PRK10789 400 -LFSDTVANNIAL-GRPDATQQEIEHVARLASV----HDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 176 IADEPISALDVSIQAQVVNLLKklQKEKGLTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-244 |
1.43e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 26 KAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkksrAELKKFNRKMQMIFQDPY-ASLN 104
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI------SLLPLHARARRGIGYLPQeASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 105 PRMTVGDIIAEGIDIHGlAKSKKERMDRVHELLNTvgLNKEH-ANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISA 183
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEE--FHIEHlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 184 LDvsiQAQVVNLLKKLQ--KEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:PRK10895 168 VD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
27-214 |
2.53e-18 |
|
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: 85.10 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKkfnRKMQMIFQDPY---ASL 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVR---RRVSVCAQDAHlfdTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 --NPRMTVGDI----IAEGIDIHGLAkskkERMDRVHELLNT-VGlnkEHANRFphefSGGQRQRIGIARALAVEPEFII 176
Cdd:TIGR02868 426 reNLRLARPDAtdeeLWAALERVGLA----DWLRALPDGLDTvLG---EGGARL----SGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 506991877 177 ADEPISALDVSIQAQVVNLLkkLQKEKGLTYLFIAHDL 214
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-244 |
3.91e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.85 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKK 87
Cdd:PRK11614 5 MLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYASLNpRMTVGDIIAEGidihGLAKSKK---ERMDRVHELLNTvgLNKEHANRfPHEFSGGQRQRIGI 164
Cdd:PRK11614 77 IMREAVAIVPEGRRVFS-RMTVEENLAMG----GFFAERDqfqERIKWVYELFPR--LHERRIQR-AGTMSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 165 ARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-234 |
5.88e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 25 VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDAT--AGEVLFDGENVHGKKSRAELKkfnRKMQMIFQD---- 98
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEA---LGIVIIHQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 99 PYASlnprmtvgdiIAEGIDIhGLAKSKK------ERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEP 172
Cdd:NF040905 91 PYLS----------IAENIFL-GNERAKRgvidwnETNRRARELLAKVGL-DESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 173 EFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-233 |
1.10e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 80.39 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 25 VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTI---IRLYDATAGEVLFDGEnvhgkksraELKKfnRKMQMIF----Q 97
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ---------PRKP--DQFQKCVayvrQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 98 DPYasLNPRMTVGDIIAEGIDIHGLAKSKKERMDRVHEllnTVGLNKEHANRFPHEF----SGGQRQRIGIARALAVEPE 173
Cdd:cd03234 89 DDI--LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVE---DVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-239 |
1.46e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkf 88
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nrKMQMIFQDPYASLNPRMTVgdiiAEGIDIHG--LAKSKKERMDRVHELLNTVGLNKEhANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK13537 79 --RQRVGVVPQFDNLDPDFTV----RENLLVFGryFGLSAAAARALVPPLLEFAKLENK-ADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKeKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV------ELTTSE 239
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIaegaphALIESE 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-233 |
3.96e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVlfdgeNVHGKKSRAELKKfnRKMQMIFQDPYASLNPR 106
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQK--NLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 MTVGDIIAEGIDIHG--LAKSKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISAL 184
Cdd:PRK15056 95 VLVEDVVMMGRYGHMgwLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506991877 185 DVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIgVMYRGQIV 233
Cdd:PRK15056 174 DVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-234 |
4.42e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkKSRAELKKf 88
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARLAR- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nRKMQMIFQdpYASLNPRMTVgdiiAEGIDIHG--LAKSKKERMDRVHELLNTVGLNKEhANRFPHEFSGGQRQRIGIAR 166
Cdd:PRK13536 114 -ARIGVVPQ--FDNLDLEFTV----RENLLVFGryFGMSTREIEAVIPSLLEFARLESK-ADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKeKGLTYLFIAHDLSMVKYISDRIGVMYRG-QIVE 234
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-233 |
4.50e-17 |
|
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: 77.59 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 19 DVSGGVVKAVNDISFDIYRGETFGLVGESGCGKST-----TGRTIirlYDATAGEVLFDGENVHgkksraeLKKFNRKMQ 93
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTllnalAGRRT---GLGVSGEVLINGRPLD-------KRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 94 MIFQDPYasLNPRMTVgdiiAEGIDIHglAKSKkermdrvhellntvGLnkehanrfphefSGGQRQRIGIARALAVEPE 173
Cdd:cd03213 86 YVPQDDI--LHPTLTV----RETLMFA--AKLR--------------GL------------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYIS-DRIGVMYRGQIV 233
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELfDKLLLLSQGRVI 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-258 |
9.83e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKK 87
Cdd:PLN03232 1234 SIKFEDV--HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV----AKFGLTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDPYA-SLNPRMTVgDIIAEGIDI---HGLAKSK-KERMDRvhellNTVGLNKEhANRFPHEFSGGQRQRI 162
Cdd:PLN03232 1308 LRRVLSIIPQSPVLfSGTVRFNI-DPFSEHNDAdlwEALERAHiKDVIDR-----NPFGLDAE-VSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAqvvnLLKKLQKE--KGLTYLFIAHDLSMVkYISDRIGVMYRGQIVELTTSEE 240
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQE 1455
|
250
....*....|....*...
gi 506991877 241 LYANPVHPYTKSLLSAIP 258
Cdd:PLN03232 1456 LLSRDTSAFFRMVHSTGP 1473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-240 |
1.17e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 2 TKQREKLIEVKNVKQHFDvsggvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkKS 81
Cdd:PRK09700 259 NLAHETVFEVRNVTSRDR------KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 82 RAELKKFNRKMQMIFQD-------PYASLNPRMTVGDIIAEG--IDIHGLAKSKKER--MDRVHELLNtvgLNKEHANRF 150
Cdd:PRK09700 330 RSPLDAVKKGMAYITESrrdngffPNFSIAQNMAISRSLKDGgyKGAMGLFHEVDEQrtAENQRELLA---LKCHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 151 PHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRG 230
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
250
....*....|
gi 506991877 231 QIVELTTSEE 240
Cdd:PRK09700 486 RLTQILTNRD 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-222 |
1.37e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVKQHFDVSGGVVK--AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkksraelkk 87
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKmqmifqdpyaslnprmtvgdiiAEGIDIHGLAKSKKERMdrvhELLNTVGLNKEHA-NRFPHEFSGGQRQRIGIAR 166
Cdd:COG2401 96 FGRE----------------------ASLIDAIGRKGDFKDAV----ELLNAVGLSDAVLwLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 167 ALAVEPEFIIADEPISALDVSiQAQVVNL-LKKLQKEKGLTYLFIAHDLSMVKYISD 222
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQP 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-226 |
2.11e-16 |
|
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: 77.06 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 17 HFDVSGGvvkavndisfDIYRGETFGLVGESGCGKSTtgrtIIRLYdatAGEVLFDGEnvhgkKSRAELKKFNRKMQmif 96
Cdd:cd03237 14 TLEVEGG----------SISESEVIGILGPNGIGKTT----FIKML---AGVLKPDEG-----DIEIELDTVSYKPQ--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 97 qdpYASLNPRMTVGDIIAEGIDIHGLAKSKKErmdrvhELLNTVGLNKEHANRFPhEFSGGQRQRIGIARALAVEPEFII 176
Cdd:cd03237 69 ---YIKADYEGTVRDLLSSITKDFYTHPYFKT------EIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506991877 177 ADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGV 226
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-244 |
3.60e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.01 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKKfnrKMQMIFQDPYA-------SL 103
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-SKFGLMDLRK---VLGIIPQAPVLfsgtvrfNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 NPRMTVGDIiaegiDIHglakskkERMDRVH--ELL--NTVGLNKEHANRfPHEFSGGQRQRIGIARALAVEPEFIIADE 179
Cdd:PLN03130 1334 DPFNEHNDA-----DLW-------ESLERAHlkDVIrrNSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 180 PISALDVSIQAqvvnLLKKLQKE--KGLTYLFIAHDLSMVkyI-SDRIGVMYRGQIVELTTSEELYAN 244
Cdd:PLN03130 1401 ATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-232 |
3.96e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDVSggvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLY--DATAG---EVLFDGENVHGKK 80
Cdd:PRK09984 2 QTIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 SRaELKKFNRKMQMIFQDpyASLNPRMTVgdiiAEGIDIHGLAKS----------KKERMDRVHELLNTVGLNkehanRF 150
Cdd:PRK09984 78 AR-DIRKSRANTGYIFQQ--FNLVNRLSV----LENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMV-----HF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 151 PHE----FSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGV 226
Cdd:PRK09984 146 AHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVA 225
|
....*.
gi 506991877 227 MYRGQI 232
Cdd:PRK09984 226 LRQGHV 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-232 |
4.00e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.33 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-ATAGEVLFDGENVhgkKSRAE 84
Cdd:TIGR02633 255 DVILEARNLTCW-DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPV---DIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 LKKFNRKMQMIFQD-PYASLNPRMTVGdiiaEGIDIHGLAK-SKKERMDRVHELLNTVGLNKEHANRFPHEF------SG 156
Cdd:TIGR02633 331 AQAIRAGIAMVPEDrKRHGIVPILGVG----KNITLSVLKSfCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigrlSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-239 |
4.89e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 25 VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVH--GKKSRAElkkfnRKMQMIFQDpyas 102
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQE-----AGIGIIHQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 103 LN--PRMTvgdiIAEGIdihGLAKSKKERMDRVH---------ELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVE 171
Cdd:PRK10762 88 LNliPQLT----IAENI---FLGREFVNRFGRIDwkkmyaeadKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 172 PEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQ-IVELTTSE 239
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIAEREVAD 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-212 |
5.78e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.93 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLF-DGEnvhgkksraelkkfnrkmQMIF--QDPY---A 101
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGA------------------RVLFlpQRPYlplG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 SL-------NPRMTVGDiiaegidihglakskkermDRVHELLNTVGLnkEH-ANRF------PHEFSGGQRQRIGIARA 167
Cdd:COG4178 441 TLreallypATAEAFSD-------------------AELREALEAVGL--GHlAERLdeeadwDQVLSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQvvnLLKKLQKE-KGLTYLFIAH 212
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAA---LYQLLREElPGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
29-213 |
1.67e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 29 NDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGenvhgkksraelkkfNRKMQMIFQDPYasLNPRMT 108
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------------GLRIGYLPQEPP--LDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 109 VGDIIAEG----------------------IDIHGLAK--SKKERMD------RVHELLNTVGLNKEHANRFPHEFSGGQ 158
Cdd:COG0488 78 VLDTVLDGdaelraleaeleeleaklaepdEDLERLAElqEEFEALGgweaeaRAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDV-SIQAqvvnLLKKLQKEKGlTYLFIAHD 213
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLeSIEW----LEEFLKNYPG-TVLVVSHD 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-246 |
2.98e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVkqhfdvSGgvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKK----- 80
Cdd:PRK10762 255 EVRLKVDNL------SG---PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdgl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 81 --------------------------SRAELKKFNRKMQMIFQDpyaslNPRMTVGDIIaegidihGLAKSKKERMDRVH 134
Cdd:PRK10762 326 angivyisedrkrdglvlgmsvkenmSLTALRYFSRAGGSLKHA-----DEQQAVSDFI-------RLFNIKTPSMEQAI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 135 ELLntvglnkehanrfphefSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDL 214
Cdd:PRK10762 394 GLL-----------------SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEM 455
|
250 260 270
....*....|....*....|....*....|....*..
gi 506991877 215 SMVKYISDRIGVMYRGQI-----VELTTSEELYANPV 246
Cdd:PRK10762 456 PEVLGMSDRILVMHEGRIsgeftREQATQEKLMAAAV 492
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-241 |
4.43e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkfnRK----MQMIFqdpyaS 102
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT------RRrvgyMSQAF-----S 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 103 LNPRMTVgdiiAEGIDIHglAK----SKKERMDRVHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIAD 178
Cdd:NF033858 350 LYGELTV----RQNLELH--ARlfhlPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 179 EPISALDVSIQAQVVNLLKKLQKEKGLTylfIahdlsmvkYIS----------DRIGVMYRGQIVELTTSEEL 241
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELSREDGVT---I--------FISthfmneaercDRISLMHAGRVLASDTPAAL 484
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-243 |
1.30e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKKfnrKMQMIFQDPY---ASLNPR 106
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL-SSLSHSVLRQ---GVAMVQQDPVvlaDTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 MTVGDIIAEgidihglakskkermDRVHELLNTVGLNkEHANRFP-----------HEFSGGQRQRIGIARALAVEPEFI 175
Cdd:PRK10790 435 VTLGRDISE---------------EQVWQALETVQLA-ELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 176 IADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVkYISDRIGVMYRGQIVELTTSEELYA 243
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTI-VEADTILVLHRGQAVEQGTHQQLLA 563
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-241 |
1.81e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKqhfdVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTII--RLYDATAGEVLFDGENVHGK--KSR 82
Cdd:CHL00131 6 PILEIKNLH----ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLepEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 83 AELKKFnrkmqMIFQDPyaslnprmtvgdiiaegIDIHGL-----------AKSKKERMDRVHEL---------LNTVGL 142
Cdd:CHL00131 82 AHLGIF-----LAFQYP-----------------IEIPGVsnadflrlaynSKRKFQGLPELDPLefleiinekLKLVGM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 143 NKEHANRFPHE-FSGGQRQRIGIARALAVEPEFIIADEPISALDVS---IQAQVVNLLKKLQKekglTYLFIAHDLSMVK 218
Cdd:CHL00131 140 DPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLD 215
|
250 260
....*....|....*....|....
gi 506991877 219 YIS-DRIGVMYRGQIVElTTSEEL 241
Cdd:CHL00131 216 YIKpDYVHVMQNGKIIK-TGDAEL 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-226 |
3.17e-14 |
|
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: 72.89 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 2 TKQREKLIEVKNVKQHFD-----VSGGvvkavndisfDIYRGETFGLVGESGCGKSTTGRTIirlydatAGEVLFDGENV 76
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGgfsleVEGG----------EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 77 HGKKsraelkKFNRKMQmifqdpYASLNPRMTVGDIiaegidihgLAKSKKERMDRV---HELLNTVGLNKEHANRFPhE 153
Cdd:COG1245 398 DEDL------KISYKPQ------YISPDYDGTVEEF---------LRSANTDDFGSSyykTEIIKPLGLEKLLDKNVK-D 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 154 FSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGV 226
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-196 |
4.00e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAelkkfnrkmQMIFQDPYASLNPRMTV 109
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---------ACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GDIIAEGIDIHGlakskkERMDRVHELLNTVGLNkeH-ANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSI 188
Cdd:PRK13539 91 AENLEFWAAFLG------GEELDIAAALEAVGLA--PlAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*...
gi 506991877 189 QAQVVNLL 196
Cdd:PRK13539 163 VALFAELI 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-226 |
5.31e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 3 KQREKLIEVKNVKQHFD-----VSGGvvkavndisfDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDgenvh 77
Cdd:PRK13409 335 SERETLVEYPDLTKKLGdfsleVEGG----------EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 78 gkksraelKKFNRKMQmifqdpYASLNPRMTVGDIIAegidihglakSKKERMDRV---HELLNTVGLNKEHANRFPhEF 154
Cdd:PRK13409 400 --------LKISYKPQ------YIKPDYDGTVEDLLR----------SITDDLGSSyykSEIIKPLQLERLLDKNVK-DL 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGV 226
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-245 |
5.93e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTtgrtiirLYDATAGEVLFDGE-NVHGKKSRA-ELKKFNRKMQMIFQDP---YASLNP 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTS-------LLNALLGFLPYQGSlKINGIELRElDPESWRKHLSWVGQNPqlpHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAEGIDI-HGLAKSKkermdrVHELLN--TVGLN---KEHANRFphefSGGQRQRIGIARALAVEPEFIIADE 179
Cdd:PRK11174 442 NVLLGNPDASDEQLqQALENAW------VSEFLPllPQGLDtpiGDQAAGL----SVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 180 PISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYIsDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-233 |
6.32e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKqhfdvsGGVVKAvnDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAEL 85
Cdd:PRK11288 255 EVRLRLDGLK------GPGLRE--PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKF------NRKMQMIFqdPYASlnprmtvgdiIAEGIDI----HGL-------AKSKKERMDRVHELLNTVGLNKEHAN 148
Cdd:PRK11288 327 RAGimlcpeDRKAEGII--PVHS----------VADNINIsarrHHLragclinNRWEAENADRFIRSLNIKTPSREQLI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 149 RFpheFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:PRK11288 395 MN---LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMR 470
|
....*
gi 506991877 229 RGQIV 233
Cdd:PRK11288 471 EGRIA 475
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-241 |
7.49e-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: 68.92 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAELKKfnrkmQMIFQDPYASLNPRMTVg 110
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEPHE-----NILYLGHLPGLKPELSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 111 diiAEGID----IHGLAkskkERMdrVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDV 186
Cdd:TIGR01189 91 ---LENLHfwaaIHGGA----QRT--IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 187 SIQAQvvnllkklqkekgLTYLFIAHdlsmvkyisdrigvMYRGQIVELTTSEEL 241
Cdd:TIGR01189 161 AGVAL-------------LAGLLRAH--------------LARGGIVLLTTHQDL 188
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-212 |
1.04e-13 |
|
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: 67.95 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVlfdgenvhgkksraelkKFNRKMQMIF--QDPYaslnp 105
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------------GMPEGEDLLFlpQRPY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 rMTVG---DIIAegidihglakskkermdrvhellntvglnkehanrFP--HEFSGGQRQRIGIARALAVEPEFIIADEP 180
Cdd:cd03223 75 -LPLGtlrEQLI-----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|..
gi 506991877 181 ISALDVSIQAQVVNLLkklqKEKGLTYLFIAH 212
Cdd:cd03223 119 TSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-239 |
1.20e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFDVSGGVVKAVNdisFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELK 86
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNrkmqMIFQDPY---ASLNPRMTVGD--IIAEGIDIHGLaKSKKERMDrvHELLNTvglnkehanrfphEFSGGQRQR 161
Cdd:PRK10522 398 LFS----AVFTDFHlfdQLLGPEGKPANpaLVEKWLERLKM-AHKLELED--GRISNL-------------KLSKGQKKR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 162 IGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSmvkYI--SDRIGVMYRGQIVELTTSE 239
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH---YFihADRLLEMRNGQLSELTGEE 534
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-234 |
1.42e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFDvsGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFdGENVHgkksraelk 86
Cdd:COG0488 314 KVLELEGLSKSYG--DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 kfnrkmqmI--F-QDpYASLNPRMTVGDIIAEGidihglAKSKKERmdRVHELLNTVGLNKEHANRFPHEFSGGQRQRIG 163
Cdd:COG0488 380 --------IgyFdQH-QEELDPDKTVLDELRDG------APGGTEQ--EVRGYLGRFLFSGDDAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 164 IARALAVEPEFIIADEPISALDV-SIQAqvvnLLKKLQKEKGlTYLFIAHDLSMVKYISDRIGVMYRGQIVE 234
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-233 |
1.61e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQHFdvSGgvVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgKKSRAELKK 87
Cdd:PRK15439 11 LLCARSISKQY--SG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-RLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNrkMQMIFQDPYasLNPRMTVGDIIAegidiHGLAKSKkERMDRVHELLNTVGLnkeHANrfPHEFSG----GQRQRIG 163
Cdd:PRK15439 86 LG--IYLVPQEPL--LFPNLSVKENIL-----FGLPKRQ-ASMQKMKQLLAALGC---QLD--LDSSAGslevADRQIVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 164 IARALAVEPEFIIADEPISALdvsIQAQVVNLLKKLQK--EKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-217 |
1.88e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 67.64 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLfdgenVHGKKSRAELkkfnrkmqmifqdPYASLNPR 106
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----RAGGARVAYV-------------PQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 ---MTVGDIIAEGIDIHGLAKSKKERMDR--VHELLNTVGLnKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPI 181
Cdd:NF040873 69 slpLTVRDLVAMGRWARRGLWRRLTRDDRaaVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 506991877 182 SALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMV 217
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-224 |
2.76e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKqhfdVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLfdgenvhgkksRAELKK 87
Cdd:PRK09544 4 LVSLENVS----VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 FNRKMQMIFQDP--------YASLNPRMTVGDIIAEgidihglakskkerMDRVhellntvglNKEHANRFP-HEFSGGQ 158
Cdd:PRK09544 69 IGYVPQKLYLDTtlpltvnrFLRLRPGTKKEDILPA--------------LKRV---------QAGHLIDAPmQKLSGGE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 159 RQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRI 224
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-241 |
2.86e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 29 NDISFDIYRGETFGLVGESGCGKsTTGRTIIRLYDAT----AGEVLFDGEnvhgkksRAELKKFNRKMQMIFQDpyaSLN 104
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGK-TTLMNALAFRSPKgvkgSGSVLLNGM-------PIDAKEMRAISAYVQQD---DLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 105 -PRMTVgdiiAEGIDIHGLAK-----SKKERMDRVHELLNTVGLNKEHANRFPHE-----FSGGQRQRIGIARALAVEPE 173
Cdd:TIGR00955 111 iPTLTV----REHLMFQAHLRmprrvTKKEKRERVDEVLQALGLRKCANTRIGVPgrvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKY-ISDRIGVMYRGQIVELTTSEEL 241
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELFeLFDKIILMAEGRVAYLGSPDQA 254
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-245 |
8.85e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENV--HGkksraeLKKFNRKMQMIFQDPY----- 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgaYG------LRELRRQFSMIPQDPVlfdgt 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 101 --ASLNP--RMTVGDIIA--EGIDIHGLAKSKKERMD-RVHEllntVGLNkehanrfpheFSGGQRQRIGIARALAVEPE 173
Cdd:PTZ00243 1400 vrQNVDPflEASSAEVWAalELVGLRERVASESEGIDsRVLE----GGSN----------YSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 174 -FIIADEPIS----ALDVSIQAQVVNLLkklqkeKGLTYLFIAHDLSMV-KYisDRIGVMYRGQIVELTTSEELYANP 245
Cdd:PTZ00243 1466 gFILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVaQY--DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-232 |
1.83e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHfDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYD-ATAGEVLFDGENVhgkKSRAE 84
Cdd:PRK13549 257 EVILEVRNLTAW-DPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV---KIRNP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 LKKFNRKMQMIFQDPYA-SLNPRMTVGdiiaEGIDIHGLAK-SKKERMDRVHELLNTVGLNKEHANRFPHEF------SG 156
Cdd:PRK13549 333 QQAIAQGIAMVPEDRKRdGIVPVMGVG----KNITLAALDRfTGGSRIDDAAELKTILESIQRLKVKTASPElaiarlSG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 157 GQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-233 |
4.49e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 16 QHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTtgrtiirLYDATAGEvLFDGENVHGKKSRAELKkfnrkmqmI 95
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKST-------LLKALAGD-LTGGGAPRGARVTGDVT--------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 96 FQDPYASLNPR------------------MTVGDIIAEGIDIHG-----LAKSKKERMDRVHELLNTVGLnkehANRFPH 152
Cdd:PRK13547 69 NGEPLAAIDAPrlarlravlpqaaqpafaFSAREIVLLGRYPHArragaLTHRDGEIAWQALALAGATAL----VGRDVT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 EFSGGQRQRIGIARALA---------VEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDR 223
Cdd:PRK13547 145 TLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADR 224
|
250
....*....|
gi 506991877 224 IGVMYRGQIV 233
Cdd:PRK13547 225 IAMLADGAIV 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-240 |
5.89e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 33 FDIYRGETFGLVGESGCGKSTTGRTIirlydatAGEVLFD-GENVHGKK---SRAElkkfnrkmqmifQDPyaslnPRM- 107
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDlivARLQ------------QDP-----PRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 108 --TVGDIIAEGI-----------DI-HGLAKSKKERM--------------------DRVHELLNTVGLNkehANRFPHE 153
Cdd:PRK11147 80 egTVYDFVAEGIeeqaeylkryhDIsHLVETDPSEKNlnelaklqeqldhhnlwqleNRINEVLAQLGLD---PDAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 154 FSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKekglTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
250
....*....|....*
gi 506991877 234 E--------LTTSEE 240
Cdd:PRK11147 233 SypgnydqyLLEKEE 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-224 |
6.60e-12 |
|
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: 62.08 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDvsGGVVkaVNDISFDIYRGETFGLVGESGCGKSTtgrtiirlydatagevLFdgenvhgkksraelkkf 88
Cdd:cd03221 1 IELENLSKTYG--GKLL--LKDISLTINPGDRIGLVGRNGAGKST----------------LL----------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 nrkmqmifqdpyaslnpRMTVGDIIA-EGIDIHGlakskkermdrvhellntvglnkeHANRFPH--EFSGGQRQRIGIA 165
Cdd:cd03221 44 -----------------KLIAGELEPdEGIVTWG------------------------STVKIGYfeQLSGGEKMRLALA 82
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKekglTYLFIAHDLSMVKYISDRI 224
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKI 137
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-232 |
7.39e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.19 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 11 VKNVKQHFDVSGGvvKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLfdgenVHGKKSRAELKKFNR 90
Cdd:TIGR01257 931 VKNLVKIFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL-----VGGKDIETNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 91 KMQMIFQdpYASLNPRMTVGDIIAEGIDIHGlaKSKKERMDRVHELLNTVGLNKEHaNRFPHEFSGGQRQRIGIARALAV 170
Cdd:TIGR01257 1004 SLGMCPQ--HNILFHHLTVAEHILFYAQLKG--RSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVG 1078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 171 EPEFIIADEPISALDVSIQAQVVNLLkkLQKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQI 232
Cdd:TIGR01257 1079 DAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-226 |
8.61e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKF 88
Cdd:PTZ00265 1166 IEIMDVNFRY-ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQ--------------DPYASLNprmTVGDIIAEGIDI-------------------------------HGLA 123
Cdd:PTZ00265 1245 DEEQNVGMKnvnefsltkeggsgEDSTVFK---NSGKILLDGVDIcdynlkdlrnlfsivsqepmlfnmsiyenikFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 124 KSKKERMDR------VHELLNTVGlNKEHANRFPH--EFSGGQRQRIGIARALAVEPEFIIADEPISALDVS----IQAQ 191
Cdd:PTZ00265 1322 DATREDVKRackfaaIDEFIESLP-NKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKT 1400
|
250 260 270
....*....|....*....|....*....|....*
gi 506991877 192 VVNLLKKLQKekglTYLFIAHDLSMVKYiSDRIGV 226
Cdd:PTZ00265 1401 IVDIKDKADK----TIITIAHRIASIKR-SDKIVV 1430
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-218 |
8.63e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgKKSRAELKKfnrkmQMIFQDPYASLNPRM 107
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQK-----QLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 108 TVGDIIAegIDIHGLAKSKKermdrVHELLNTVGLnkEHANRFP-HEFSGGQRQRIGIARALAVEPEFIIADEPISALDv 186
Cdd:PRK13540 90 TLRENCL--YDIHFSPGAVG-----ITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD- 159
|
170 180 190
....*....|....*....|....*....|....*
gi 506991877 187 siQAQVVNLLKKLQ--KEKGLTYLFIAH-DLSMVK 218
Cdd:PRK13540 160 --ELSLLTIITKIQehRAKGGAVLLTSHqDLPLNK 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-243 |
1.21e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRKMQMIFQDPY-------AS 102
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----AKIGLHDLRFKITIIPQDPVlfsgslrMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 103 LNPRMTVGD----IIAEGIDIHGLAKSKKERMDrvHELLNTvGLNkehanrfpheFSGGQRQRIGIARALAVEPEFIIAD 178
Cdd:TIGR00957 1380 LDPFSQYSDeevwWALELAHLKTFVSALPDKLD--HECAEG-GEN----------LSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 179 EPISALDVS----IQAQVvnllkKLQKEKgLTYLFIAHDLSMVKYISdRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR00957 1447 EATAAVDLEtdnlIQSTI-----RTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
24-250 |
1.81e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 63.00 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 24 VVKAVNDIsfdIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkkSRAELKKFNRKMQMIFQDPYA-- 101
Cdd:cd03288 36 VLKHVKAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI----SKLPLHTLRSRLSIILQDPILfs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 -----SLNPRMTVGD-IIAEGIDIHGLAKSKKERMDRVHELLNTVGLNkehanrfpheFSGGQRQRIGIARALAVEPEFI 175
Cdd:cd03288 109 gsirfNLDPECKCTDdRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN----------FSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 176 IADEPISALDVSIQaqvvNLLKK--LQKEKGLTYLFIAHDLSMVkYISDRIGVMYRGQIVELTTSEELYANPVHPYT 250
Cdd:cd03288 179 IMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-231 |
3.50e-11 |
|
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: 61.33 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 29 NDISFDIYRGETFGLVGESGCGKSTtgrtiirLYDATAGEVLFDGENVHGKKSRAelkkfnrkmqmifqdpYASLNP--- 105
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSS-------LLSALLGELEKLSGSVSVPGSIA----------------YVSQEPwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 106 RMTVGDIIAEGIDIHglakskKERMDRV-------------HELLNTV----GLNkehanrfpheFSGGQRQRIGIARAL 168
Cdd:cd03250 79 NGTIRENILFGKPFD------EERYEKVikacalepdleilPDGDLTEigekGIN----------LSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVN--LLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQ 231
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-228 |
3.90e-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: 62.00 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYR------GETFGLVGESGCGKSTTGRTIirlydatAGEVL-----FDGE----NVHGKKSRAELKKF-----NRK 91
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKIL-------AGKLKpnlgkFDDPpdwdEILDEFRGSELQNYftkllEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 92 MQMIFQDPYASLNPRMTVGDIIAegidihgLAKSKKERmDRVHELLNTVGLNKEhANRFPHEFSGGQRQRIGIARALAVE 171
Cdd:cd03236 87 VKVIVKPQYVDLIPKAVKGKVGE-------LLKKKDER-GKLDELVDQLELRHV-LDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 172 PEFIIADEPISALDVSIQAQVVNLLKKLQKEKGlTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-263 |
6.33e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYRGETFGLVGESGCGKSTTGRtiirlydATAGE-VLFDGENVHgkksraelkKFNR-------KMQMIFQDPYASL 103
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAR-------ALAGElPLLSGERQS---------QFSHitrlsfeQLQKLVSDEWQRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 NPRM----------TVGDIIAEGidihglakSKKErmDRVHELLNTVGLNKEHANRFPHeFSGGQRQRIGIARALAVEPE 173
Cdd:PRK10938 87 NTDMlspgeddtgrTTAEIIQDE--------VKDP--ARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 174 FIIADEPISALDVSIQAQVVNLLKKLQKeKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEE-----LYANPVHP 248
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEilqqaLVAQLAHS 234
|
250
....*....|....*
gi 506991877 249 YTkslLSAIPLPDPD 263
Cdd:PRK10938 235 EQ---LEGVQLPEPD 246
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-241 |
8.91e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 25 VKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHGKKSRAELKKfnrKMQMIFQDpyASLN 104
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN---GISMVHQE--LNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 105 PRMTVGDIIAEG--------IDIHGLAKSKKERMDrvhELLNTVGLNKEHANrfpheFSGGQRQRIGIARALAVEPEFII 176
Cdd:PRK10982 86 LQRSVMDNMWLGryptkgmfVDQDKMYRDTKAIFD---ELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 177 ADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-233 |
1.88e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTI---IRLYDATAGEVLFDGENVHGKKSRAelkkfnrKMQMIFQDPYASLN 104
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKY-------PGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 105 PRMTVGdiiaegidihglakskkermdrvhELLNTVGLNKehANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISAL 184
Cdd:cd03233 96 PTLTVR------------------------ETLDFALRCK--GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506991877 185 DVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKY-ISDRIGVMYRGQIV 233
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGRQI 199
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
231-298 |
2.04e-10 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 56.60 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 231 QIVELTTSEELYANPVHPYTKSLLSAIPLPDpdyERNRKRI-----VYDPSQHDYG---------------SEVPTMREI 290
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIK---KRDRKLIsipgeVPSLINLPSGcrfyprcpyaqdecrKEPPALVEI 77
|
....*...
gi 506991877 291 RPGHFVLC 298
Cdd:TIGR01727 78 AEGHRVAC 85
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-224 |
2.30e-10 |
|
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: 59.04 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAELKKfnrkmQMIFQDPYASLNPRMTVG 110
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIAR-----GLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 111 DIIAEGIDIHGlakskkerMDRVHELLNTVGLNK-EHanRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQ 189
Cdd:cd03231 92 ENLRFWHADHS--------DEQVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 506991877 190 AQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRI 224
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-228 |
3.16e-10 |
|
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: 60.95 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYR------GETFGLVGESGCGKSTT------------GR--------TIIRLYdatAGEVLFDgenvHGKKSRAEL 85
Cdd:COG1245 87 GFRLYGlpvpkkGKVTGILGPNGIGKSTAlkilsgelkpnlGDydeepswdEVLKRF---RGTELQD----YFKKLANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFNRKMQMIfqdpyaSLNPRM---TVGDIIaEGIDIHGLAKSKKERMDrvhelLNTVgLNKEHAnrfphEFSGGQRQRI 162
Cdd:COG1245 160 IKVAHKPQYV------DLIPKVfkgTVRELL-EKVDERGKLDELAEKLG-----LENI-LDRDIS-----ELSGGELQRV 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 163 GIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-196 |
4.47e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVHgkKSRAElkkFNRkmQMIFQDPYASLNPRMTV 109
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRDE---YHQ--DLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 gdiiAEGID----IHGLAKSkkermDRVHELLNTVGL-NKEHAnrfP-HEFSGGQRQRIGIARALAVEPEFIIADEPISA 183
Cdd:PRK13538 92 ----LENLRfyqrLHGPGDD-----EALWEALAQVGLaGFEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170
....*....|...
gi 506991877 184 LDVSIQAQVVNLL 196
Cdd:PRK13538 160 IDKQGVARLEALL 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-228 |
4.63e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYR------GETFGLVGESGCGKSTT-----GRTIIRL--YDATAG--EVL--FDG-------ENVHGKKSRAElkk 87
Cdd:PRK13409 87 GFKLYGlpipkeGKVTGILGPNGIGKTTAvkilsGELIPNLgdYEEEPSwdEVLkrFRGtelqnyfKKLYNGEIKVV--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fnRKMQMIFQDPYASlnpRMTVGDIIaEGIDIHGLAKSKKERMdrvhELLNTVglnkehaNRFPHEFSGGQRQRIGIARA 167
Cdd:PRK13409 164 --HKPQYVDLIPKVF---KGKVRELL-KKVDERGKLDEVVERL----GLENIL-------DRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKglTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-213 |
5.24e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 10 EVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVlfdgenvhgkksraelkKFN 89
Cdd:PRK11147 321 EMENV--NYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 90 RKMQMIFQDPY-ASLNPRMTVGDIIAEGidihglaksKKERMdrvhellntVGLNKEHANRFPHEF-------------- 154
Cdd:PRK11147 380 TKLEVAYFDQHrAELDPEKTVMDNLAEG---------KQEVM---------VNGRPRHVLGYLQDFlfhpkramtpvkal 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVsiqaQVVNLLKKLQKEKGLTYLFIAHD 213
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-230 |
9.01e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.73 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 22 GGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvHGKKSRAELKKFNRkmqmiFQDPYA 101
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN-ESEPSFEATRSRNR-----YSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 102 SLNPRM---TVGDIIAEGidihglAKSKKERMDRVHELLNTvglnKEHANRFPH-----------EFSGGQRQRIGIARA 167
Cdd:cd03290 85 AQKPWLlnaTVEENITFG------SPFNKQRYKAVTDACSL----QPDIDLLPFgdqteigergiNLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991877 168 LAVEPEFIIADEPISALDVSIQAQVVN--LLKKLQKEKgLTYLFIAHDLSMVKYiSDRIGVMYRG 230
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-241 |
1.15e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 5 REKLIEVKNVKQHFDVSggvvkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhgkKSRAE 84
Cdd:PRK10982 247 GEVILEVRNLTSLRQPS------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI---NNHNA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 85 LKKFNRKMQMIFQDP-----YASLNprMTVGDIIAEgIDIH----GLAKSKKERMDrVHELLNTVGLNKEHANRFPHEFS 155
Cdd:PRK10982 318 NEAINHGFALVTEERrstgiYAYLD--IGFNSLISN-IRNYknkvGLLDNSRMKSD-TQWVIDSMRVKTPGHRTQIGSLS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 156 GGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKL-QKEKGLtyLFIAHDLSMVKYISDRIGVMYRGQ--- 231
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLvag 471
|
250
....*....|..
gi 506991877 232 IVEL--TTSEEL 241
Cdd:PRK10982 472 IVDTktTTQNEI 483
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-215 |
1.29e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 38 GETFGLVGESGCGKSTtgrtiirLYDATAGEVlfDGENVHGK---KSRAELKKFNRKMQMIFQDPYasLNPRMTVGDIIA 114
Cdd:PLN03211 94 GEILAVLGPSGSGKST-------LLNALAGRI--QGNNFTGTilaNNRKPTKQILKRTGFVTQDDI--LYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 115 eGIDIHGLAKS--KKERMDRVHELLNTVGLNKEH----ANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSI 188
Cdd:PLN03211 163 -FCSLLRLPKSltKQEKILVAESVISELGLTKCEntiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180
....*....|....*....|....*..
gi 506991877 189 QAQVVNLLKKLqKEKGLTYLFIAHDLS 215
Cdd:PLN03211 242 AYRLVLTLGSL-AQKGKTIVTSMHQPS 267
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-233 |
1.99e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.16 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTtgrtiirLYDATA------GEVLFDGENVhGKKSRAELKKFnRKM--QmifQDPYAS 102
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST-------LLARMAgllpgqGEILLNGRPL-SDWSAAELARH-RAYlsQ---QQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 103 LnprMTVGDIIAegidIHGLAK-SKKERMDRVHELLNTVGLNKEhANRFPHEFSGGQRQRIGIARAL-----AVEPE--F 174
Cdd:COG4138 83 A---MPVFQYLA----LHQPAGaSSEAVEQLLAQLAEALGLEDK-LSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 175 IIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-219 |
2.06e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENvhgkksraelkkfnrKMQMIFQDPYASLN--- 104
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG---------------KLFYVPQRPYMTLGtlr 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 105 -----PrMTVGDIIAEGIDIHGLakskKERMDRVH-ELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIAD 178
Cdd:TIGR00954 533 dqiiyP-DSSEDMKRRGLSDKDL----EQILDNVQlTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506991877 179 EPISALDVSIQAQVVNLLkklqKEKGLTYLFIAHDLSMVKY 219
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
155-244 |
2.42e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNllKKLQKE-KGLTYLFIAHDLSMVKYIsDRIGVMYRGQIV 233
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
90
....*....|.
gi 506991877 234 ELTTSEELYAN 244
Cdd:PLN03130 819 EEGTYEELSNN 829
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
153-228 |
2.60e-09 |
|
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: 55.66 E-value: 2.60e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 153 EFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKYISDRIGVMY 228
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-241 |
3.13e-09 |
|
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: 58.10 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 21 SGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVlfdgeNVHGKKSRAELKKFNRKMQMIFQdpY 100
Cdd:TIGR01257 1948 SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDA-----TVAGKSILTNISDVHQNMGYCPQ--F 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 101 ASLNPRMTVGDIIAEGIDIHGLAKSKKERMdrVHELLNTVGLNKeHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEP 180
Cdd:TIGR01257 2021 DAIDDLLTGREHLYLYARLRGVPAEEIEKV--ANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506991877 181 ISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-244 |
4.29e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVlfdgeNVHGKKSRAELKkfnrkmqmifqdpyASLNPR 106
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAIS--------------SGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 MT-VGDIIAEGIdIHGLAKSK-KERMDRVHELLNTvglnkehaNRFPHE----FSGGQRQRIGIARALAVEPEFIIADEp 180
Cdd:PRK13545 100 LTgIENIELKGL-MMGLTKEKiKEIIPEIIEFADI--------GKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDE- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 181 isALDVSIQAQVVNLLKKLQ--KEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEELYAN 244
Cdd:PRK13545 170 --ALSVGDQTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-243 |
5.20e-09 |
|
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: 57.26 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 28 VNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGeNVHGKKSRAELKKFNRKMQMIFQDPyasLNPRM 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSLRENILFGKA---LNEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 108 TVGDIIAEGI--DIHGLAKSkkermDRVHelLNTVGLNkehanrfpheFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:TIGR00957 730 YQQVLEACALlpDLEILPSG-----DRTE--IGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 186 VSIQAQVV-NLLKKLQKEKGLTYLFIAHDLSMVKYIsDRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR00957 793 AHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-224 |
5.91e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.64 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 20 VSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTtgrtiirlydatageVLFDGENVHGKKSRAELKKFNRKMQMIFQDP 99
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEGLYASGKARLISFLPKFSRNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 100 YASLnprmtvgdiiaegIDihglakskkermdrvhellntVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPE--FIIA 177
Cdd:cd03238 68 LQFL-------------ID---------------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506991877 178 DEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKYiSDRI 224
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-234 |
1.19e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVkqHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTII--RLYDATAGEVLFDGENVhgkksrAEL 85
Cdd:PRK09580 1 MLSIKDL--HVSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDL------LEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 86 KKFNRKMQ---MIFQDPY------------ASLNP-RMTVGDIIAEGIDIHGLAKSKKERMDRVHELLN---TVGlnkeh 146
Cdd:PRK09580 71 SPEDRAGEgifMAFQYPVeipgvsnqfflqTALNAvRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTrsvNVG----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 147 anrfpheFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKgLTYLFIAHDLSMVKYIS-DRIG 225
Cdd:PRK09580 146 -------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYQRILDYIKpDYVH 217
|
....*....
gi 506991877 226 VMYRGQIVE 234
Cdd:PRK09580 218 VLYQGRIVK 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-241 |
2.37e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKSTtGRTIIRLYDATAGEVLFDGENVHGkkSRAELKKF 88
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCA--NRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYASLNPRMTVGdIIAEGIDIhglakSKKERMDRVHELLNTVGLNkEHANRFPHEFSGGQRQRIGIARAL 168
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLY-MIGR*LDL-----SRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 169 AVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEkGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-244 |
2.91e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.80 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVK-QHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGENVhGKKSRAELKk 87
Cdd:COG4615 328 LELRGVTyRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-TADNREAYR- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 88 fnrkmQM---IFQDPYasLNPRMtvgdiiaegIDIHGLAKSkkermDRVHELLNTVGLnkEH-----ANRF-PHEFSGGQ 158
Cdd:COG4615 406 -----QLfsaVFSDFH--LFDRL---------LGLDGEADP-----ARARELLERLEL--DHkvsveDGRFsTTDLSQGQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 159 RQRIGIARALAVEPEFIIADEpiSALDvsiQ---------AQvvnLLKKLqKEKGLTYLFIAHDlsmVKYIS--DRIGVM 227
Cdd:COG4615 463 RKRLALLVALLEDRPILVFDE--WAAD---QdpefrrvfyTE---LLPEL-KARGKTVIAISHD---DRYFDlaDRVLKM 530
|
250
....*....|....*..
gi 506991877 228 YRGQIVELTTSEELYAN 244
Cdd:COG4615 531 DYGKLVELTGPAALAAS 547
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-244 |
2.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKlQKEKGLTYLFIAHDLSMVKYIsDRIGVMYRGQIVE 234
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKE 819
|
90
....*....|
gi 506991877 235 LTTSEELYAN 244
Cdd:PLN03232 820 EGTFAELSKS 829
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-233 |
3.76e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 31 ISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDAtAGEVLFDGENVhGKKSRAELKKfnRKMQMIFQDPYASLNPrmtvg 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPL-EAWSAAELAR--HRAYLSQQQTPPFAMP----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 111 diIAEGIDIHGLAKSKKERM-DRVHELLNTVGL-NKEHanRFPHEFSGGQRQRIGIARA-LAVEPE------FIIADEPI 181
Cdd:PRK03695 86 --VFQYLTLHQPDKTRTEAVaSALNEVAEALGLdDKLG--RSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506991877 182 SALDVSIQAQVVNLLKKLQkEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIV 233
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-224 |
1.70e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 38 GETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGenvhgkksraelkkfNRKMQMIFQDPYASLNPRMTV---GD--- 111
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------------NWQLAWVNQETPALPQPALEYvidGDrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 112 --------IIAEGIDIHGLA--KSKKERMD------RVHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFI 175
Cdd:PRK10636 92 rqleaqlhDANERNDGHAIAtiHGKLDAIDawtirsRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506991877 176 IADEPISALDVSiqaQVVNLLKKLQKEKGlTYLFIAHDLSMVKYISDRI 224
Cdd:PRK10636 172 LLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-213 |
3.33e-07 |
|
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: 48.91 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 37 RGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLF-DGENvhgkksraelkkfnrkmqmifqdpyaslnprmtvgdiiae 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGED---------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 116 gidihglakskkermdrvHELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQV--- 192
Cdd:smart00382 41 ------------------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLlll 102
|
170 180
....*....|....*....|...
gi 506991877 193 --VNLLKKLQKEKGLTYLFIAHD 213
Cdd:smart00382 103 eeLRLLLLLKSEKNLTVILTTND 125
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-281 |
6.18e-07 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 45.85 E-value: 6.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 506991877 233 VELTTSEELYANPVHPYTKSLLSAIPLPDP--DYERNRKRIVYDPSQHDYG 281
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPpkRPLYTIPGNVPSLLELPEG 51
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-241 |
6.45e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 27 AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGEnvhgkksrAELKKFNrkmqmifqdpyASLNPR 106
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------VSVIAIS-----------AGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 107 MTVGDIIAEGIDIHGLA-KSKKERMDRVHElLNTVGlnkEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEpisALD 185
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKrKEIKAMTPKIIE-FSELG---EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506991877 186 VSIQAQVVNLLKKLQ--KEKGLTYLFIAHDLSMVKYISDRIGVMYRGQIVELTTSEEL 241
Cdd:PRK13546 173 VGDQTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-186 |
1.30e-06 |
|
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: 49.55 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKNVKQHFDvsGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFdGENVH---GKKSR 82
Cdd:TIGR03719 320 DKVIEAENLTKAFG--DKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayVDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 83 aelkkfnrkmqmifqdpyASLNPRMTVGDIIAEGIDIhgLAKSKKERMDRVH-ELLNTVGLNKEhanRFPHEFSGGQRQR 161
Cdd:TIGR03719 395 ------------------DALDPNKTVWEEISGGLDI--IKLGKREIPSRAYvGRFNFKGSDQQ---KKVGQLSGGERNR 451
|
170 180
....*....|....*....|....*
gi 506991877 162 IGIARALAVEPEFIIADEPISALDV 186
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-186 |
1.72e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 16 QHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIrlYDATAG-----EVLFDGENVHGKKSRA------- 83
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGipkncQILHVEQEVVGDDTTAlqcvlnt 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 --ELKKFNRKMQMIFQDPYASLNPRMTVGDIIAEGIDIHGLAKSKK-----ERMD---------RVHELLNTVGLNKEHA 147
Cdd:PLN03073 259 diERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRleeiyKRLElidaytaeaRAASILAGLSFTPEMQ 338
|
170 180 190
....*....|....*....|....*....|....*....
gi 506991877 148 NRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDV 186
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-233 |
2.02e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 32 SFDIYR--------GETFGLVGESGCGKSTTGRTI-IRLYD---ATAGEVLFDGenvHGKksrAELKKFNRKMQMifqdp 99
Cdd:TIGR00956 73 TFDILKpmdglikpGELTVVLGRPGSGCSTLLKTIaSNTDGfhiGVEGVITYDG---ITP---EEIKKHYRGDVV----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 100 YASLN----PRMTVGDII-----AEGIDIHGLAKSKKERMDRVHEL-LNTVGL----NKEHANRFPHEFSGGQRQRIGIA 165
Cdd:TIGR00956 142 YNAETdvhfPHLTVGETLdfaarCKTPQNRPDGVSREEYAKHIADVyMATYGLshtrNTKVGNDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 166 RALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKEKGLTYLFIAHDLSMVKY-ISDRIGVMYRGQIV 233
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQI 290
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-180 |
2.75e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFdvsgGVVKAVNDISFDIYRGETFGLVGESGCGKST-----TGRTIIRlydatAGEVLFDGENVHGKKSRA 83
Cdd:NF033858 2 ARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSllsliAGARKIQ-----QGRVEVLGGDMADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 84 ELKKfnRKMQMifqdP-------YASLNprmtvgdiIAEGIDIHG--LAKSKKERMDRVHELLNTVGLNkehanRFPH-- 152
Cdd:NF033858 73 AVCP--RIAYM----PqglgknlYPTLS--------VFENLDFFGrlFGQDAAERRRRIDELLRATGLA-----PFADrp 133
|
170 180 190
....*....|....*....|....*....|
gi 506991877 153 --EFSGGQRQRIGIARALAVEPEFIIADEP 180
Cdd:NF033858 134 agKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-213 |
4.91e-06 |
|
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: 48.01 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 23 GVVKAVN-------DISFDIYRGETFGLVGESGCGKSTTGRTIirlydatAG-EVLFDGENVHGKksraelkkfNRKMQM 94
Cdd:TIGR03719 9 RVSKVVPpkkeilkDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGvDKDFNGEARPQP---------GIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 95 IFQDPYasLNPRMTVGDIIAEGI----------------------DIHGLAkskkERMDRVHELLNTVG---LNKE---- 145
Cdd:TIGR03719 73 LPQEPQ--LDPTKTVRENVEEGVaeikdaldrfneisakyaepdaDFDKLA----AEQAELQEIIDAADawdLDSQleia 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991877 146 -HANRFP------HEFSGGQRQRIGIARALAVEPEFIIADEPISALDvsiqAQVVNLLKK-LQKEKGlTYLFIAHD 213
Cdd:TIGR03719 147 mDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPG-TVVAVTHD 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-199 |
5.61e-06 |
|
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: 46.08 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 12 KNVKQHFDVSGGVVKAVNDISFDIYRGETFGLVGESGCGKST-----TGRTIIRLydaTAGEVLFDGenvhgkksRAELK 86
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGV---ITGEILING--------RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 KFNRkmqmifqdpyaslnprmTVGdiIAEGIDIHgLAKSKKERMDRVHELLNtvGLNKEhanrfphefsggQRQRIGIAR 166
Cdd:cd03232 76 NFQR-----------------STG--YVEQQDVH-SPNLTVREALRFSALLR--GLSVE------------QRKRLTIGV 121
|
170 180 190
....*....|....*....|....*....|...
gi 506991877 167 ALAVEPEFIIADEPISALDVSIQAQVVNLLKKL 199
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-189 |
1.16e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 9 IEVKNVKQHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDaTAGEVLFDGENVhgkkSRAELKKF 88
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSW----NSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 89 NRKMQMIFQDPYASLNPrmtvgdiIAEGIDIHGlaKSKKERMDRVHEllnTVGLnKEHANRFPHE-----------FSGG 157
Cdd:cd03289 76 RKAFGVIPQKVFIFSGT-------FRKNLDPYG--KWSDEEIWKVAE---EVGL-KSVIEQFPGQldfvlvdggcvLSHG 142
|
170 180 190
....*....|....*....|....*....|...
gi 506991877 158 QRQRIGIARALAVEPEFIIADEPISALD-VSIQ 189
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-189 |
4.23e-05 |
|
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: 45.29 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 8 LIEVKNVKQ------HFDVSGGVVK-------AVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYdATAGEVLFDGE 74
Cdd:TIGR01271 1202 VIENPHAQKcwpsggQMDVQGLTAKyteagraVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGV 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 75 NVHGKKSRAELKKFNRKMQMIFqdpyaslnprmTVGDIIAEGIDIHglAKSKKERMDRVHEllnTVGLnKEHANRFPHE- 153
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVF-----------IFSGTFRKNLDPY--EQWSDEEIWKVAE---EVGL-KSVIEQFPDKl 1343
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 506991877 154 ----------FSGGQRQRIGIARALAVEPEFIIADEPISALD-VSIQ 189
Cdd:TIGR01271 1344 dfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-243 |
2.08e-04 |
|
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: 42.98 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 24 VVKAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIrlydatagevlfdgenvhgkksrAELKKFNRKMQMIFQDPYASL 103
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-----------------------GELEPSEGKIKHSGRISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 NPRMTVGdIIAEGIdIHGLAKSKKermdRVHELLNTVGLnKEHANRFPHE-----------FSGGQRQRIGIARALAVEP 172
Cdd:TIGR01271 495 TSWIMPG-TIKDNI-IFGLSYDEY----RYTSVIKACQL-EEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDA 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991877 173 EFIIADEPISALDVSIQAQVV-NLLKKLQKEKglTYLFIAHDLSMVKYiSDRIGVMYRGQIVELTTSEELYA 243
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFeSCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQA 636
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-186 |
4.22e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 7 KLIEVKNVKQHFdvsGGVVkAVNDISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFdGENVhgkksraelk 86
Cdd:PRK11819 323 KVIEAENLSKSF---GDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 87 kfnrkmQMIFQDPY-ASLNPRMTVGDIIAEGIDIHGLAksKKERMDRVHellntVGlnkehanRFphEF----------- 154
Cdd:PRK11819 388 ------KLAYVDQSrDALDPNKTVWEEISGGLDIIKVG--NREIPSRAY-----VG-------RF--NFkggdqqkkvgv 445
|
170 180 190
....*....|....*....|....*....|...
gi 506991877 155 -SGGQRQRIGIARALAVEPEFIIADEPISALDV 186
Cdd:PRK11819 446 lSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-239 |
5.32e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 6 EKLIEVKN-VKQHFDVSGGVVkaVNDISFDIYRGETFGLVGESGCGK-----STTGRTIIRlydATAGEVLFDGENVHGK 79
Cdd:NF040905 255 EVVFEVKNwTVYHPLHPERKV--VDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGR---NISGTVFKDGKEVDVS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 80 KSRAELKKF------NRKmqmifqdpYASLNprmtVGDIIAEGIDIHGLAK-SKKERMDRVHELLNTVGLNKEHANRFPH 152
Cdd:NF040905 330 TVSDAIDAGlayvteDRK--------GYGLN----LIDDIKRNITLANLGKvSRRGVIDENEEIKVAEEYRKKMNIKTPS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 153 EF------SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLKKLQKE-KGLtyLFIAHDLSMVKYISDRIG 225
Cdd:NF040905 398 VFqkvgnlSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGV--IVISSELPELLGMCDRIY 475
|
250
....*....|....*
gi 506991877 226 VMYRGQIV-ELTTSE 239
Cdd:NF040905 476 VMNEGRITgELPREE 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
131-185 |
5.74e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 5.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 506991877 131 DRVHEL----LNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:PRK10938 375 DRQQKLaqqwLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
155-246 |
6.33e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 155 SGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVN--LLKKLqkeKGLTYLFIAHDLSMVKYiSDRIGVMYRGQI 232
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGAL---AGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
90
....*....|....
gi 506991877 233 VELTTSEELYANPV 246
Cdd:PTZ00243 860 EFSGSSADFMRTSL 873
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-241 |
6.53e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.61 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 30 DISFDIYRGETFGLVGESGCGKSTTGRTIIRLYDATAGEVLFDGEnVHGKKSRAELKKFNRKMQMIFQDPYASLNPRMTV 109
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 110 GdiiaegidihglAKSKKERMDRVHELLNTV----GLNkehanrfpheFSGGQRQRIGIARALAVEPEFIIADEPISALD 185
Cdd:cd03291 134 K------------ACQLEEDITKFPEKDNTVlgegGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506991877 186 VSIQAQVV-NLLKKLQKEKglTYLFIAHDLSMVKyISDRIGVMYRGQIVELTTSEEL 241
Cdd:cd03291 192 VFTEKEIFeSCVCKLMANK--TRILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 245
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-260 |
1.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 132 RVHELLNtVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFI--IADEPISALDVSIQAQVVNLLKKLqKEKGLTYLF 209
Cdd:PRK00635 456 RLSILID-LGLPYLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLL 533
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 210 IAHDLSMVKYiSDRI------GVMYRGQIVELTTSEELYANPvHPYTKSLLS---AIPLP 260
Cdd:PRK00635 534 VEHDEQMISL-ADRIidigpgAGIFGGEVLFNGSPREFLAKS-DSLTAKYLRqelTIPIP 591
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
125-199 |
1.72e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 125 SKKERMDRVHELLNTV---------------GLNKEhanrfphefsggQRQRIGIARALAVEPEFII-ADEPISALDVSI 188
Cdd:TIGR00956 870 SKSEKMEYVEEVIKLLemesyadavvgvpgeGLNVE------------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
90
....*....|.
gi 506991877 189 QAQVVNLLKKL 199
Cdd:TIGR00956 938 AWSICKLMRKL 948
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-241 |
2.53e-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: 39.61 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 135 ELLNTVGLNKEHANRFPHEFSGGQRQRIGIARAL---AVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGLTYLFIA 211
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIE 889
|
90 100 110
....*....|....*....|....*....|....*.
gi 506991877 212 HDLSMVKyISDRI------GVMYRGQIVELTTSEEL 241
Cdd:TIGR00630 890 HNLDVIK-TADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
125-193 |
6.82e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.29 E-value: 6.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506991877 125 SKKERMDRVHELLNTVGLN--KEHANRFP--HEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVV 193
Cdd:PLN03140 987 SKEEKMMFVDEVMELVELDnlKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-222 |
9.24e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 132 RVHELLNT---VGLNKEHANRFPHEFSGGQRQRIGIARAL---AVEPEFIIADEPISALDVSIQAQVVNLLKKLqKEKGL 205
Cdd:cd03271 145 KIARKLQTlcdVGLGYIKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGN 223
|
90 100
....*....|....*....|
gi 506991877 206 TYLFIAHDLSMVK---YISD 222
Cdd:cd03271 224 TVVVIEHNLDVIKcadWIID 243
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
104-224 |
9.26e-03 |
|
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: 36.85 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991877 104 NPRMTVGDIiAEGIDIHGLAKSK---KERMdrvhELLNTVGLNKEHANRFPHEFSGGQRQRIGIARALAVEPEFI--IAD 178
Cdd:cd03270 90 NPRSTVGTV-TEIYDYLRLLFARvgiRERL----GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVlyVLD 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 506991877 179 EPISALDVSIQAQVVNLLKKLqKEKGLTYLFIAHDLSMVKyISDRI 224
Cdd:cd03270 165 EPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR-AADHV 208
|
|
| |
