|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-328 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 637.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 3 AANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ 82
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISNLSEEKLRKsVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFS 162
Cdd:COG4608 81 DITGLSGRELRP-LRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMEL 242
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 243 TGKFELYDNPLHPYTQALLSSVPVTRKRGsvKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEAAPSHF 322
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAVPVPDPER--RRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQ 317
|
....*.
gi 2181075557 323 VACHLY 328
Cdd:COG4608 318 VACHLA 323
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-328 |
0e+00 |
|
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: 530.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP---TEGQILFKGQDIS 85
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 86 NLSEEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHP--SFAGRYPHEFSG 163
Cdd:COG0444 74 KLSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELT 243
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 244 GKFELYDNPLHPYTQALLSSVPVTRKRGsvkRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEAAPSHFV 323
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPDG---RRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRV 310
|
....*
gi 2181075557 324 ACHLY 328
Cdd:COG0444 311 ACHLY 315
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-326 |
1.53e-166 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 466.36 E-value: 1.53e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFPIRSGLFqRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGR--TMIRlyKPTEGQILFKGQD 83
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARllTMIE--TPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 ISNLSEEKlRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSG 163
Cdd:PRK11308 79 LLKADPEA-QKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELT 243
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 244 GKFELYDNPLHPYTQALLSSVPvtRKRGSVKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEAApSHFV 323
Cdd:PRK11308 238 TKEQIFNNPRHPYTQALLSATP--RLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYD-GRLV 314
|
...
gi 2181075557 324 ACH 326
Cdd:PRK11308 315 ACF 317
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-325 |
2.97e-157 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 442.99 E-value: 2.97e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 2 TAANQETILELRDVKKYFPIRSG--LFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILF 79
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 80 KGQDISNLSEEKLRKsVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNT-HNMYTMRERNEKVEELLARVGLHPSFAGRYP 158
Cdd:PRK15079 81 LGKDLLGMKDDEWRA-VRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 159 HEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 239 MMELTGKFELYDNPLHPYTQALLSSVPVTrkrgSVKRERI----VLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEF 314
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVPIP----DPDLERNktiqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL 315
|
330
....*....|.
gi 2181075557 315 kEAAPSHFVAC 325
Cdd:PRK15079 316 -EGSFRHAVSC 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-266 |
7.64e-152 |
|
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: 436.26 E-value: 7.64e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 2 TAANQETILELRDVKKYFPIRSGlfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKG 81
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEKLRKsVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEF 161
Cdd:COG1123 327 KDLTKLSRRSLRE-LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
250 260
....*....|....*....|....*
gi 2181075557 242 LTGKFELYDNPLHPYTQALLSSVPV 266
Cdd:COG1123 486 DGPTEEVFANPQHPYTRALLAAVPS 510
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-265 |
9.04e-145 |
|
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: 418.70 E-value: 9.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 3 AANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYkPTEGQILFKGQ 82
Cdd:COG4172 269 PPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISNLSEEKLRkSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNM-YTMRERNEKVEELLARVGLHPSFAGRYPHEF 161
Cdd:COG4172 348 DLDGLSRRALR-PLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGLDPAARHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....
gi 2181075557 242 LTGKFELYDNPLHPYTQALLSSVP 265
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-241 |
8.16e-127 |
|
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: 361.82 E-value: 8.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsglfqRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:cd03257 1 LLEVKNLSVSFP-------TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EeKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYT-MRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQ 167
Cdd:cd03257 74 R-RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-265 |
4.87e-117 |
|
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: 337.93 E-value: 4.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNlse 89
Cdd:COG1124 2 LEVRNLSVSYGQGGR-------RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMytmRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRI 169
Cdd:COG1124 72 -RRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGL---PDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELY 249
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 2181075557 250 DNPLHPYTQALLSSVP 265
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-324 |
1.66e-108 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 329.12 E-value: 1.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 2 TAANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKG 81
Cdd:PRK10261 306 TVVDGEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEKLrKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEF 161
Cdd:PRK10261 386 QRIDTLSPGKL-QALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 242 LTGKFELYDNPLHPYTQALLSSVPVTRKrGSVKRERIVLKGELPSPanppkgcvFHTRCPVAKPIckeqipEFKEAAPSH 321
Cdd:PRK10261 545 IGPRRAVFENPQHPYTRKLMAAVPVADP-SRQRPQRVLLSDDLPSN--------IHLRGEEVAAV------SLQCVGPGH 609
|
...
gi 2181075557 322 FVA 324
Cdd:PRK10261 610 YVA 612
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-283 |
1.96e-97 |
|
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: 297.75 E-value: 1.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKkyfpIRsglFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP----TEGQILFK 80
Cdd:COG4172 2 MSMPLLSVEDLS----VA---FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDISNLSEEKLRKsVRKN-IQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLH-PSF-AGRY 157
Cdd:COG4172 75 GQDLLGLSERELRR-IRGNrIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPERrLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 158 PHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLG 237
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2181075557 238 KMMELTGKFELYDNPLHPYTQALLSSVPVTRKRGSVKRERIVLKGE 283
Cdd:COG4172 234 EIVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-263 |
1.64e-96 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 286.35 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSGLFQRKvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ---- 82
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRRQ--QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkley 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 -DISNLSeeklrksvrKNIQMVFQDPFASLNPRKTLRSIIKEP--FNTHnmYTMRERNEKVEELLARVGLHPSFAGRYPH 159
Cdd:COG4167 80 gDYKYRC---------KHIRMIFQDPNTSLNPRLNIGQILEEPlrLNTD--LTAEEREERIFATLRLVGLLPEHANFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 160 EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 2181075557 240 MELTGKFELYDNPLHPYTQALLSS 263
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTKRLIES 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-326 |
1.90e-85 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 260.43 E-value: 1.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAANQETILELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKS-TAGRTMIRLYKP--TEGQI 77
Cdd:PRK09473 4 LAQQQADALLDVKDLRVTFSTPDG-------DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 78 LFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLhPSFAGR- 156
Cdd:PRK09473 77 TFNGREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 157 --YPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:PRK09473 156 kmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 235 YLGKMMELTGKFELYDNPLHPYTQALLSSVPvtrkrgsvkreRIVLKGE-LPS-PANP------PKGCVFHTRCPVAKPI 306
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQPSHPYSIGLLNAVP-----------RLDAEGEsLLTiPGNPpnllrlPKGCPFQPRCPHAMEI 304
|
330 340
....*....|....*....|
gi 2181075557 307 CKEQiPEFKEAAPSHFVACH 326
Cdd:PRK09473 305 CSSA-PPLEEFGPGRLRACF 323
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-262 |
6.83e-84 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 262.72 E-value: 6.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 3 AANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYkPTEGQILFKGQ 82
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISNLSEEKLRkSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHN-MYTMRERNEKVEELLARVGLHPSFAGRYPHEF 161
Cdd:PRK15134 348 PLHNLNRRQLL-PVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
250 260
....*....|....*....|.
gi 2181075557 242 LTGKFELYDNPLHPYTQALLS 262
Cdd:PRK15134 507 QGDCERVFAAPQQEYTRQLLA 527
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
8-268 |
2.92e-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: 247.41 E-value: 2.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFpiRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNL 87
Cdd:TIGR02769 1 SLLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 88 SEEKlRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQ 167
Cdd:TIGR02769 79 DRKQ-RRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFE 247
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
250 260
....*....|....*....|....*
gi 2181075557 248 LyDNPLHPYTQALLSSV----PVTR 268
Cdd:TIGR02769 238 L-LSFKHPAGRNLQSAVlpehPVRR 261
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-277 |
9.13e-78 |
|
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: 246.35 E-value: 9.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPirsglfqrkVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPT---EGQILFKGQD 83
Cdd:COG1123 2 TPLLEVRDLSVRYP---------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 ISNLSEEKLRKSvrknIQMVFQDPFASLNPRkTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSG 163
Cdd:COG1123 73 LLELSEALRGRR----IGMVFQDPMTQLNPV-TVGDQIAEALENLGL-SRAEARARVLELLEAVGL-ERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELT 243
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260 270
....*....|....*....|....*....|....
gi 2181075557 244 GKFELYDNPlhpytqALLSSVPVTRKRGSVKRER 277
Cdd:COG1123 226 PPEEILAAP------QALAAVPRLGAARGRAAPA 253
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
34-326 |
7.55e-76 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 235.79 E-value: 7.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLY----KPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFA 109
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 110 SLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLhPSFAGR---YPHEFSGGQRQRIGIARALTLNPELIIADE 186
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 187 PVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLSSVPv 266
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP- 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 267 trkRGSVKRERIV-LKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKeAAPSHFVACH 326
Cdd:PRK11022 259 ---EFAQDKARLAsLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALN-MLAGRQSKCH 315
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-268 |
2.18e-74 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 229.96 E-value: 2.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFpiRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNL 87
Cdd:PRK10419 2 TLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 88 SEEKlRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQ 167
Cdd:PRK10419 80 NRAQ-RKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME-----L 242
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpvgD 238
|
250 260 270
....*....|....*....|....*....|
gi 2181075557 243 TGKFElydnplHPYTQALLSSV----PVTR 268
Cdd:PRK10419 239 KLTFS------SPAGRVLQNAVlpafPVRR 262
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-265 |
4.46e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.50 E-value: 4.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsglfqRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:COG1135 1 MIELENLSKTFP-------TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKsVRKNIQMVFQDpFASLNpRKT--------LRsIIKEPfnthnmytMRERNEKVEELLARVGLhPSFAGRYPHE 160
Cdd:COG1135 74 ERELRA-ARRKIGMIFQH-FNLLS-SRTvaenvalpLE-IAGVP--------KAEIRKRVAELLELVGL-SDKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260
....*....|....*....|....*.
gi 2181075557 241 ElTGK-FELYDNPLHPYTQALLSSVP 265
Cdd:COG1135 221 E-QGPvLDVFANPQSELTRRFLPTVL 245
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
7-263 |
3.93e-69 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 216.58 E-value: 3.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSGLFQRKvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISn 86
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFRRQ--TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEEKLRKsvrKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQR 166
Cdd:PRK15112 79 FGDYSYRS---QRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKF 246
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*..
gi 2181075557 247 ELYDNPLHPYTQALLSS 263
Cdd:PRK15112 236 DVLASPLHELTKRLIAG 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-261 |
8.49e-69 |
|
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: 214.84 E-value: 8.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIS 85
Cdd:COG1127 2 SEPMIEVRNLTKSF-----------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 86 NLSEEKLRKsVRKNIQMVFQDP--FASLNprktlrsiIKE----PFNTHNMYTMRERNEKVEELLARVGLhPSFAGRYPH 159
Cdd:COG1127 71 GLSEKELYE-LRRRIGMLFQGGalFDSLT--------VFEnvafPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 160 EFSGGQRQRIGIARALTLNPELIIADEPVSALDvSIQAQVIN-LMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLD-PITSAVIDeLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
250 260
....*....|....*....|....
gi 2181075557 239 MMElTGKF-ELYDNPlHPYTQALL 261
Cdd:COG1127 220 IIA-EGTPeELLASD-DPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-252 |
7.56e-68 |
|
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: 212.06 E-value: 7.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:cd03258 1 MIELKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKsVRKNIQMVFQDpFASLNpRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQR 168
Cdd:cd03258 74 GKELRK-ARRRIGMIFQH-FNLLS-SRTVFENVALPLEIAGV-PKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 169 IGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFEL 248
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
....
gi 2181075557 249 YDNP 252
Cdd:cd03258 229 FANP 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
31-326 |
1.23e-67 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 214.77 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP----TEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQD 106
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 107 PFASLNPRKTL-----RSIIKEPFNTHNMYTMRERNEKVEELLARVGL--HPSFAGRYPHEFSGGQRQRIGIARALTLNP 179
Cdd:COG4170 98 PSSCLDPSAKIgdqliEAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQA 259
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 260 LLSSVPVTRKRGSVKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIP--EFKEaapsHFVACH 326
Cdd:COG4170 258 LLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRlrKIKG----HEFACH 322
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-265 |
3.04e-67 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 219.58 E-value: 3.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFpiRSGLFQRKVgdvkaVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYkPT------EGQILFKG 81
Cdd:PRK15134 4 PLLAIENLSVAF--RQQQTVRTV-----VNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEKLRKsVRKN-IQMVFQDPFASLNPRKTLRSIIKEPFNTHNmyTMRERNEKVEEL--LARVGLHPSfAGR-- 156
Cdd:PRK15134 76 ESLLHASEQTLRG-VRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR--GMRREAARGEILncLDRVGIRQA-AKRlt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 157 -YPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMY 235
Cdd:PRK15134 152 dYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270
....*....|....*....|....*....|
gi 2181075557 236 LGKMMELTGKFELYDNPLHPYTQALLSSVP 265
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPTHPYTQKLLNSEP 261
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-238 |
8.69e-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: 201.58 E-value: 8.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03261 1 IELRGLTKSF-----------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKsVRKNIQMVFQDP--FASLnprkTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQ 167
Cdd:cd03261 70 AELYR-LRRRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDvSIQAQVI-NLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLD-PIASGVIdDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
31-326 |
1.38e-60 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 196.56 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP----TEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQD 106
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 107 PFASLNP-----RKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGL--HPSFAGRYPHEFSGGQRQRIGIARALTLNP 179
Cdd:PRK15093 98 PQSCLDPservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIkdHKDAMRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQA 259
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 260 LLSSVPVTRKRGSVKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQiPEFKeAAPSHFVACH 326
Cdd:PRK15093 258 LIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRLT-GAKNHLYACH 322
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-264 |
4.95e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 195.79 E-value: 4.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 11 ELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEE 90
Cdd:PRK11153 3 ELKNISKVFPQGGR-------TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 91 KLRKsVRKNIQMVFQDpFASLNPRkTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIG 170
Cdd:PRK11153 76 ELRK-ARRQIGMIFQH-FNLLSSR-TVFDNVALPLELAGT-PKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 171 IARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYD 250
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
250
....*....|....
gi 2181075557 251 NPLHPYTQALLSSV 264
Cdd:PRK11153 231 HPKHPLTREFIQST 244
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-256 |
8.09e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 195.32 E-value: 8.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFK 80
Cdd:COG3842 2 AMPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmiAG-----FETPDSGRILLD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDISNLSEEKlrksvRkNIQMVFQDpFAsLNPRKT--------LRsiikepfnthnmytMR-----ERNEKVEELLARV 147
Cdd:COG3842 66 GRDVTGLPPEK-----R-NVGMVFQD-YA-LFPHLTvaenvafgLR--------------MRgvpkaEIRARVAELLELV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 148 GLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHD----LSv 223
Cdd:COG3842 124 GL-EGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA- 201
|
250 260 270
....*....|....*....|....*....|...
gi 2181075557 224 vrhISDRVGVMYLGKMMELTGKFELYDNPLHPY 256
Cdd:COG3842 202 ---LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-231 |
1.30e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 190.64 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKG 81
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnilGG-----LDRPTSGEVLIDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEKLRKSVRKNIQMVFQDPFasLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEF 161
Cdd:COG1136 70 QDISSLSERELARLRRRHIGFVFQFFN--LLPELTALENVALPLLLAGV-SRKERRERARELLERVGL-GDRLDHRPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRV 231
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRV 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-231 |
8.11e-59 |
|
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: 188.47 E-value: 8.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03255 1 IELKNLSKTY-------GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQMVFQDPfaSLNPRKTLRSIIKEPFnthnMYT---MRERNEKVEELLARVGLhPSFAGRYPHEFSGGQR 166
Cdd:cd03255 74 KELAAFRRRHIGFVFQSF--NLLPDLTALENVELPL----LLAgvpKKERRERAEELLERVGL-GDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRV 231
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRI 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-268 |
2.63e-58 |
|
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: 189.01 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDp 107
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 FAsLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:cd03294 111 FA-LLPHRTVLENVAFGLEVQGV-PRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 188 VSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLSSVPVT 267
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRA 267
|
.
gi 2181075557 268 R 268
Cdd:cd03294 268 K 268
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-251 |
5.70e-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: 5.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNL 87
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 88 SEEKLRKsVRKNIQMVFQDPfaSLNPRKT---------------LRSIIkepfnthNMYTMRERnEKVEELLARVGLhPS 152
Cdd:COG3638 71 RGRALRR-LRRRIGMIFQQF--NLVPRLSvltnvlagrlgrtstWRSLL-------GLFPPEDR-ERALEALERVGL-AD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 153 FAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVG 232
Cdd:COG3638 139 KAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
250 260
....*....|....*....|....*..
gi 2181075557 233 VMYLGKMM------ELTGKF--ELYDN 251
Cdd:COG3638 219 GLRDGRVVfdgppaELTDAVlrEIYGG 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-265 |
2.15e-57 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 195.46 E-value: 2.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ----------DISNLSEEKLRKS 95
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 96 VRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFA--GRYPHEFSGGQRQRIGIAR 173
Cdd:PRK10261 102 RGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 174 ALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPL 253
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
250
....*....|..
gi 2181075557 254 HPYTQALLSSVP 265
Cdd:PRK10261 262 HPYTRALLAAVP 273
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-264 |
9.10e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 183.66 E-value: 9.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsNLS 88
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKsVRKNIQMVFQDpFaSLNPRKT-LRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQ 167
Cdd:COG1126 69 KKDINK-LRRKVGMVFQQ-F-NLFPHLTvLENVTLAPIKVKKM-SKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFE 247
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
250
....*....|....*..
gi 2181075557 248 LYDNPLHPYTQALLSSV 264
Cdd:COG1126 223 FFENPQHERTRAFLSKV 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-252 |
1.43e-55 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 180.96 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03295 1 IEFENVTKRYG----------GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQMVfqdpfaSLNPRKTLR-------SIIKEPfnthnmytMRERNEKVEELLARVGLHP-SFAGRYPHEF 161
Cdd:cd03295 71 VELRRKIGYVIQQI------GLFPHMTVEenialvpKLLKWP--------KEKIRERADELLALVGLDPaEFADRYPHEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
250
....*....|.
gi 2181075557 242 LTGKFELYDNP 252
Cdd:cd03295 217 VGTPDEILRSP 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
1.54e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 181.44 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAAnqETILELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEG 75
Cdd:COG1116 1 MSAA--APALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTllrliAG-----LEKPTSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 76 QILFKGQDISNLSEEklrksvrknIQMVFQDPfaSLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPsFAG 155
Cdd:COG1116 67 EVLVDGKPVTGPGPD---------RGVVFQEP--ALLPWLTVLDNVALGLELRGV-PKAERRERARELLELVGLAG-FED 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 156 RYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV----SIQaqviNLMEELQEEFNLTYLFISHDLS-VVRhISDR 230
Cdd:COG1116 134 AYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVDeAVF-LADR 208
|
....
gi 2181075557 231 VGVM 234
Cdd:COG1116 209 VVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-234 |
2.25e-55 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 179.59 E-value: 2.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsglfqRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlse 89
Cdd:cd03293 1 LEVRNVSKTYG-------GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklrkSVRKNIQMVFQDPfaSLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRI 169
Cdd:cd03293 70 -----GPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGV-PKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-238 |
3.18e-55 |
|
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: 178.87 E-value: 3.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03259 1 LELKGLSKTY-----------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EklrksvRKNIQMVFQDPfaSLNPRKTLRSIIKEPFNTHNMYTmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRI 169
Cdd:cd03259 70 E------RRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPK-AEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-234 |
3.90e-55 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 181.83 E-value: 3.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 11 ELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRtMI-RLYKPTEGQILFKGQDISNLSE 89
Cdd:COG1125 3 EFENVTKRYP----------DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLR-MInRLIEPTSGRILIDGEDIRDLDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKS---------------VRKNIQMVfqdpfaslnPRktlrsIIKEPfnthnmytmRER-NEKVEELLARVGLHPS- 152
Cdd:COG1125 72 VELRRRigyviqqiglfphmtVAENIATV---------PR-----LLGWD---------KERiRARVDELLELVGLDPEe 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 153 FAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVG 232
Cdd:COG1125 129 YRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIA 208
|
..
gi 2181075557 233 VM 234
Cdd:COG1125 209 VM 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-238 |
5.71e-54 |
|
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: 174.68 E-value: 5.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlSE 89
Cdd:cd03229 1 LELKNVSKRY-----------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--DL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQMVFQDPfaSLNPRKTLRSIIKEPFnthnmytmrernekveellarvglhpsfagryphefSGGQRQRI 169
Cdd:cd03229 68 EDELPPLRRRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-240 |
6.14e-53 |
|
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: 173.67 E-value: 6.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlse 89
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQMVFQDP----FASlnprktlrSIIKE----PFNTHnmYTMRERNEKVEELLARVGLHpSFAGRYPHEF 161
Cdd:COG1122 67 KKNLRELRRKVGLVFQNPddqlFAP--------TVEEDvafgPENLG--LPREEIRERVEEALELVGLE-HLADRPPHEL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-234 |
9.42e-53 |
|
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: 172.71 E-value: 9.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsNLSE 89
Cdd:cd03262 1 IEIKNLHKSF-----------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKsVRKNIQMVFQDpFaSLNPRKT-LRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQR 168
Cdd:cd03262 69 KNINE-LRQKVGMVFQQ-F-NLFPHLTvLENITLAPIKVKGM-SKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 169 IGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFM 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-239 |
2.65e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.17 E-value: 2.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EklrksVRKNIQMVFQDP--FASLNPRKTLRSIIKepfnthnMYTM--RERNEKVEELLARVGLHPsFAGRYPHEFSGGQ 165
Cdd:COG1131 70 E-----VRRRIGYVPQEPalYPDLTVRENLRFFAR-------LYGLprKEARERIDELLELFGLTD-AADRKVGTLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 166 RQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-241 |
7.90e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 170.82 E-value: 7.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK-----PTEGQILFKGQDI 84
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKLrkSVRKNIQMVFQDPfaslNP-RKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGR-YPHEFS 162
Cdd:cd03260 70 YDLDVDVL--ELRRRVGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDvSIQAQVI-NLMEELQEEfnLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALD-PISTAKIeELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
26-238 |
2.96e-51 |
|
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: 168.80 E-value: 2.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQ 105
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DPFASL-NPrkTLRSIIKepFNTHNMYTMR-ERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:cd03225 83 NPDDQFfGP--TVEEEVA--FGLENLGLPEeEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-249 |
5.71e-51 |
|
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: 168.90 E-value: 5.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 24 GLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRkSVRKNIQMV 103
Cdd:cd03256 5 NLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALR-QLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 104 FQDP-------------FASLNPRKTLRSIIkepfnthNMYTMRERnEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIG 170
Cdd:cd03256 84 FQQFnlierlsvlenvlSGRLGRRSTWRSLF-------GLFPKEEK-QRALAALERVGLL-DKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 171 IARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDR-VG-----VMYLGKMMELTG 244
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRiVGlkdgrIVFDGPPAELTD 234
|
....*..
gi 2181075557 245 KF--ELY 249
Cdd:cd03256 235 EVldEIY 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-231 |
5.92e-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: 166.32 E-value: 5.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:TIGR02315 1 MLEVENLSKVYP----------NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKsVRKNIQMVFQDpFASLNPRKTLRSIIKEPFNTHNMYTM------RERNEKVEELLARVGLhPSFAGRYPHEFS 162
Cdd:TIGR02315 71 GKKLRK-LRRRIGMIFQH-YNLIERLTVLENVLHGRLGYKPTWRSllgrfsEEDKERALSALERVGL-ADKAYQRADQLS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRV 231
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-231 |
5.47e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.68 E-value: 5.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVkkyfpirsglfQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:COG4619 1 LELEGL-----------SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRkniqMVFQDPFAslnPRKTLRSIIKEPFNTHNMYTMRERnekVEELLARVGLHPSFAGRYPHEFSGGQRQRI 169
Cdd:COG4619 70 PEWRRQVA----YVPQEPAL---WGGTVRDNLPFPFQLRERKFDRER---ALELLERLGLPPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRV 231
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRV 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
7-238 |
6.19e-49 |
|
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: 164.06 E-value: 6.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTagrtMIRL----YKPTEGQILFKGQ 82
Cdd:COG0411 2 DPLLEVRGLTKRF-----------GGLVAVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLitgfYRPTSGRILFDGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISNLSEEKLrksVRKNIQMVFQDP--FASL----N-----PRKTLRSIIKEPFNT-HNMYTMRERNEKVEELLARVGLH 150
Cdd:COG0411 67 DITGLPPHRI---ARLGIARTFQNPrlFPELtvleNvlvaaHARLGRGLLAALLRLpRARREEREARERAEELLERVGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 151 PsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDR 230
Cdd:COG0411 144 D-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
....*...
gi 2181075557 231 VGVMYLGK 238
Cdd:COG0411 223 IVVLDFGR 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-264 |
1.92e-48 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 163.17 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 4 ANQETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGRTMirlykPTEGQIL 78
Cdd:PRK11701 1 MMDQPLLSVRGLTKLY-----------GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTllnalSARLA-----PDAGEVH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 79 FKGQ-----DISNLSEEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPfnthnMYTMRERN-----EKVEELLARVG 148
Cdd:PRK11701 65 YRMRdgqlrDLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGER-----LMAVGARHygdirATAGDWLERVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 149 LHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHIS 228
Cdd:PRK11701 140 IDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLA 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 2181075557 229 DRVGVMYLGKMME--LTGKfeLYDNPLHPYTQALLSSV 264
Cdd:PRK11701 220 HRLLVMKQGRVVEsgLTDQ--VLDDPQHPYTQLLVSSV 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-240 |
5.64e-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: 161.07 E-value: 5.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03219 1 LEVRGLTKRF-----------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLrksVRKNIQMVFQDP--FASL----NPRKTLRSIIKEPFNTH-NMYTMRERNEKVEELLARVGLHPsFAGRYPHEFS 162
Cdd:cd03219 70 HEI---ARLGIGRTFQIPrlFPELtvleNVMVAAQARTGSGLLLArARREEREARERAEELLERVGLAD-LADRPAGELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQeEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-245 |
9.51e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.22 E-value: 9.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:COG2884 1 MIRFENVSKRYP----------GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKsVRKNIQMVFQDpFaSLNPRKT--------LRSIIKEPfnthnmytmRERNEKVEELLARVGLHpSFAGRYPHE 160
Cdd:COG2884 71 RREIPY-LRRRIGVVFQD-F-RLLPDRTvyenvalpLRVTGKSR---------KEIRRRVREVLDLVGLS-DKAKALPHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
....*
gi 2181075557 241 ELTGK 245
Cdd:COG2884 217 RDEAR 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-187 |
1.71e-47 |
|
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: 157.04 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDPFasLNPRK 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQ--LFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 116 TLRSIIKEPFNTHNMYTmRERNEKVEELLARVGL---HPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:pfam00005 75 TVRENLRLGLLLKGLSK-REKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-252 |
2.25e-47 |
|
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: 159.32 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03300 1 IELENVSKFY-----------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKlrksvrKNIQMVFQDpFAsLNPRKTLRSIIKEPFnthnmyTMR-----ERNEKVEELLARVGLHpSFAGRYPHEFSGG 164
Cdd:cd03300 70 HK------RPVNTVFQN-YA-LFPHLTVFENIAFGL------RLKklpkaEIKERVAEALDLVQLE-GYANRKPSQLSGG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 165 QRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTG 244
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
....*...
gi 2181075557 245 KFELYDNP 252
Cdd:cd03300 215 PEEIYEEP 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-293 |
2.28e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 162.93 E-value: 2.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:COG3839 4 LELENVSKSY-----------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKlRksvrkNIQMVFQDpFAsLNPRKTLRsiikepfntHNM-YTMR-------ERNEKVEELLARVGLHPsFAGRYPHEF 161
Cdd:COG3839 73 KD-R-----NIAMVFQS-YA-LYPHMTVY---------ENIaFPLKlrkvpkaEIDRRVREAAELLGLED-LLDRKPKQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHD----LSvvrhISDRVGVMYLG 237
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDG 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 238 KMMELtGK-FELYDNPLHPYTQALLSSVPVTRKRGSVKRERIVLKG---ELPSPANPPKG 293
Cdd:COG3839 211 RIQQV-GTpEELYDRPANLFVAGFIGSPPMNLLPGTVEGGGVRLGGvrlPLPAALAAAAG 269
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-295 |
2.80e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 162.62 E-value: 2.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKGQDI 84
Cdd:COG1118 3 IEVRNISKRF-----------GSFTLLDDVSLEIASGELVALLGPSGSGKTTllriiAG-----LETPDSGRIVLNGRDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 -SNLseeklrkSVRK-NIQMVFQDP-------------FAsLNPRKTLRSIIKepfnthnmytmrernEKVEELLARVGL 149
Cdd:COG1118 67 fTNL-------PPRErRVGFVFQHYalfphmtvaeniaFG-LRVRPPSKAEIR---------------ARVEELLELVQL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 150 hPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISD 229
Cdd:COG1118 124 -EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELAD 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 230 RVGVMYLGKMMELTGKFELYDNPLHPYTQALLSSV---PVTRKRGSVKRERIVLKGELPSPANPPKGCV 295
Cdd:COG1118 203 RVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVnvlRGRVIGGQLEADGLTLPVAEPLPDGPAVAGV 271
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-238 |
6.31e-47 |
|
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: 156.00 E-value: 6.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKkyfpirsglFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSe 89
Cdd:cd03228 1 IEFKNVS---------FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklRKSVRKNIQMVFQDPFasLnprktlrsiikepFNThnmyTMRErNekveeLLarvglhpsfagryphefSGGQRQRI 169
Cdd:cd03228 71 ---LESLRKNIAYVPQDPF--L-------------FSG----TIRE-N-----IL-----------------SGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGK 238
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
31-240 |
1.18e-46 |
|
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: 158.28 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDPFAS 110
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS----RRELARRIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LN------------PRKTlrsiikePFNTHNmytmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:COG1120 88 FGltvrelvalgryPHLG-------LFGRPS----AEDREAVEEALERTGLEH-LADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
28-266 |
2.16e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 154.57 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrksvRKNIQMVFQDp 107
Cdd:TIGR00968 8 KRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR------DRKIGFVFQH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 fASLNPRKTLRSiikepfNTHNMYTMRERN-----EKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELI 182
Cdd:TIGR00968 81 -YALFKHLTVRD------NIAFGLEIRKHPkakikARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 183 IADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLS 262
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
....
gi 2181075557 263 SVPV 266
Cdd:TIGR00968 233 EVNV 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-256 |
1.15e-44 |
|
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: 152.49 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03296 3 IEVRNVSKRF-----------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKlrksvrKNIQMVFQDpfASLNPRKTLRSII------KEPFNTHNMYTMRERnekVEELLARVGLHpSFAGRYPHEFSG 163
Cdd:cd03296 72 QE------RNVGFVFQH--YALFRHMTVFDNVafglrvKPRSERPPEAEIRAK---VHELLKLVQLD-WLADRYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELT 243
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
250
....*....|...
gi 2181075557 244 GKFELYDNPLHPY 256
Cdd:cd03296 220 TPDEVYDHPASPF 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-239 |
1.61e-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: 152.32 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnlse 89
Cdd:COG4555 2 IEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQMVFQDPFasLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRI 169
Cdd:COG4555 66 RKEPREARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-239 |
1.86e-44 |
|
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: 149.86 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlse 89
Cdd:cd03230 1 IEVRNLSKRY-----------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eKLRKSVRKNIQMVFQDPfaSLNPRKTlrsiikepfnthnmytmrernekVEELLarvglhpsfagryphEFSGGQRQRI 169
Cdd:cd03230 66 -KEPEEVKRRIGYLPEEP--SLYENLT-----------------------VRENL---------------KLSGGMKQRL 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
31-241 |
5.26e-44 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 160.38 E-value: 5.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDPFas 110
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID----PASLRRQIGVVLQDVF-- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 lnprktlrsiikePFNThnmyTMRErN----------EKVEELLARVGLHpSFAGRYPH-----------EFSGGQRQRI 169
Cdd:COG2274 560 -------------LFSG----TIRE-NitlgdpdatdEEIIEAARLAGLH-DFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMME 241
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVE 689
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-238 |
1.03e-43 |
|
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: 147.39 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 27 QRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKsvrkNIQMVFQd 106
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR----RIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 107 pfaslnprktlrsiikepfnthnmytmrernekveellarvglhpsfagrypheFSGGQRQRIGIARALTLNPELIIADE 186
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 187 PVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-241 |
1.81e-43 |
|
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: 149.04 E-value: 1.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglfQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:TIGR02211 1 LLKCENLGKRY-------QEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKSVRKNIQMVFQdpFASLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPSfAGRYPHEFSGGQRQR 168
Cdd:TIGR02211 74 SNERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-SVKEAKERAYEMLEKVGLEHR-INHRPSELSGGERQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 169 IGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHIsDRVGVMYLGKMME 241
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
29-239 |
5.22e-43 |
|
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: 146.43 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 29 KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQdpf 108
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 aslnprktlrsiikepfnthnmytmrernekveeLLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:cd03214 81 ----------------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 189 SALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-242 |
5.33e-43 |
|
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: 147.40 E-value: 5.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03301 1 VELENVTKRF-----------GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKlrksvrKNIQMVFQDpFAsLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRI 169
Cdd:cd03301 70 KD------RDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMEL 242
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-252 |
1.46e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 150.25 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIS 85
Cdd:PRK11432 3 QKNFVVLKNITKRF-----------GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 86 NLSEEKlrksvrKNIQMVFQD----PFASL--NPRKTLR--SIIKEpfnthnmytmrERNEKVEELLARVGLhPSFAGRY 157
Cdd:PRK11432 72 HRSIQQ------RDICMVFQSyalfPHMSLgeNVGYGLKmlGVPKE-----------ERKQRVKEALELVDL-AGFEDRY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 158 PHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLG 237
Cdd:PRK11432 134 VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
250
....*....|....*
gi 2181075557 238 KMMELTGKFELYDNP 252
Cdd:PRK11432 214 KIMQIGSPQELYRQP 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-252 |
1.58e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 147.10 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKaVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKlrksvrKNIQMVFQDp 107
Cdd:cd03299 8 KDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK------RDISYVPQN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 fASLNPRKTLRSIIKepfnthnmYTMRERNEKVEELLARVGLHPSFAG------RYPHEFSGGQRQRIGIARALTLNPEL 181
Cdd:cd03299 80 -YALFPHMTVYKNIA--------YGLKKRKVDKKEIERKVLEIAEMLGidhllnRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 182 IIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNP 252
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
31-264 |
1.89e-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: 147.28 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQD-----ISNLSEEKLRKSVRKNIQMVFQ 105
Cdd:TIGR02323 14 GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 dpfaslNPRKTLR-------SIIKEPFNTHNMYTMRERnEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:TIGR02323 94 ------NPRDGLRmrvsagaNIGERLMAIGARHYGNIR-ATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQ 258
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQ 246
|
....*.
gi 2181075557 259 ALLSSV 264
Cdd:TIGR02323 247 LLVSSI 252
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-239 |
5.91e-42 |
|
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: 142.95 E-value: 5.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSe 89
Cdd:cd03216 1 LELRGITKRF-----------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 ekLRKSVRKNIQMVFQdpfaslnprktlrsiikepfnthnmytmrernekveellarvglhpsfagrypheFSGGQRQRI 169
Cdd:cd03216 69 --PRDARRAGIAMVYQ-------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
34-238 |
6.76e-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: 146.44 E-value: 6.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTagrtMIR----LYKPTEGQILFKGQDISNLSEEKLrKSVRKNIQMVFQDP-- 107
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKST----LIQhlngLLKPTSGTVTIDGRDITAKKKKKL-KDLRKKVGLVFQFPeh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 --FAslnprktlRSIIKE-PFNTHNM-YTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:TIGR04521 94 qlFE--------ETVYKDiAFGPKNLgLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGK 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-268 |
9.75e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.41 E-value: 9.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 29 KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDpF 108
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS-F 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 AsLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:PRK10070 116 A-LMPHMTVLDNTAFGMELAGI-NAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 189 SALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLSSVPVTR 268
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQ 272
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-262 |
9.83e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 145.56 E-value: 9.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAA--NQETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK--P---T 73
Cdd:COG1117 1 MTAPasTLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 74 EGQILFKGQDIS----NLSEeklrksVRKNIQMVFQDPfaslNP-RKTlrsiIKE----PFNTHNMYTMRERNEKVEELL 144
Cdd:COG1117 70 EGEILLDGEDIYdpdvDVVE------LRRRVGMVFQKP----NPfPKS----IYDnvayGLRLHGIKSKSELDEIVEESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 145 ARVG--------LHPSfagryPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFnlTYLF 216
Cdd:COG1117 136 RKAAlwdevkdrLKKS-----ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVI 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2181075557 217 ISHDLSVVRHISDRVGVMYLGKMMEL--TGK-FElydNPLHPYTQALLS 262
Cdd:COG1117 209 VTHNMQQAARVSDYTAFFYLGELVEFgpTEQiFT---NPKDKRTEDYIT 254
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-234 |
1.42e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 152.24 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDPFas 110
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT----LESLRRQIGVVPQDTF-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LnprktlrsiikepFNThnmyTMRErN----------EKVEELLARVGLHPsFAGRYPH-----------EFSGGQRQRI 169
Cdd:COG1132 425 L-------------FSG----TIRE-NirygrpdatdEEVEEAAKAAQAHE-FIEALPDgydtvvgergvNLSGGQRQRI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVM 234
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVL 547
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
40-234 |
5.29e-41 |
|
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: 142.43 E-value: 5.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSLK-----KGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdISNLSEEKLRKSVRK-NIQMVFQDpfASLNP 113
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKINLPPQQrKIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKEPFNTHNMYTMRERnekVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRIS---VDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2181075557 194 SIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
28-239 |
1.65e-40 |
|
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: 141.35 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrksVRKNIQMVFQDP 107
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-----VRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 faSLNPRKTLRsiikepfntHNMYTM--------RERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNP 179
Cdd:cd03265 83 --SVDDELTGW---------ENLYIHarlygvpgAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-262 |
5.13e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.26 E-value: 5.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIS---------NLSEEKLRKSV 96
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 97 RKNIQMVFQDpFASLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALT 176
Cdd:PRK10619 91 RTRLTMVFQH-FNLWSHMTVLENVMEAPIQVLGL-SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 177 LNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPY 256
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
....*.
gi 2181075557 257 TQALLS 262
Cdd:PRK10619 248 LQQFLK 253
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-243 |
6.14e-40 |
|
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: 140.26 E-value: 6.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAANQeTILELRDVKKYFPIRSGlfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEG 75
Cdd:COG4181 1 MSSSSA-PIIELRGLTKTVGTGAG-------ELTILKGISLEVEAGESVAIVGASGSGKSTllgllAG-----LDRPTSG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 76 QILFKGQDISNLSEE---KLRksvRKNIQMVFQDpFaSLNPRKT----------LRSiikepfnthnmytMRERNEKVEE 142
Cdd:COG4181 68 TVRLAGQDLFALDEDaraRLR---ARHVGFVFQS-F-QLLPTLTalenvmlpleLAG-------------RRDARARARA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 143 LLARVGLhpsfAGR---YPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISH 219
Cdd:COG4181 130 LLERVGL----GHRldhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTH 205
|
250 260
....*....|....*....|....
gi 2181075557 220 DLSVVRHiSDRVGVMYLGKMMELT 243
Cdd:COG4181 206 DPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-241 |
7.59e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 141.31 E-value: 7.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKkyfpirsglFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDi 84
Cdd:PRK13635 1 MKEEIIRVEHIS---------FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 snLSEEKLRKsVRKNIQMVFQDP---FASlnprKTLRSIIKepFNTHNMYTMRERN-EKVEELLARVGLHpSFAGRYPHE 160
Cdd:PRK13635 71 --LSEETVWD-VRRQVGMVFQNPdnqFVG----ATVQDDVA--FGLENIGVPREEMvERVDQALRQVGME-DFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRVGVMYLGKMM 240
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
.
gi 2181075557 241 E 241
Cdd:PRK13635 220 E 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-252 |
8.91e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.55 E-value: 8.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAANQETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFK 80
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSF-----------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDISNLSEEKlrksvrKNIQMVFQDpFAsLNPRKTLRSII-------KEPFnthnmytmRERNEKVEELLARVGLHpSF 153
Cdd:PRK09452 75 GQDITHVPAEN------RHVNTVFQS-YA-LFPHMTVFENVafglrmqKTPA--------AEITPRVMEALRMVQLE-EF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 154 AGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGV 233
Cdd:PRK09452 138 AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVV 217
|
250
....*....|....*....
gi 2181075557 234 MYLGKMMELTGKFELYDNP 252
Cdd:PRK09452 218 MRDGRIEQDGTPREIYEEP 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
31-231 |
1.03e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnlseEKLRKSV-----RKNIQMVFq 105
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIgyvpqRAEVDWDF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 dPF-------ASLNPRKTLRSIIKepfnthnmytmRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:COG1121 91 -PItvrdvvlMGRYGRRGLFRRPS-----------RADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRV 231
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRV 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
32-263 |
2.92e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 139.06 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP----TEGQILFKGQDISnlsEEKLRKsvrKNIQMVFQDP 107
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA---PCALRG---RKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 FASLNPRKTLRSiikepfntHNMYTMRER-----NEKVEELLARVGLH--PSFAGRYPHEFSGGQRQRIGIARALTLNPE 180
Cdd:PRK10418 89 RSAFNPLHTMHT--------HARETCLALgkpadDATLTAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 181 LIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQAL 260
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
...
gi 2181075557 261 LSS 263
Cdd:PRK10418 241 VSA 243
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-247 |
4.52e-39 |
|
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: 144.90 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrkSVRKNIQMVFQDP--F 108
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA----SWRRQIAWVPQNPylF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASlnprkTLRSIIKepfnthnMYTMRERNEKVEELLARVGLHpSFAGRYPH-------E----FSGGQRQRIGIARALTL 177
Cdd:COG4988 424 AG-----TIRENLR-------LGRPDASDEELEAALEAAGLD-EFVAALPDgldtplgEggrgLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 178 NPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMElTGKFE 247
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVE-QGTHE 556
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-241 |
7.66e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 137.45 E-value: 7.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ--DISNLSEEKLRKSVRKNIQMVFQDpf 108
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRELRRNVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKT-LRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:PRK11124 91 YNLWPHLTvQQNLIEAPCRVLGL-SKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 188 VSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-247 |
9.22e-39 |
|
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: 136.97 E-value: 9.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDPFas 110
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS----RKSLRSMIGVVLQDTF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRkTLRSIIKepfnthnMYTMRERNEKVEELLARVGLHPsFAGRYP-----------HEFSGGQRQRIGIARALTLNP 179
Cdd:cd03254 88 LFSG-TIMENIR-------LGRPNATDEEVIEAAKEAGAHD-FIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMElTGKFE 247
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIE-EGTHD 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-264 |
1.62e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 136.76 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsNLS 88
Cdd:PRK09493 1 MIEFKNVSKHF-----------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKsVRKNIQMVFQDpFaSLNPRKT-LRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQ 167
Cdd:PRK09493 69 KVDERL-IRQEAGMVFQQ-F-YLFPHLTaLENVMFGPLRVRGA-SKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFE 247
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
250
....*....|....*..
gi 2181075557 248 LYDNPLHPYTQALLSSV 264
Cdd:PRK09493 223 LIKNPPSQRLQEFLQHV 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-234 |
2.10e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.08 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPirsglfqrkvGdVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKG 81
Cdd:COG1129 2 EPLLEMRGISKSFG----------G-VKALDGVSLELRPGEVHALLGENGAGKSTlmkilSG-----VYQPDSGEILLDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSeekLRKSVRKNIQMVFQDP------------FASLNPRKtlRSIIKEpfnthnmytmRERNEKVEELLARVGL 149
Cdd:COG1129 66 EPVRFRS---PRDAQAAGIAIIHQELnlvpnlsvaeniFLGREPRR--GGLIDW----------RAMRRRARELLARLGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 150 HPSfagryPH----EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVR 225
Cdd:COG1129 131 DID-----PDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVF 204
|
....*....
gi 2181075557 226 HISDRVGVM 234
Cdd:COG1129 205 EIADRVTVL 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-241 |
2.19e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 137.19 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 4 ANQETILELRDVKkyfpirsglFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQD 83
Cdd:PRK13648 2 EDKNSIIVFKNVS---------FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 IS--NLSEeklrksVRKNIQMVFQDPfaslnPRKTLRSIIKE--PFNTHN-MYTMRERNEKVEELLARVGLHpSFAGRYP 158
Cdd:PRK13648 73 ITddNFEK------LRKHIGIVFQNP-----DNQFVGSIVKYdvAFGLENhAVPYDEMHRRVSEALKQVDML-ERADYEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 159 HEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRVGVMYLGK 238
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGT 219
|
...
gi 2181075557 239 MME 241
Cdd:PRK13648 220 VYK 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
35-248 |
3.53e-38 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 142.79 E-value: 3.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDP--FAsln 112
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT----RASLRRNIAVVFQDAglFN--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 prktlRSI-----IKEPFNTH-NMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADE 186
Cdd:PRK13657 423 -----RSIednirVGRPDATDeEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 187 PVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMElTGKF-EL 248
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVE-SGSFdEL 556
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
31-252 |
1.80e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.98 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ--DISNLSEEKLRKSVRKNIQMVFQDpf 108
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQKVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKT-LRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:COG4161 91 YNLWPHLTvMENLIEAPCKVLGL-SKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 188 VSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMElTGKFELYDNP 252
Cdd:COG4161 169 TAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHFTQP 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-266 |
2.77e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 136.89 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirSGLFqrkvgdvkAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:PRK11607 19 LLEIRNLTKSF---DGQH--------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 eeklrkSVRKNIQMVFQDpfASLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQR 168
Cdd:PRK11607 88 ------PYQRPINMMFQS--YALFPHMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 169 IGIARALTLNPELIIADEPVSALDVSI----QAQVINLMEELqeefNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTG 244
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250 260
....*....|....*....|..
gi 2181075557 245 KFELYDNPLHPYTQALLSSVPV 266
Cdd:PRK11607 234 PEEIYEHPTTRYSAEFIGSVNV 255
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-263 |
2.83e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 133.77 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAANQETiLELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFK 80
Cdd:COG4598 1 MTDTAPPA-LEVRDLHKSF-----------GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDIsnlseeKLRKS---------------VRKNIQMVFQdpfaSLN--PRKT-LRSIIKEPFNTHNMyTMRERNEKVEE 142
Cdd:COG4598 69 GEEI------RLKPDrdgelvpadrrqlqrIRTRLGMVFQ----SFNlwSHMTvLENVIEAPVHVLGR-PKAEAIERAEA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 143 LLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNlTYLFISHDLS 222
Cdd:COG4598 138 LLAKVGLA-DKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMG 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2181075557 223 VVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLSS 263
Cdd:COG4598 216 FARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
51-291 |
2.85e-37 |
|
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: 135.70 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 51 IVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrksvRKNIQMVFQDpfASLNPRKTLRSIIKEPFNthnm 130
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQS--YALFPHMTVEENVAFGLK---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 131 ytMR-----ERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEE 205
Cdd:TIGR01187 69 --MRkvpraEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 206 LQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLSSVPVTRK-----------RGSVK 274
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAtvierkseqvvLAGVE 225
|
250
....*....|....*..
gi 2181075557 275 RERIVLKGELPSPANPP 291
Cdd:TIGR01187 226 GRRCDIYTDVPVEKDQP 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-249 |
5.29e-37 |
|
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: 132.66 E-value: 5.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 11 ELRDVKKYFPIRSglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEE 90
Cdd:cd03249 2 EFKNVSFRYPSRP--------DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 91 KLRKsvrkNIQMVFQDP--FASlnprkTLRSIIKepfnthnmYTMRERNEKVEELLARVGLHPSFAGRYPHEF------- 161
Cdd:cd03249 74 WLRS----QIGLVSQEPvlFDG-----TIAENIR--------YGKPDATDEEVEEAAKKANIHDFIMSLPDGYdtlvger 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 ----SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLG 237
Cdd:cd03249 137 gsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNG 213
|
250
....*....|...
gi 2181075557 238 KMMElTGKF-ELY 249
Cdd:cd03249 214 QVVE-QGTHdELM 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-231 |
9.31e-37 |
|
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: 131.79 E-value: 9.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPI--RSGLfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ-- 82
Cdd:COG4778 2 TTLLEVENLSKTFTLhlQGGK------RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDgg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 --DISNLSE-EKLRksVRKN-IQMVFQdpFASLNPRKTLRSIIKEPfnthnmytMRERN-------EKVEELLARVGLHP 151
Cdd:COG4778 76 wvDLAQASPrEILA--LRRRtIGYVSQ--FLRVIPRVSALDVVAEP--------LLERGvdreearARARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 152 SFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRV 231
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-239 |
1.90e-36 |
|
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: 130.61 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03292 1 IEFINVTKTYP----------NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKsVRKNIQMVFQDpFASLNPRK-------TLRSIIKEPfnthnmytmRERNEKVEELLARVGL-HPSFAgrYPHEF 161
Cdd:cd03292 71 RAIPY-LRRKIGVVFQD-FRLLPDRNvyenvafALEVTGVPP---------REIRKRVPAALELVGLsHKHRA--LPAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMeelqEEFNL---TYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03292 138 SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL----KKINKagtTVVVATHAKELVDTTRHRVIALERGK 213
|
.
gi 2181075557 239 M 239
Cdd:cd03292 214 L 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-248 |
2.96e-36 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 130.43 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrkSVRKNIQMVFQDpfaslnp 113
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD----SLRRAIGVVPQD------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 rKTLrsiikepFNTHNMYTMR-----ERNEKVEELLARVGLHPSFAgRYPHEF-----------SGGQRQRIGIARALTL 177
Cdd:cd03253 84 -TVL-------FNDTIGYNIRygrpdATDEEVIEAAKAAQIHDKIM-RFPDGYdtivgerglklSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 178 NPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMELTGKFEL 248
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
31-238 |
3.69e-36 |
|
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: 129.58 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnlseEKLRKSV-----RKNIQMVFq 105
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIgyvpqRRSIDRDF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 dP-----FAS--LNPRKTLRSIIKepfnthnmytmRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:cd03235 84 -PisvrdVVLmgLYGHKGLFRRLS-----------KADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRvgVMYLGK 238
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDR--VLLLNR 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
35-234 |
6.73e-36 |
|
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: 136.43 E-value: 6.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrkSVRKNIQMVFQDPFAslnpr 114
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED----DLRRRIAVVPQRPHL----- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 ktlrsiikepFNThnmyTMRErN----------EKVEELLARVGLHPsFAGRYPH-------E----FSGGQRQRIGIAR 173
Cdd:COG4987 421 ----------FDT----TLRE-NlrlarpdatdEELWAALERVGLGD-WLAALPDgldtwlgEggrrLSGGERRRLALAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 174 ALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHIsDRVGVM 234
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVL 542
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
40-231 |
8.44e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.10 E-value: 8.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKGQDISNLSEEKlrksvRKnIQMVFQDP--FASL- 111
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTllnliAG-----FLPPDSGRILWNGQDLTALPPAE-----RP-VSMLFQENnlFPHLt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 ---------NPRktLRsiikepfnthnmYTMRERnEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELI 182
Cdd:COG3840 88 vaqniglglRPG--LK------------LTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2181075557 183 IADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRV 231
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRV 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-241 |
2.09e-35 |
|
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: 127.72 E-value: 2.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03268 1 LKTNDLTKTY-----------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklrksVRKNIQMVFQDPfaSLNPRKTLRsiikepfntHNMYT----MRERNEKVEELLARVGLHPSfAGRYPHEFSGGQ 165
Cdd:cd03268 70 ------ALRRIGALIEAP--GFYPNLTAR---------ENLRLlarlLGIRKKRIDEVLDVVGLKDS-AKKKVKGFSLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 166 RQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-239 |
2.34e-35 |
|
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: 131.39 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVkAVDgVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQI------LFKGQDISNLSEEKLRksvrkn 99
Cdd:TIGR02142 5 FSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtLFDSRKGIFLPPEKRR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 100 IQMVFQDpfASLNPRKTLRSiikepfnthNM-YTMR-----ERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIAR 173
Cdd:TIGR02142 77 IGYVFQE--ARLFPHLSVRG---------NLrYGMKrarpsERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 174 ALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:TIGR02142 145 ALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
38-262 |
2.44e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 128.71 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfKGQDIS-----NLSEEK-LRKSVRKNIQMVFQDpFASL 111
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITidtarSLSQQKgLIRQLRQHVGFVFQN-FNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 NPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhpsfAGR---YPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:PRK11264 98 PHRTVLENIIEGPVIVKGE-PKEEATARARELLAKVGL----AGKetsYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 189 SALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLS 262
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-241 |
4.91e-35 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 127.35 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklRKSVRKNIQMVFQDPFAsl 111
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT----LASLRRQIGLVSQDVFL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 nprktlrsiikepFNThnmyTMRER---------NEKVEELLARVGLHpSFAGRYPHEF-----------SGGQRQRIGI 171
Cdd:cd03251 88 -------------FND----TVAENiaygrpgatREEVEEAARAANAH-EFIMELPEGYdtvigergvklSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 172 ARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMME 241
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-239 |
5.64e-35 |
|
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: 126.94 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSe 89
Cdd:cd03245 3 IEFRNVSFSYPNQ---------EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklRKSVRKNIQMVFQDP--FASlnprkTLRSIIkepfnthnmyTMRERNEKVEELLA---RVGLHPsFAGRYPHEF--- 161
Cdd:cd03245 73 ---PADLRRNIGYVPQDVtlFYG-----TLRDNI----------TLGAPLADDERILRaaeLAGVTD-FVNKHPNGLdlq 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 --------SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVI-NLMEELQEEfnlTYLFISHDLSVVRhISDRVG 232
Cdd:cd03245 134 igergrglSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKeRLRQLLGDK---TLIIITHRPSLLD-LVDRII 209
|
....*..
gi 2181075557 233 VMYLGKM 239
Cdd:cd03245 210 VMDSGRI 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-245 |
6.89e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 128.28 E-value: 6.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNlsEEKLRKsVRKNIQMVFQDPfaslnPR 114
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD--EENLWD-IRNKAGMVFQNP-----DN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 KTLRSIIKE--PFNTHNM-YTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSAL 191
Cdd:PRK13633 97 QIVATIVEEdvAFGPENLgIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 192 DVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRVGVMYLGKM-MELTGK 245
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVvMEGTPK 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-240 |
7.54e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlS 88
Cdd:PRK13639 1 ILETRDLKYSYP----------DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--Y 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHnmYTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQR 168
Cdd:PRK13639 69 DKKSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLG--LSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 169 IGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
29-248 |
1.90e-34 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 125.95 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 29 KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTM--IRLYKPTEGQILFKGQDISNLS-EEKlrksVRKNIQMVFQ 105
Cdd:COG0396 9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSpDER----ARAGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DP--FASLNPRKTLRSIIKEpfNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHE-FSGGQRQRIGIARALTLNPELI 182
Cdd:COG0396 85 YPveIPGVSVSNFLRTALNA--RRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 183 IADEPVSALDV-SIQAqVINLMEELQEEfNLTYLFISHDLSVVRHIS-DRVGVMYLGKMMElTGKFEL 248
Cdd:COG0396 163 ILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIKpDFVHVLVDGRIVK-SGGKEL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
34-237 |
1.98e-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: 125.06 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlseeklRKSVRKNIQMVFQDP---FAS 110
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQDVdyqLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLRSIIKEPfnthnmytmRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSA 190
Cdd:cd03226 87 DSVREELLLGLKEL---------DAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2181075557 191 LDVSIQAQVINLMEELQEEFNlTYLFISHDLSVVRHISDRvgVMYLG 237
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDR--VLLLA 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-247 |
3.26e-34 |
|
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: 131.08 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKK-YFPIRSGLfqrkvgdVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFK-GQDI 84
Cdd:TIGR03269 277 EPIIKVRNVSKrYISVDRGV-------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEW 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEK--LRKSVRKNIQMVFQDpfASLNPRKTLRSIIKE------PFNTHNM---YTMRE---RNEKVEELLARvglh 150
Cdd:TIGR03269 350 VDMTKPGpdGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEaiglelPDELARMkavITLKMvgfDEEKAEEILDK---- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 151 psfagrYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDR 230
Cdd:TIGR03269 424 ------YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
250
....*....|....*..
gi 2181075557 231 VGVMYLGKMMElTGKFE 247
Cdd:TIGR03269 498 AALMRDGKIVK-IGDPE 513
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
36-252 |
6.65e-34 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 127.80 E-value: 6.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP--TEGQILFKGQDISNLSEEKlrksvrKNIQMVFQDpfASLNP 113
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHK------RGLALLFQN--YALFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:TIGR03258 93 HLKVEDNVAFGLRAQKM-PKADIAERVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 194 SIQAQVINLMEELQEEF-NLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNP 252
Cdd:TIGR03258 171 NIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-245 |
7.25e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.93 E-value: 7.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlsEEKLR-KSVRKNIQMVFQDPFASLN 112
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT---DKKVKlSDIRKKVGLVFQYPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 PRKTLRSIIKEPFNTHnmYTMRERNEKVEELLARVGL-HPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSAL 191
Cdd:PRK13637 98 EETIEKDIAFGPINLG--LSEEEIENRVKRAMNIVGLdYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 192 DVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKmMELTGK 245
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK-CELQGT 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-234 |
1.25e-33 |
|
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: 126.75 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKGQDisnLSEEKLRKSV---RKNIQMVFQDP--F 108
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTllraiAG-----LERPDSGRIRLGGEV---LQDSARGIFLpphRRRIGYVFQEArlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKTLRsiikepfnthnmYTMR-----ERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:COG4148 90 PHLSVRGNLL------------YGRKrapraERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLL 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
36-249 |
2.98e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.07 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDisnLSEEKLRKsVRKNIQMVFQdpfaslNPRK 115
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWD-IRHKIGMVFQ------NPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIKE---PFNTHN----MYTMRERnekVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:PRK13650 93 QFVGATVEddvAFGLENkgipHEEMKER---VNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 189 SALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRhISDRVGVMYLGKMMELTGKFELY 249
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
35-260 |
3.69e-33 |
|
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: 122.59 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQ--MVF----QDPF 108
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQenVLFnrsiRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGlhpsfAGrypheFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:cd03252 97 ALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQG-----AG-----LSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 189 SALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMELTGKFELYD-NPLHPYTQAL 260
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAeNGLYAYLYQL 236
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
9-231 |
6.58e-33 |
|
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: 121.34 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsgLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ----DI 84
Cdd:TIGR02324 1 LLEVEDLSKTFT----LHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEgawvDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKLRKSVRKNIQMVFQdpFASLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPSFAGRYPHEFSGG 164
Cdd:TIGR02324 77 AQASPREVLEVRRKTIGYVSQ--FLRVIPRVSALEVVAEPLLERGV-PREAARARARELLARLNIPERLWHLPPATFSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 165 QRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRV 231
Cdd:TIGR02324 154 EQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
238-327 |
7.32e-33 |
|
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: 117.08 E-value: 7.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 238 KMMELTGKFELYDNPLHPYTQALLSSVPVTRKRGsvkRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEA 317
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRD---RKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEI 77
|
90
....*....|
gi 2181075557 318 APSHFVACHL 327
Cdd:TIGR01727 78 AEGHRVACHL 87
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-242 |
1.83e-32 |
|
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: 120.65 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksvrkniqMVFQDpfASLNPRK 115
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQN--YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIKEPFNTHNMYTMR-ERNEKVEELLARVGLHPSfAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVS 194
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKsERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 195 IQAqviNLMEELQ---EEFNLTYLFISHDLSVVRHISDRVGVM------YLGKMMEL 242
Cdd:TIGR01184 149 TRG---NLQEELMqiwEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEV 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-249 |
2.32e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.81 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNP 113
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKEPFNtHNMyTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:PRK13646 101 DTVEREIIFGPKN-FKM-NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 194 SIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELY 249
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
35-239 |
4.83e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIS--NLSEeklrksVRKNIQMVFQDP---FA 109
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKE------IRKKIGIIFQNPdnqFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 110 SLnprkTLRSIIKepFNTHN-MYTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:PRK13632 98 GA----TVEDDIA--FGLENkKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 189 SALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRhISDRVGVMYLGKM 239
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
4.96e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 120.72 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIs 85
Cdd:PRK13636 2 EDYILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 86 NLSEEKLRKsVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHnmYTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQ 165
Cdd:PRK13636 71 DYSRKGLMK-LRESVGMVFQDPDNQLFSASVYQDVSFGAVNLK--LPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 166 RQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
39-244 |
5.19e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.54 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKlrKSVRKNIQMVFQDPFASLNPRKTLR 118
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA--KAELRNQKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 119 SIIKEPFNTHNMYTmRERNEKVEELLARVGLHPSFAGRyPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQ 198
Cdd:PRK11629 106 ENVAMPLLIGKKKP-AEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2181075557 199 VINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM--YLGKMMELTG 244
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRdgRLTAELSLMG 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-239 |
7.13e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.37 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILF 79
Cdd:COG3845 1 MMPPALELRGITKRF-----------GGVVANDDVSLTVRPGEIHALLGENGAGKSTlmkilYG-----LYQPDSGEILI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 80 KGQ--DISNlseekLRKSVRKNIQMVFQ-----DPF-------ASLNPRKTLRsiikepfnthnmYTMRERNEKVEELLA 145
Cdd:COG3845 65 DGKpvRIRS-----PRDAIALGIGMVHQhfmlvPNLtvaenivLGLEPTKGGR------------LDRKAARARIRELSE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 146 RVGLH--PSfagRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALdvSIQ--AQVINLMEELQEEfNLTYLFISHDL 221
Cdd:COG3845 128 RYGLDvdPD---AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKL 201
|
250
....*....|....*...
gi 2181075557 222 SVVRHISDRVGVMYLGKM 239
Cdd:COG3845 202 REVMAIADRVTVLRRGKV 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
31-205 |
7.33e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.97 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnlseEKLRKSVRKNIQMVFQDP--F 108
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDYRRRLAYLGHADglK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKTLRSIIKepfnthnMYTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:COG4133 88 PELTVRENLRFWAA-------LYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170
....*....|....*..
gi 2181075557 189 SALDVSIQAQVINLMEE 205
Cdd:COG4133 160 TALDAAGVALLAELIAA 176
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-238 |
7.66e-32 |
|
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: 118.69 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:cd03224 1 LEVENLNAGY-----------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLrksVRKNIQMVFQDP--FASLNPRKTLRsiikepfnthnMYTMRERNEKVEELLARV-GLHP---SFAGRYPHEFSG 163
Cdd:cd03224 70 HER---ARAGIGYVPEGRriFPELTVEENLL-----------LGAYARRRAKRKARLERVyELFPrlkERRKQLAGTLSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-249 |
2.94e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.66 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 29 KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdisNLSEEKLRkSVRKNIQMVFQDPf 108
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVW-NLRRKIGMVFQNP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 aslnPRKTLRSIIKE--PFNTHNMYTMRERN-EKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIAD 185
Cdd:PRK13642 91 ----DNQFVGATVEDdvAFGMENQGIPREEMiKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 186 EPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRVGVMYLGKMMELTGKFELY 249
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-258 |
7.07e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 7.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRT---MIRLYKP--TEGQILFKGQDI 84
Cdd:PRK14247 4 IEIRDLKVSF-----------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKLRKSVrkniQMVFQDPfaslNPRKTLrSIIKE----PFNTHNMYTMRERNEKVEELLARVGLHPSFAGRY--- 157
Cdd:PRK14247 73 FKMDVIELRRRV----QMVFQIP----NPIPNL-SIFENvalgLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdap 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 158 PHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfnLTYLFISHDLSVVRHISDRVGVMYLG 237
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKG 221
|
250 260
....*....|....*....|.
gi 2181075557 238 KMMELTGKFELYDNPLHPYTQ 258
Cdd:PRK14247 222 QIVEWGPTREVFTNPRHELTE 242
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
32-240 |
7.72e-31 |
|
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: 122.67 E-value: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKsvrkNIQMVFQDP--FA 109
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR----NIGYVPQDPrlFY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 110 SlnprkTLRSIIkepfnthnmyTMRERNEKVEELLA---RVGLHpSFAGRYPHEF-----------SGGQRQRIGIARAL 175
Cdd:TIGR03375 553 G-----TLRDNI----------ALGAPYADDEEILRaaeLAGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 176 TLNPELIIADEPVSALDVSIQAQVI-NLMEELQEEfnlTYLFISHDLSVVRhISDRVGVMYLGKMM 240
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKdRLKRWLAGK---TLVLVTHRTSLLD-LVDRIIVMDNGRIV 678
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-239 |
8.56e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.03 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:PRK10851 3 IEIANIKKSF-----------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKlrksvrKNIQMVFQ-----------DPFA---SLNPRKtlrsiiKEPfnthNMYTMRernEKVEELLARVGLhPSFAG 155
Cdd:PRK10851 72 RD------RKVGFVFQhyalfrhmtvfDNIAfglTVLPRR------ERP----NAAAIK---AKVTQLLEMVQL-AHLAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 156 RYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMY 235
Cdd:PRK10851 132 RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
....
gi 2181075557 236 LGKM 239
Cdd:PRK10851 212 QGNI 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
35-252 |
1.29e-30 |
|
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: 115.28 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSvrknIQMVFQDP--FASln 112
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR----ISIIPQDPvlFSG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 prkTLRSIIkEPFNTHNmytmrerNEKVEELLARVGL---HPSFAGRYPHE-------FSGGQRQRIGIARALTLNPELI 182
Cdd:cd03244 93 ---TIRSNL-DPFGEYS-------DEELWQALERVGLkefVESLPGGLDTVveeggenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 183 IADEPVSALDVSIQAQVinlMEELQEEF-NLTYLFISHDLSVVRHiSDRVGVMYLGKMMEltgkfelYDNP 252
Cdd:cd03244 162 VLDEATASVDPETDALI---QKTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVE-------FDSP 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-220 |
1.50e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.11 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsGLFQRKVgdvkAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKGQDI 84
Cdd:COG4525 4 LTVRHVSVRYP---GGGQPQP----ALQDVSLTIESGEFVVALGASGCGKTTllnliAG-----FLAPSSGEITLDGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKlrkSVrkniqmVFQD----PFasLNPRK------TLRSIIKepfnthnmytmRERNEKVEELLARVGLHpSFA 154
Cdd:COG4525 72 TGPGADR---GV------VFQKdallPW--LNVLDnvafglRLRGVPK-----------AERRARAEELLALVGLA-DFA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 155 GRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHD 220
Cdd:COG4525 129 RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-239 |
2.05e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 114.30 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKG-------- 81
Cdd:cd03269 1 LEVENVTKRF-----------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaar 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEK-LRKSVRKNIQMVFqdpFASLnprktlrsiikepfntHNMyTMRERNEKVEELLARVGLHPsFAGRYPHE 160
Cdd:cd03269 70 NRIGYLPEERgLYPKMKVIDQLVY---LAQL----------------KGL-KKEEARRRIDEWLERLELSE-YANKRVEE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-240 |
6.61e-30 |
|
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: 113.37 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTagrT--MIR-LYKPTEGQILFKGQDISn 86
Cdd:cd03263 1 LQIRNLTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTT---TlkMLTgELRPTSGTAYINGYSIR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 lseeKLRKSVRKNIQMVFQDP--FASLNPRKTLR--SIIKEPFNthnmytmRERNEKVEELLARVGLHPsFAGRYPHEFS 162
Cdd:cd03263 68 ----TDRKAARQSLGYCPQFDalFDELTVREHLRfyARLKGLPK-------SEIKEEVELLLRVLGLTD-KANKRARTLS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:cd03263 136 GGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-241 |
7.01e-30 |
|
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: 119.44 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:TIGR02203 331 VEFRNVTFRYPGR---------DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQ--MVFQDPFASlNPRKTLRSIIKEpfnthnmytmrernEKVEELLARVGLHpSFAGRYPHEF------ 161
Cdd:TIGR02203 402 ASLRRQVALVSQdvVLFNDTIAN-NIAYGRTEQADR--------------AEIERALAAAYAQ-DFVDKLPLGLdtpige 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 -----SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYL 236
Cdd:TIGR02203 466 ngvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDD 542
|
....*
gi 2181075557 237 GKMME 241
Cdd:TIGR02203 543 GRIVE 547
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
36-220 |
7.49e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.96 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKST-----AGrTMIRLYKpTEGQILFKGQDISNLSEEklrksvRKNIQMVFQDP--F 108
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTllaaiAG-TLSPAFS-ASGEVLLNGRRLTALPAE------QRRIGILFQDDllF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKTLrsiikePFNTHNMYTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:COG4136 89 PHLSVGENL------AFALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|..
gi 2181075557 189 SALDVSIQAQVINLMEELQEEFNLTYLFISHD 220
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-221 |
9.67e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.03 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGRtmirlYKPTEGQILFKGQD 83
Cdd:COG1101 1 MLELKNLSKTF------NPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTllnaiAGS-----LPPDSGSILIDGKD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 ISNLSEEKlrksvR-KNIQMVFQDPFASLNPRKTlrsiIKEpfnthNM--------------YTMRERNEKVEELLA--- 145
Cdd:COG1101 70 VTKLPEYK-----RaKYIGRVFQDPMMGTAPSMT----IEE-----NLalayrrgkrrglrrGLTKKRRELFRELLAtlg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 146 ---------RVGLhpsfagrypheFSGGQRQrigiarALTL------NPELIIADEPVSALDVSIQAQVINLMEELQEEF 210
Cdd:COG1101 136 lglenrldtKVGL-----------LSGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEN 198
|
250
....*....|.
gi 2181075557 211 NLTYLFISHDL 221
Cdd:COG1101 199 NLTTLMVTHNM 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-239 |
1.06e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.82 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN-- 86
Cdd:COG4152 1 MLELKGLTKRF-----------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPed 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 ------LSEEK-LRKSVRKNIQMVFqdpFASLnprktlrsiikepfntHNMyTMRERNEKVEELLARVGLhPSFAGRYPH 159
Cdd:COG4152 70 rrrigyLPEERgLYPKMKVGEQLVY---LARL----------------KGL-SKAEAKRRADEWLERLGL-GDRANKKVE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 160 EFSGGQRQRIGIARALTLNPELIIADEPVSALDvSIQAQVI-NLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGR 206
|
.
gi 2181075557 239 M 239
Cdd:COG4152 207 K 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-252 |
1.95e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.67 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKKYFPIRSglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDI 84
Cdd:TIGR00958 474 NLEGLIEFQDVSFSYPNRP--------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKLRKSVRkniqMVFQDP--FAslnprktlRSIikepfnTHNMYTMRERNEKVEELLARV--GLHpSFAGRYPHE 160
Cdd:TIGR00958 546 VQYDHHYLHRQVA----LVGQEPvlFS--------GSV------RENIAYGLTDTPDEEIMAAAKaaNAH-DFIMEFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 161 F-----------SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAqvinLMEELQEEFNLTYLFISHDLSVVRHiSD 229
Cdd:TIGR00958 607 YdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-AD 681
|
250 260
....*....|....*....|...
gi 2181075557 230 RVGVMYLGKMMELTGKFELYDNP 252
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-252 |
2.06e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.77 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNP 113
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKEPFNTHnmYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:PRK13641 101 NTVLKDVEFGPKNFG--FSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 194 SIQAQVINLMEELQEEFNlTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNP 252
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-238 |
3.20e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 112.39 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 23 SGLFQRkVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKL-RKSVRKNIQ 101
Cdd:PRK11300 9 SGLMMR-FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 102 MV--FQDPFASLN-----PRKTLRSIIKEPFNTHNmYTMRERN--EKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIA 172
Cdd:PRK11300 88 HVrlFREMTVIENllvaqHQQLKTGLFSGLLKTPA-FRRAESEalDRAATWLERVGLLE-HANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 173 RALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
37-247 |
4.09e-29 |
|
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: 117.75 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 37 DGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrkSVRKNIQMVFQDpfASLNPRKT 116
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQ----AVRRQLGVVLQN--GRLMSGSI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 117 LRSIIkepfnTHNMYTMRERNEKVEEL-LAR------VGLHP--SFAGRyphEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:TIGR03797 544 FENIA-----GGAPLTLDEAWEAARMAgLAEdirampMGMHTviSEGGG---TLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 188 VSALDVSIQAQVINLMEELqeefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMElTGKFE 247
Cdd:TIGR03797 616 TSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQ-QGTYD 669
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-258 |
4.59e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.45 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 30 VGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK------PTEGQILFKGQDISNLSEEKLRKSVrkniQMV 103
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEV----GMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 104 FQDPfaSLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRY---PHEFSGGQRQRIGIARALTLNPE 180
Cdd:PRK14246 96 FQQP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 181 LIIADEPVSALDVSIQAQVINLMEELQEEfnLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQ 258
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-264 |
4.89e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.86 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK-----PTEGQILFKGQDISNLSEEKLRksVRKNIQMVFQ 105
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIE--VRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 --DPFaslnPRKTLRSIIKEPFNTHNMYTMR-ERNEKVEELLARVGLHPSFAGR---YPHEFSGGQRQRIGIARALTLNP 179
Cdd:PRK14267 93 ypNPF----PHLTIYDNVAIGVKLNGLVKSKkELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEFnlTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQA 259
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEK 246
|
....*
gi 2181075557 260 LLSSV 264
Cdd:PRK14267 247 YVTGA 251
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-238 |
5.05e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKvgdvkAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQ 105
Cdd:PRK13634 18 FERR-----ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DPFASLNPRKTLRSIIKEPFNthnmYTMRERN--EKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:PRK13634 93 FPEHQLFEETVEKDICFGPMN----FGVSEEDakQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-238 |
6.84e-29 |
|
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: 110.54 E-value: 6.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrksVRKNIQMVFq 105
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-----ARRRLGFVS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DPFAsLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIAD 185
Cdd:cd03266 85 DSTG-LYDRLTARENLEYFAGLYGL-KGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 186 EPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
32-249 |
6.87e-29 |
|
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: 116.72 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSvrknIQMVFQDPfasl 111
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR----MALVPQDP---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 nprkTLrsiikepFNTHNMYTMRERN-----EKVEELlARVGLHPSFAGRYPHEF-----------SGGQRQRIGIARAL 175
Cdd:TIGR02204 424 ----VL-------FAASVMENIRYGRpdatdEEVEAA-ARAAHAHEFISALPEGYdtylgergvtlSGGQRQRIAIARAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 176 TLNPELIIADEPVSALDVSIQAQVINLMEELQEEfnLTYLFISHDLSVVRHiSDRVGVMYLGKMM------ELTGKFELY 249
Cdd:TIGR02204 492 LKDAPILLLDEATSALDAESEQLVQQALETLMKG--RTTLIIAHRLATVLK-ADRIVVMDQGRIVaqgthaELIAKGGLY 568
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-266 |
7.32e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.41 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTagrtMIRLykpTEGQILFK-GQDI-------SNLSEEKLRKSVRKNIQMV 103
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKST----MIQL---TNGLIISEtGQTIvgdyaipANLKKIKEVKRLRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 104 FQDPFASLNPRKTLRSIIKEPFNTHNmyTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:PRK13645 96 FQFPEYQLFQETIEKDIAFGPVNLGE--NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNplhpytQALLSS 263
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTK 247
|
...
gi 2181075557 264 VPV 266
Cdd:PRK13645 248 IEI 250
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
36-248 |
1.65e-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: 116.00 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKsvrkNIQMVFQDPFasLNPRK 115
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR----QMGVVLQENV--LFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSI-IKEPfnthNMytmreRNEKVEELLARVGLHpSFAGRYPHEF-----------SGGQRQRIGIARALTLNPELII 183
Cdd:TIGR01846 547 IRDNIaLCNP----GA-----PFEHVIHAAKLAGAH-DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILI 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMMELTGKFEL 248
Cdd:TIGR01846 617 FDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-262 |
2.74e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRL--YKP---TEGQILFKG 81
Cdd:PRK14239 3 EPILQVSDLSVYY-----------NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEKLRksVRKNIQMVFQDPfaslNPRktlrsiikePFNTHN--MYTMRERNEKVEELLARV------------ 147
Cdd:PRK14239 72 HNIYSPRTDTVD--LRKEIGMVFQQP----NPF---------PMSIYEnvVYGLRLKGIKDKQVLDEAvekslkgasiwd 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 148 ----GLHPSFAGrypheFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFnlTYLFISHDLSV 223
Cdd:PRK14239 137 evkdRLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQ 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 2181075557 224 VRHISDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLS 262
Cdd:PRK14239 210 ASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
36-239 |
4.76e-28 |
|
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: 106.92 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksvRKNIQMVFQDP--FASlnp 113
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDHVGYLPQDDelFSG--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 rkTLRSIIkepfnthnmytmrernekveellarvglhpsfagrypheFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:cd03246 91 --SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2181075557 194 SIQAQVINLMEELQEEfNLTYLFISHDLSVVRhISDRVGVMYLGKM 239
Cdd:cd03246 130 EGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-239 |
5.88e-28 |
|
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: 108.33 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:cd03248 9 KGIVKFQNVTFAYPTRP--------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEEKLRKSVrkniQMVFQDP--FAslnprKTLRSIIKEPFNTHNMytmrernEKVEELLARVGLHpSFAGRYPHEF--- 161
Cdd:cd03248 81 YEHKYLHSKV----SLVGQEPvlFA-----RSLQDNIAYGLQSCSF-------ECVKEAAQKAHAH-SFISELASGYdte 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 --------SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGV 233
Cdd:cd03248 144 vgekgsqlSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILV 220
|
....*.
gi 2181075557 234 MYLGKM 239
Cdd:cd03248 221 LDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-250 |
8.11e-28 |
|
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: 107.23 E-value: 8.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 29 KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRL--YKPTEGQILFKGQDISNLS-EEKlrksVRKNIQMVFQ 105
Cdd:cd03217 9 SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpEER----ARLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DP--FASLNPRKTLRSIikepfnthnmytmrerNEKveellarvglhpsfagrypheFSGGQRQRIGIARALTLNPELII 183
Cdd:cd03217 85 YPpeIPGVKNADFLRYV----------------NEG---------------------FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHI-SDRVGVMYLGKMMElTGKFELYD 250
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK-SGDKELAL 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-239 |
1.60e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 107.27 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 30 VGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrKSVRKNIQMVFQDPFA 109
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREV-PFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 110 SLNprKTLRSIIKEPFNTHNMYTMRERnEKVEELLARVGLHPSfAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:PRK10908 91 LMD--RTVYDNVAIPLIIAGASGDDIR-RRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2181075557 190 ALDVSIQAQVINLMEELQeEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:PRK10908 167 NLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-238 |
2.60e-27 |
|
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: 106.12 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGeTLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlseeKLRKSVRKNIQMVFQDP------ 107
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-----KQPQKLRRRIGYLPQEFgvypnf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 --FASLNPRKTLRSIIKepfnthnmytmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIAD 185
Cdd:cd03264 88 tvREFLDYIAWLKGIPS-----------KEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 186 EPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
31-240 |
3.92e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVrkniqmvfqdpfaS 110
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL-------------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRK-------TLRSII---KEPFNTHNMYTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPE 180
Cdd:PRK11231 80 LLPQHhltpegiTVRELVaygRSPWLSLWGRLSAEDNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 181 LIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
34-234 |
4.12e-27 |
|
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: 111.22 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEeklrKSVRKNIQMVFQDPFAslnP 113
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA----DSWRDQIAWVPQHPFL---F 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKepfnthnMYTMRERNEKVEELLARVGLHPSFA----------GRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:TIGR02857 409 AGTIAENIR-------LARPDASDAEIREALERAGLDEFVAalpqgldtpiGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVrHISDRVGVM 234
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-241 |
5.83e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKkyfpirsglFQrkVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDI 84
Cdd:PRK10247 3 ENSPLLQLQNVG---------YL--AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKLRKSVRKNIQ--MVFQDpfaslnprkTLRSIIKEPFNThnmytmreRNEKVEEL-----LARVGLHPSFAGRY 157
Cdd:PRK10247 72 STLKPEIYRQQVSYCAQtpTLFGD---------TVYDNLIFPWQI--------RNQQPDPAiflddLERFALPDTILTKN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 158 PHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM-YL 236
Cdd:PRK10247 135 IAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQpHA 214
|
....*
gi 2181075557 237 GKMME 241
Cdd:PRK10247 215 GEMQE 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-239 |
1.07e-26 |
|
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: 104.50 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 45 KGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLseeklrKSVRKNIQMVFQDP--FASL----------N 112
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPADRPVSMLFQENnlFAHLtveqnvglglS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 PRKTLRSiikepfnthnmytmrERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALD 192
Cdd:cd03298 97 PGLKLTA---------------EDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2181075557 193 VSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-245 |
1.29e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNP 113
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIikePFNTHNMYTMRERNEKV-EELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALD 192
Cdd:PRK13649 101 ETVLKDV---AFGPQNFGVSQEEAEALaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 193 VSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMeLTGK 245
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLV-LSGK 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-291 |
1.35e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.53 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILfKGQdi 84
Cdd:PRK11247 8 NQGTPLLLNAVSKRY-----------GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEeklrksVRKNIQMVFQDpfASLNPRKT--------LRSIIKepfnthnmytmrernEKVEELLARVGLHPSfAGR 156
Cdd:PRK11247 74 APLAE------AREDTRLMFQD--ARLLPWKKvidnvglgLKGQWR---------------DAALQALAAVGLADR-ANE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 157 YPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYL 236
Cdd:PRK11247 130 WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 237 GKM-MELTgkfelydnplhpytqallSSVPVTRKRGSVK---RERIVLKGELPSPANPP 291
Cdd:PRK11247 210 GKIgLDLT------------------VDLPRPRRRGSARlaeLEAEVLQRVMSRGESEP 250
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-234 |
1.46e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 109.91 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 37 DGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrkSVRKNIQMVFQDPfaSLnprkt 116
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA----SLRAAIGIVPQDT--VL----- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 117 lrsiikepFNThnmyTMRErN----------EKVEELLARVGLHPsFAGRYPHEF-----------SGGQRQRIGIARAL 175
Cdd:COG5265 444 --------FND----TIAY-NiaygrpdaseEEVEAAARAAQIHD-FIESLPDGYdtrvgerglklSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 176 TLNPELIIADEPVSALDV----SIQAQvinlMEELQEefNLTYLFISHDLSVVRHiSDRVGVM 234
Cdd:COG5265 510 LKNPPILIFDEATSALDSrterAIQAA----LREVAR--GRTTLVIAHRLSTIVD-ADEILVL 565
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-252 |
1.50e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.62 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRtMIR-LYKPTEGQILFKGQDISNLs 88
Cdd:PRK11650 4 LKLQAVRKSYD----------GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAgLERITSGEIWIGGRVVNEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRksvrkNIQMVFQDpFAsLNPRKTLRSiikepfnthNM-YTMR-------ERNEKVEELLARVGLHPsFAGRYPHE 160
Cdd:PRK11650 72 EPADR-----DIAMVFQN-YA-LYPHMSVRE---------NMaYGLKirgmpkaEIEERVAEAARILELEP-LLDRKPRE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
250
....*....|..
gi 2181075557 241 ELTGKFELYDNP 252
Cdd:PRK11650 215 QIGTPVEVYEKP 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-239 |
1.61e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.04 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlsEEKLRKsVRKNIQMVFQDPFAS 110
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIRE-VRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLRSIIKEPFNTH-NMYTMRERnekVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGlDEETVAHR---VSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2181075557 190 ALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
34-252 |
1.87e-26 |
|
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: 104.03 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSvrknIQMVFQDP--FASl 111
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS----LTIIPQDPtlFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 nprkTLRSIIkEPFnthNMYTmrerNEKVEELLaRV---GLHpsfagrypheFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:cd03369 97 ----TIRSNL-DPF---DEYS----DEEIYGAL-RVsegGLN----------LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 189 SALDVSIQAQvinLMEELQEEF-NLTYLFISHDLSVVRHIsDRVGVMYLGKMMEltgkfelYDNP 252
Cdd:cd03369 154 ASIDYATDAL---IQKTIREEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVKE-------YDHP 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-239 |
1.89e-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: 102.90 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKkyfpirsglfqrkVGDvkAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:cd03215 2 EPVLEVRGLS-------------VKG--AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSeekLRKSVRKNIQMVFQDpfaslnpRKtlrsiikepfnthnmytmrernekveellaRVGLHPSFAGRY----PHEFS 162
Cdd:cd03215 67 RS---PRDAIRAGIAYVPED-------RK------------------------------REGLVLDLSVAEnialSSLLS 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03215 107 GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-223 |
2.64e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.43 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAanqetILELRDVKKYFPirSGlfqrkVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFK 80
Cdd:PRK10535 1 MTA-----LLELKDIRRSYP--SG-----EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDISNLSEEKLRKSVRKNIQMVFQdpfaslnpRKTLRSIIKEPFNTH--NMYTMRERNEKVE---ELLARVGLHPSfAG 155
Cdd:PRK10535 69 GQDVATLDADALAQLRREHFGFIFQ--------RYHLLSHLTAAQNVEvpAVYAGLERKQRLLraqELLQRLGLEDR-VE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 156 RYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNlTYLFISHDLSV 223
Cdd:PRK10535 140 YQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQV 206
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
36-234 |
3.98e-26 |
|
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: 108.30 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRK--------------SVRKNIQ 101
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhigylpqdvelfdgTIAENIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 102 MvfqdpFASLNPrktlrsiikepfnthnmytmrernEKVEELLARVGLHP---SFAGRY-------PHEFSGGQRQRIGI 171
Cdd:COG4618 428 R-----FGDADP------------------------EKVVAAAKLAGVHEmilRLPDGYdtrigegGARLSGGQRQRIGL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 172 ARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHiSDRVGVM 234
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVL 539
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-241 |
4.58e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFPIRSGLFQR-----------KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQ 76
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPSRSlkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 77 ILFKGQdISNLSE------EKLrkSVRKNIQMVfqdpfASLnprktlrsiikepfntHNMyTMRERNEKVEELLArvglh 150
Cdd:COG1134 83 VEVNGR-VSALLElgagfhPEL--TGRENIYLN-----GRL----------------LGL-SRKEIDEKFDEIVE----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 151 psFA--GRYPHE----FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVV 224
Cdd:COG1134 133 --FAelGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAV 209
|
250
....*....|....*..
gi 2181075557 225 RHISDRVGVMYLGKMME 241
Cdd:COG1134 210 RRLCDRAIWLEKGRLVM 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-241 |
5.56e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 101.62 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLseeklRKSVRKNIQMVFQ 105
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-----EKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DPFAslnprktlrsiikepFNThnmyTMRERnekveellarVGLhpsfagryphEFSGGQRQRIGIARALTLNPELIIAD 185
Cdd:cd03247 83 RPYL---------------FDT----TLRNN----------LGR----------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 186 EPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHIsDRVGVMYLGKMME 241
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-295 |
5.75e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.17 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPIRS----------GLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIL 78
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 79 FKGQDISnlseeKLRKSVRKNIQMVF-Q------DpfasLNPRKTLRsIIKEpfnthnMY--TMRERNEKVEELLARVGL 149
Cdd:COG4586 81 VLGYVPF-----KRRKEFARRIGVVFgQrsqlwwD----LPAIDSFR-LLKA------IYriPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 150 HPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISD 229
Cdd:COG4586 145 GE-LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCD 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 230 RVGVMYLGKMmeltgkfeLYDNPLHpytqALlssvpvtRKRGSVKRE-RIVLKGELPSPANPPKGCV 295
Cdd:COG4586 224 RVIVIDHGRI--------IYDGSLE----EL-------KERFGPYKTiVLELAEPVPPLELPRGGEV 271
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-252 |
9.12e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.93 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 27 QRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQI-----------LFKGQDISNLSEE-KLRK 94
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkkNNHELITNPYSKKiKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 95 SVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHnmYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARA 174
Cdd:PRK13631 113 ELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALG--VKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 175 LTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNP 252
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-238 |
9.13e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.94 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYkPT---EGQILFKGQ 82
Cdd:PRK13549 2 MEYLLEMKNITKTF-----------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DisnLSEEKLRKSVRKNIQMVFQDpfASLNPRKTLRSII---KEPfnTHN-------MYtmrernEKVEELLARVGLHPS 152
Cdd:PRK13549 70 E---LQASNIRDTERAGIAIIHQE--LALVKELSVLENIflgNEI--TPGgimdydaMY------LRAQKLLAQLKLDIN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 153 FAGRYpHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVG 232
Cdd:PRK13549 137 PATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTIC 214
|
....*.
gi 2181075557 233 VMYLGK 238
Cdd:PRK13549 215 VIRDGR 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-221 |
9.31e-26 |
|
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: 107.45 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 2 TAANQETILELRDVKKYFPirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKG 81
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 82 QDISNLSEEKLRKSVRkniqMVFQDP--FASlnprkTLRSiikepfnthNMYTMRER--NEKVEELLARVGLHPSFAGRy 157
Cdd:TIGR02868 397 VPVSSLDQDEVRRRVS----VCAQDAhlFDT-----TVRE---------NLRLARPDatDEELWAALERVGLADWLRAL- 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 158 PH-----------EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMeeLQEEFNLTYLFISHDL 221
Cdd:TIGR02868 458 PDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-252 |
9.68e-26 |
|
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: 102.75 E-value: 9.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:COG0410 1 MPMLEVENLHAGY-----------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEEKLrksVRKNIQMVFQDP--FASLNPRKTLRsiikepfnthnM--YTMRERnEKVEELLARV-GLHP-------SFA 154
Cdd:COG0410 70 LPPHRI---ARLGIGYVPEGRriFPSLTVEENLL-----------LgaYARRDR-AEVRADLERVyELFPrlkerrrQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 155 GRypheFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:COG0410 135 GT----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVL 209
|
250
....*....|....*....
gi 2181075557 235 YLGKM-MELTGKfELYDNP 252
Cdd:COG0410 210 ERGRIvLEGTAA-ELLADP 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-250 |
1.04e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 25 LFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlseEKLRKSVRKNIQMVF 104
Cdd:PRK13647 10 LHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----AENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 105 QDP----FASlnprktlrSIIKE-PFNTHNM-YTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:PRK13647 86 QDPddqvFSS--------TVWDDvAFGPVNMgLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYD 250
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-239 |
1.57e-25 |
|
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: 101.84 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSGLFQRK-----------VGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIL 78
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 79 FKGQDISNLS-----EEKLrkSVRKNIQMVfqdpfASLNPRKTlrsiikepfnthnmytmRERNEKVEELLArvglhpsF 153
Cdd:cd03220 81 VRGRVSSLLGlgggfNPEL--TGRENIYLN-----GRLLGLSR-----------------KEIDEKIDEIIE-------F 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 154 A--GRYPHE----FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNlTYLFISHDLSVVRHI 227
Cdd:cd03220 130 SelGDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRL 208
|
250
....*....|..
gi 2181075557 228 SDRVGVMYLGKM 239
Cdd:cd03220 209 CDRALVLEKGKI 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-234 |
2.26e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEeklrKSVRKNIQMVFQDpfAS 110
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA----RAASRRVASVPQD--TS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLRSIIKEPFNTH--NMYTMRERNEK-VEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:PRK09536 88 LSFEFDVRQVVEMGRTPHrsRFDTWTETDRAaVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2181075557 188 VSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLL 212
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
36-241 |
2.92e-25 |
|
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: 106.18 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVrkniQMVFQDPFASlnpRK 115
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV----AMVDQDIFLF---EG 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIkepfnthNMY--TMRERNekVEELLARVGLHPSFAGR---YPHE-------FSGGQRQRIGIARALTLNPELII 183
Cdd:TIGR03796 568 TVRDNL-------TLWdpTIPDAD--LVRACKDAAIHDVITSRpggYDAElaegganLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 184 ADEPVSALDVSIQAQVinlMEELQEEfNLTYLFISHDLSVVRHiSDRVGVMYLGKMME 241
Cdd:TIGR03796 639 LDEATSALDPETEKII---DDNLRRR-GCTCIIVAHRLSTIRD-CDEIIVLERGKVVQ 691
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-240 |
4.15e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNP 113
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIikePFNTHNMYTMRERNEKVE-ELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALD 192
Cdd:PRK13643 100 ETVLKDV---AFGPQNFGIPKEKAEKIAaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2181075557 193 VSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-240 |
8.95e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 3 AANQETILELRDvkkyfpirsgLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ 82
Cdd:COG3845 251 AEPGEVVLEVEN----------LSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISNLSEEKLRK-------------------SVRKNIqmvfqdpfaslnprkTLRSIIKEPFNTHNMYTMRERNEKVEEL 143
Cdd:COG3845 321 DITGLSPRERRRlgvayipedrlgrglvpdmSVAENL---------------ILGRYRRPPFSRGGFLDRKAIRAFAEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 144 LARvglhpsFAGRYPHE------FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFI 217
Cdd:COG3845 386 IEE------FDVRTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLI 458
|
250 260
....*....|....*....|...
gi 2181075557 218 SHDLSVVRHISDRVGVMYLGKMM 240
Cdd:COG3845 459 SEDLDEILALSDRIAVMYEGRIV 481
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-239 |
1.07e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeKLrKSVRKNIQMVFQDPFASLNPR 114
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KL-QGIRKLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 KTLRSIIKEPFNThnMYTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVS 194
Cdd:PRK13644 94 TVEEDLAFGPENL--CLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2181075557 195 IQAQVINLMEELQEEfNLTYLFISHDLSVVrHISDRVGVMYLGKM 239
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
36-239 |
1.08e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKStagrTMIRL----YKPTEGQILFKGQDISNLSEEKL--RKSV-RKNIQMVFqdPF 108
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKS----TLLRAlsgeLSPDSGEVRLNGRPLADWSPAELarRRAVlPQHSSLSF--PF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 aslnprkTLRSIIK---EPFNTHNmytmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALT------LNP 179
Cdd:PRK13548 92 -------TVEEVVAmgrAPHGLSR----AEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-262 |
1.12e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEklrksvRKNIQMVFQDpfASLNPRKTLRS 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQE--NNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 120 IIKEPFNThNMYTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQV 199
Cdd:PRK10771 91 NIGLGLNP-GLKLNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 200 INLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMeltgkfelYDNPlhpyTQALLS 262
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA--------WDGP----TDELLS 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-245 |
7.78e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 13 RDVKKYFPIRSglfqRKVGDV----------KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQ 82
Cdd:COG1129 239 RELEDLFPKRA----AAPGEVvleveglsvgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISN-------------LSEEklRK--------SVRKNIQMVFQDPFAS---LNPRktlrsiikepfnthnmytmRERnE 138
Cdd:COG1129 315 PVRIrsprdairagiayVPED--RKgeglvldlSIRENITLASLDRLSRgglLDRR-------------------RER-A 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 139 KVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFIS 218
Cdd:COG1129 373 LAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVIS 451
|
250 260
....*....|....*....|....*...
gi 2181075557 219 HDLSVVRHISDRVGVMYLGKMM-ELTGK 245
Cdd:COG1129 452 SELPELLGLSDRILVMREGRIVgELDRE 479
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
36-239 |
9.57e-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: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSV---RKNIQMvfqdpFASln 112
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIgylPQDVEL-----FPG-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 prktlrsIIKEpfnthNMYTMRER--NEKVEELLARVGLHPSFAgRYPHEF-----------SGGQRQRIGIARALTLNP 179
Cdd:TIGR01842 407 -------TVAE-----NIARFGENadPEKIIEAAKLAGVHELIL-RLPDGYdtvigpggatlSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHIsDRVGVMYLGKM 239
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-229 |
1.04e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.91 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKkyfpirsglFQRkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDI 84
Cdd:PRK11831 3 SVANLVDMRGVS---------FTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEEKLRkSVRKNIQMVFQDP--FASLNPRKTLrsiikepfnthnMYTMRERNEKVEEL--------LARVGLHPSfA 154
Cdd:PRK11831 72 PAMSRSRLY-TVRKRMSMLFQSGalFTDMNVFDNV------------AYPLREHTQLPAPLlhstvmmkLEAVGLRGA-A 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 155 GRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISD 229
Cdd:PRK11831 138 KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-271 |
1.15e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSGLfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT------ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLR--------------------KSVRKNIQMVFQdpFA--SLNPRKTLRSIIkepFNTHNMYTMR-ERNEKVEELLAR 146
Cdd:PRK13651 77 TKEKekvleklviqktrfkkikkiKEIRRRVGVVFQ--FAeyQLFEQTIEKDII---FGPVSMGVSKeEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 147 VGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRH 226
Cdd:PRK13651 152 VGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 227 ISDRVGVMYLGKMMELTGKFE-------LYDNPLHPytQALLSSVPVTRKRG 271
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDilsdnkfLIENNMEP--PKLLNFVNKLEKKG 280
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-252 |
1.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKkyfpirsglFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKP---TEGQILFKGQD 83
Cdd:PRK13640 3 DNIVEFKHVS---------FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 ISnlseEKLRKSVRKNIQMVFQDP---FASlnprKTLRSIIKepFNTHNMYTMRERNEK-VEELLARVGLhPSFAGRYPH 159
Cdd:PRK13640 74 LT----AKTVWDIREKVGIVFQNPdnqFVG----ATVGDDVA--FGLENRAVPRPEMIKiVRDVLADVGM-LDYIDSEPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 160 EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHiSDRVGVMYLGKM 239
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKL 221
|
250
....*....|...
gi 2181075557 240 MELTGKFELYDNP 252
Cdd:PRK13640 222 LAQGSPVEIFSKV 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-226 |
1.63e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 101.64 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 11 ELRDVKK--YFPIRSGLFQRKvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFkgQDISNLS 88
Cdd:PTZ00265 376 KLKDIKKiqFKNVRFHYDTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLrKSVRKNIQMVFQDP-----------------------------------FASLNPRKTLRSIIKEPFN------- 126
Cdd:PTZ00265 452 DINL-KWWRSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNdmsnttd 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 127 THNMYTMRERNEKVEE-----LLARVGLH----------PSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSAL 191
Cdd:PTZ00265 531 SNELIEMRKNYQTIKDsevvdVSKKVLIHdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
250 260 270
....*....|....*....|....*....|....*
gi 2181075557 192 DVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRH 226
Cdd:PTZ00265 611 DNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-262 |
1.63e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 2 TAANQETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK--PT---EGQ 76
Cdd:PRK14243 3 TLNGTETVLRTENLNVYY-----------GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 77 ILFKGQDISNLSEEKLrkSVRKNIQMVFQ--DPFaslnPRKTLRSIIKEP-FNTH--NMYTMRERN-------EKVEELL 144
Cdd:PRK14243 72 VTFHGKNLYAPDVDPV--EVRRRIGMVFQkpNPF----PKSIYDNIAYGArINGYkgDMDELVERSlrqaalwDEVKDKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 145 ARVGLhpsfagryphEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFnlTYLFISHDLSVV 224
Cdd:PRK14243 146 KQSGL----------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2181075557 225 RHISDRV----------GVMYlGKMMELTGKFELYDNPLHPYTQALLS 262
Cdd:PRK14243 214 ARVSDMTaffnveltegGGRY-GYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-221 |
1.96e-23 |
|
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: 96.69 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKkyfpirsglFQRkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQilfkgqDISN 86
Cdd:COG1119 1 DPLLELRNVT---------VRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEEKLRKSV---RKNIQMV---FQDPF-ASLNPRKTLRSIIkepFNT---HNMYTMRERnEKVEELLARVGLHpSFAGR 156
Cdd:COG1119 64 FGERRGGEDVwelRKRIGLVspaLQLRFpRDETVLDVVLSGF---FDSiglYREPTDEQR-ERARELLELLGLA-HLADR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 157 YPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDL 221
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-240 |
2.59e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 4 ANQETILELRDVKKYFPIRSGLfqrkvgdvkavDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQD 83
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLL-----------HPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 ISNLSEEKLRKSVRKNIQmvfQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPsFAGRYPHEFSG 163
Cdd:PRK10575 75 LESWSSKAFARKVAYLPQ---QLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-234 |
2.63e-23 |
|
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: 96.05 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:TIGR03410 1 LEVSNLNVYY-----------GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLrksVRKNIQMVFQ--DPFASLNPRKTLRSiikepfnthNMYTMRERNEKV-EELLArvgLHP---SFAGRYPHEFSG 163
Cdd:TIGR03410 70 HER---ARAGIAYVPQgrEIFPRLTVEENLLT---------GLAALPRRSRKIpDEIYE---LFPvlkEMLGRRGGDLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:TIGR03410 135 GQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVM 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-248 |
2.87e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.09 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSE 89
Cdd:PRK11176 342 IEFRNVTFTYPGK---------EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKS---VRKNIQMvFQDPFA-----SLNPRKTLRSIIKEPFNTHNMytmrERNEKVEEllarvGLHpSFAGRYPHEF 161
Cdd:PRK11176 413 ASLRNQvalVSQNVHL-FNDTIAnniayARTEQYSREQIEEAARMAYAM----DFINKMDN-----GLD-TVIGENGVLL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDV----SIQAQvinlMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLG 237
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDG 554
|
250
....*....|.
gi 2181075557 238 KMMELTGKFEL 248
Cdd:PRK11176 555 EIVERGTHAEL 565
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
34-241 |
3.39e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSvrknIQMVFQ--DPFASl 111
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA----ISVVSQrvHLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 nprkTLRS--IIKEPfnthnmytmRERNEKVEELLARVGLHPSF------------AGRyphEFSGGQRQRIGIARALTL 177
Cdd:PRK11160 429 ----TLRDnlLLAAP---------NASDEALIEVLQQVGLEKLLeddkglnawlgeGGR---QLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 178 NPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHIsDRVGVMYLGKMME 241
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
34-238 |
3.39e-23 |
|
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: 95.69 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeekLRKSVRKNIQMVFQDP--FASL 111
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP---MHKRARLGIGYLPQEAsiFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 NPRKTLRSIIKEPFnthnmYTMRERNEKVEELLARVGLHP---SFAGRypheFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:cd03218 91 TVEENILAVLEIRG-----LSKKEREEKLEELLEEFHITHlrkSKASS----LSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 189 SALD-VSIQaQVINLMEELQeEFNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:cd03218 162 AGVDpIAVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-241 |
5.99e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 99.09 E-value: 5.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFPirsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTagrtmirLYK------PT---EGQILF 79
Cdd:NF040905 1 ILEMRGITKTFP-----------GVKALDDVNLSVREGEIHALCGENGAGKST-------LMKvlsgvyPHgsyEGEILF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 80 KGQ-----DIsnlseeklRKSVRKNIQMVFQD----PFASL-------NPRKTlRSIIKepfnthnmytMRERNEKVEEL 143
Cdd:NF040905 63 DGEvcrfkDI--------RDSEALGIVIIHQElaliPYLSIaeniflgNERAK-RGVID----------WNETNRRAREL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 144 LARVGLHPSfagryPHEFSG----GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISH 219
Cdd:NF040905 124 LAKVGLDES-----PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISH 197
|
250 260
....*....|....*....|..
gi 2181075557 220 DLSVVRHISDRVGVMYLGKMME 241
Cdd:NF040905 198 KLNEIRRVADSITVLRDGRTIE 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
40-239 |
6.39e-23 |
|
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: 94.54 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklrkSVRKNIQMVFQDP--FASLNPRKTL 117
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA------PYQRPVSMLFQENnlFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 118 RSIIKEPFNTHnmytmRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQA 197
Cdd:TIGR01277 92 GLGLHPGLKLN-----AEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2181075557 198 QVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-202 |
7.09e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.10 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPirsglfQRKVgdvkaVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:COG1137 1 MMTLEAENLVKSYG------KRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 -------------LSEEK--LRK-SVRKNIQMVFQdpfaslnprktLRSIIKEpfnthnmytmrERNEKVEELLARVGLH 150
Cdd:COG1137 70 lpmhkrarlgigyLPQEAsiFRKlTVEDNILAVLE-----------LRKLSKK-----------EREERLEELLEEFGIT 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 151 PsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALD---VS-IQAQVINL 202
Cdd:COG1137 128 H-LRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL 182
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
35-221 |
7.40e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 7.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKlrksvrkniQMVFQDpfASLNPR 114
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQN--EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 KT----------LRSIIKEpfnthnmytmrERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIA 184
Cdd:PRK11248 85 RNvqdnvafglqLAGVEKM-----------QRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 2181075557 185 DEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDL 221
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
34-241 |
8.52e-23 |
|
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: 99.04 E-value: 8.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSvrknIQMVFQDPFASLNp 113
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 rktlrSIIKepfnthNMYTMRERNEKVEELLARV--------------GLHPSFAgRYPHEFSGGQRQRIGIARALTLNP 179
Cdd:TIGR01193 563 -----SILE------NLLLGAKENVSQDEIWAACeiaeikddienmplGYQTELS-EEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEfnlTYLFISHDLSVVRHiSDRVGVMYLGKMME 241
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-240 |
1.13e-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: 94.32 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRS----------GLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILF 79
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 80 KGQDISnlseeKLRKSVRKNIQMVF---QDPFASLNPRKTLRSIikepfntHNMYTM-----RERNEKVEELL--ARVGL 149
Cdd:cd03267 81 AGLVPW-----KRRKKFLRRIGVVFgqkTQLWWDLPVIDSFYLL-------AAIYDLpparfKKRLDELSELLdlEELLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 150 HPSfagrypHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISD 229
Cdd:cd03267 149 TPV------RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALAR 222
|
250
....*....|.
gi 2181075557 230 RVGVMYLGKMM 240
Cdd:cd03267 223 RVLVIDKGRLL 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
51-247 |
3.12e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 95.33 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 51 IVGESGCGKST-----AGrtmirLYKPTEGQI------LFKGQDISNLSEEKlrksvrKNIQMVFQDpfASLNP----RK 115
Cdd:PRK11144 29 IFGRSGAGKTSlinaiSG-----LTRPQKGRIvlngrvLFDAEKGICLPPEK------RRIGYVFQD--ARLFPhykvRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIKEpfnthnmyTMRERNEKVEELLarvGLHPsFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSI 195
Cdd:PRK11144 96 NLRYGMAK--------SMVAQFDKIVALL---GIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 196 QAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMeLTGKFE 247
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK-AFGPLE 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-258 |
6.53e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK-----PTEGQILFKGQdisNLSEEKLR-KSVRKNIQMVFQDP 107
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQ---NIYERRVNlNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 ----------------FASLNPRKTLRSIIKEPFNTHNMYtmrernEKVEELLARVGLhpsfagryphEFSGGQRQRIGI 171
Cdd:PRK14258 98 nlfpmsvydnvaygvkIVGWRPKLEIDDIVESALKDADLW------DEIKHKIHKSAL----------DLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 172 ARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMY-----LGKMMELTGKF 246
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTK 241
|
250
....*....|..
gi 2181075557 247 ELYDNPLHPYTQ 258
Cdd:PRK14258 242 KIFNSPHDSRTR 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-238 |
6.81e-22 |
|
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: 96.05 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK--PTEGQILFKGQDisn 86
Cdd:TIGR02633 1 LLEMKGIVKTF-----------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSP--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEEKLRKSVRKNIQMVFQDpfASLNPRKT-LRSIIKEPFNTHNMYTMR--ERNEKVEELLARVGLHPSFAGRYPHEFSG 163
Cdd:TIGR02633 67 LKASNIRDTERAGIVIIHQE--LTLVPELSvAENIFLGNEITLPGGRMAynAMYLRAKNLLRELQLDADNVTRPVGDYGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:TIGR02633 145 GQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
240-307 |
1.30e-21 |
|
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: 86.69 E-value: 1.30e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 240 MELTGKFELYDNPLHPYTQALLSSVPVTRKRgsvKRERIVLKGELPSPANPPKGCVFHTRCPVAKPIC 307
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPP---KRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
41-231 |
2.34e-21 |
|
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: 90.68 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 41 FSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGqdisnlseeKLRKSVRKNIQMVFQ-DPFA---------- 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---------ASPGKGWRHIGYVPQrHEFAwdfpisvaht 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 110 SLNPRKTLRSIIKEPfnthnmytMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:TIGR03771 72 VMSGRTGHIGWLRRP--------CVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2181075557 190 ALDVSIQAQVINLMEELQEEFNlTYLFISHDLSVVRHISDRV 231
Cdd:TIGR03771 143 GLDMPTQELLTELFIELAGAGT-AILMTTHDLAQAMATCDRV 183
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-257 |
3.61e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEG-----QILFKGQDISNLSEEKlrkSVRKNIQMVFQDPfas 110
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL---EFRRRVGMLFQRP--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 lNP-RKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRY---PHEFSGGQRQRIGIARALTLNPELIIADE 186
Cdd:PRK14271 111 -NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 187 PVSALDVSIQAQVINLMEELQEEfnLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPLHPYT 257
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-248 |
7.57e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 89.70 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKyfpirsglfqrKVGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGRTMirlYKPTEGQILFKGQ 82
Cdd:CHL00131 6 PILEIKNLHA-----------SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTlskviAGHPA---YKILEGDILFKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 DISNLSEEklrKSVRKNIQMVFQDPF--ASLNPRKTLRSIikepFNT-HNMYTMRERN-----EKVEELLARVGLHPSFA 154
Cdd:CHL00131 72 SILDLEPE---ERAHLGIFLAFQYPIeiPGVSNADFLRLA----YNSkRKFQGLPELDpleflEIINEKLKLVGMDPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 155 GRYPHE-FSGGQRQRIGIARALTLNPELIIADEPVSALDVS---IQAQVINLMEELQEefnlTYLFISHDLSVVRHIS-D 229
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpD 220
|
250
....*....|....*....
gi 2181075557 230 RVGVMYLGKMMElTGKFEL 248
Cdd:CHL00131 221 YVHVMQNGKIIK-TGDAEL 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-220 |
1.11e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.68 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYfpIRSGLFQrkvgdVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:PRK10584 4 ENIVEVHHLKKS--VGQGEHE-----LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEEKLRKSVRKNIQMVFQDpFAsLNPRKTLRSIIKEPFNTHNMyTMRERNEKVEELLARVGLHPSFAgRYPHEFSGGQR 166
Cdd:PRK10584 77 MDEEARAKLRAKHVGFVFQS-FM-LIPTLNALENVELPALLRGE-SSRQSRNGAKALLEQLGLGKRLD-HLPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHD 220
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-250 |
1.21e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 12 LRDVKKYFPIRSgLFqrkvgdvkavDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKG--------QD 83
Cdd:COG0488 1 LENLSKSFGGRP-LL----------DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 IsNLSEEKlrkSVRKNIQMVFQDPFASLNPRKTLRSIIKEP-------------FNTHNMYTMRERnekVEELLARVGLH 150
Cdd:COG0488 70 P-PLDDDL---TVLDTVLDGDAELRALEAELEELEAKLAEPdedlerlaelqeeFEALGGWEAEAR---AEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 151 PSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDvsIQAqvINLMEELQEEFNLTYLFISHDlsvvRHISDR 230
Cdd:COG0488 143 EEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES--IEWLEEFLKNYPGTVLVVSHD----RYFLDR 214
|
250 260
....*....|....*....|.
gi 2181075557 231 VGvmylGKMMELT-GKFELYD 250
Cdd:COG0488 215 VA----TRILELDrGKLTLYP 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-234 |
2.96e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLsEEKLrkSVRKNIQMVFQDp 107
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKL--AAQLGIGIIYQE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 faslnprktlRSIIKEPFNTHNMYTMR---------------ERNEKVEELLARVGLHpsfagRYPHEFSG----GQRQR 168
Cdd:PRK09700 89 ----------LSVIDELTVLENLYIGRhltkkvcgvniidwrEMRVRAAMMLLRVGLK-----VDLDEKVAnlsiSHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 169 IGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVM 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-230 |
3.27e-20 |
|
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: 91.02 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAgRTMIR---LYKPTEGQIL----------------FKGQ------ 82
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRgmdQYEPTSGRIIyhvalcekcgyverpsKVGEpcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 83 --------DISNLSeEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKepfNTHNM-YTMRERNEKVEELLARVGLhpsf 153
Cdd:TIGR03269 87 gtlepeevDFWNLS-DKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLE---ALEEIgYEGKEAVGRAVDLIEMVQL---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 154 AGRYPH---EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDR 230
Cdd:TIGR03269 159 SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
39-244 |
5.60e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeekLRKSVRKNIQMVFQDPFAS-LNPRKTL 117
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TAQRLARGLVYLPEDRQSSgLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 118 R-SIIKEPFNTHNMYTMRERNEKVEELLAR-VGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSI 195
Cdd:PRK15439 359 AwNVCALTHNRRGFWIKPARENAVLERYRRaLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2181075557 196 QAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMM-ELTG 244
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISgALTG 487
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-240 |
5.99e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsNLSEEKLRkSVRKNIQMVFQDPFasl 111
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLL-ALRQQVATVFQDPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 nprktlRSIIKEPFNTHNMYTMRERNEKVEELLARV--GLHPSFAGRYPHE----FSGGQRQRIGIARALTLNPELIIAD 185
Cdd:PRK13638 88 ------QQIFYTDIDSDIAFSLRNLGVPEAEITRRVdeALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 186 EPVSALDVSIQAQVINLMEELQEEFNLTyLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
36-226 |
1.25e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILF-KGQDISNLSeeklrksvrkniqmvfQDPFAslnPR 114
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP----------------QRPYL---PL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 KTLRSIIKEPfNTHNMYTmrerNEKVEELLARVGLhPSFAGRY------PHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:COG4178 440 GTLREALLYP-ATAEAFS----DAELREALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|....*....
gi 2181075557 189 SALDVSIQAQvinLMEELQEEF-NLTYLFISHDLSVVRH 226
Cdd:COG4178 514 SALDEENEAA---LYQLLREELpGTTVISVGHRSTLAAF 549
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-239 |
1.55e-19 |
|
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: 85.79 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 26 FQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGRtmIRLYKPTEGQILFKGQDISnlseeklRKSVRKNI 100
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaiSGR--VEGGGTTSGQILFNGQPRK-------PDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 101 QMVFQDPF--ASLNPRKTLRSIIkePFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:cd03234 84 AYVRQDDIllPGLTVRETLTYTA--ILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
29-234 |
1.86e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.91 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 29 KVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAgRTMI-RLYKPTEGQILFKGQDISNLSEEKLRK--SVRKniqmvfQ 105
Cdd:COG4604 10 RYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL-LSMIsRLLPPDSGEVLVDGLDVATTPSRELAKrlAILR------Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DPfaSLNPRKTLRSII---KEPFN----ThnmytmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:COG4604 83 EN--HINSRLTVRELVafgRFPYSkgrlT------AEDREIIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 179 PELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-231 |
8.54e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 8.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGrtmirLYKPTEGQILFKGQD----ISNLSE--EKLRKSVRKN 99
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTllkvlAG-----VLRPTSGTVRRAGGArvayVPQRSEvpDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 100 IQMVFqdpFASLNPRKTLRsiikepfnthnmytmRERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNP 179
Cdd:NF040873 78 VAMGR---WARRGLWRRLT---------------RDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRV 231
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-251 |
8.69e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.49 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksvRKNIQMVFQDP--FASlnprk 115
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQAPvlFSG----- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIkEPFNTHNMYTMRERNEK--VEELLAR--VGLHP--SFAGrypHEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:PLN03130 1328 TVRFNL-DPFNEHNDADLWESLERahLKDVIRRnsLGLDAevSEAG---ENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 190 ALDVSIQAQVinlMEELQEEF-NLTYLFISHDLSVVrhI-SDRVGVMYLGKMMELTGKFELYDN 251
Cdd:PLN03130 1404 AVDVRTDALI---QKTIREEFkSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-222 |
1.13e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEeklrKSVRKNIQMVFQDpfAS 110
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQN--AT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLRSIIKEPFNTHN-MYTM--RERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:PRK10253 92 TPGDITVQELVARGRYPHQpLFTRwrKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2181075557 188 VSALDVSIQAQVINLMEELQEEFNLTYLFISHDLS 222
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLN 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-239 |
1.93e-18 |
|
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: 85.65 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPT-EGQILFKGQ--D 83
Cdd:TIGR02633 255 DVILEARNLTCWDVINP--------HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 84 ISNLSeeklrKSVRKNIQMVFQD-------PFASLNPRKTLRSIikepfnthNMYTMRER-NEKVEELLARVGL------ 149
Cdd:TIGR02633 327 IRNPA-----QAIRAGIAMVPEDrkrhgivPILGVGKNITLSVL--------KSFCFKMRiDAAAELQIIGSAIqrlkvk 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 150 --HPSFA-GRypheFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRH 226
Cdd:TIGR02633 394 taSPFLPiGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLG 468
|
250
....*....|...
gi 2181075557 227 ISDRVGVMYLGKM 239
Cdd:TIGR02633 469 LSDRVLVIGEGKL 481
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-239 |
2.47e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 81.44 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSGLFQRKVgdvkaVDGVSFSLKKGETLGIVGESGCGKST-----AGRTMirlYKPTEGQILFKGQDI 84
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQL-----LKNVSGKAKPGELTAIMGPSGAGKSTllnalAGRRT---GLGVSGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SnlseeklRKSVRKNIQMVFQDP--FASLNPRKTLrsiikepfnthnMYTMRERnekveellarvGLhpsfagryphefS 162
Cdd:cd03213 76 D-------KRSFRKIIGYVPQDDilHPTLTVRETL------------MFAAKLR-----------GL------------S 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLS-VVRHISDRVGVMYLGKM 239
Cdd:cd03213 114 GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-238 |
3.40e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPirsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:PRK10762 2 QALLQLKGIDKAFP-----------GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSEeklRKSVRKNIQMVFQDpfasLN--PRKTLRSII---KEPFNTHNMYTMRERNEKVEELLARVGLhpSFAGRYP-HE 160
Cdd:PRK10762 71 NGP---KSSQEAGIGIIHQE----LNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNL--RFSSDKLvGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-246 |
3.83e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSGlfqrkvgdVKAVDGVSFSLKKGETLGIVGESGcgkstAGRT--MIRLYKP----TEGQILFK 80
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPH--------IKRVDDVSFSLRRGEILGIAGLVG-----AGRTelVQCLFGAypgrWEGEIFID 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQ--DISNLseeklRKSVRKNIQMVFQD-------PFASLNPRKTLRSIIKepFNTHNMYTMRERNEKVEELLARVGL-- 149
Cdd:PRK13549 324 GKpvKIRNP-----QQAIAQGIAMVPEDrkrdgivPVMGVGKNITLAALDR--FTGGSRIDDAAELKTILESIQRLKVkt 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 150 -HPSFA-GRypheFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHI 227
Cdd:PRK13549 397 aSPELAiAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGL 471
|
250
....*....|....*....
gi 2181075557 228 SDRVGVMYLGKmmeLTGKF 246
Cdd:PRK13549 472 SDRVLVMHEGK---LKGDL 487
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-252 |
6.76e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.16 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 12 LRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEK 91
Cdd:PRK11000 6 LRNVTKAY-----------GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 92 lrksvrKNIQMVFQDpFAsLNPRKTLrsiikepfnTHNM-YTMR-------ERNEKVEELlARVGLHPSFAGRYPHEFSG 163
Cdd:PRK11000 75 ------RGVGMVFQS-YA-LYPHLSV---------AENMsFGLKlagakkeEINQRVNQV-AEVLQLAHLLDRKPKALSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 164 GQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELT 243
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
....*....
gi 2181075557 244 GKFELYDNP 252
Cdd:PRK11000 217 KPLELYHYP 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-233 |
8.39e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPirsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdisnlse 89
Cdd:PRK11288 5 LSFDGIGKTFP-----------GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklrksvrkniQMVFQDPFASLN-------------PRKTLRSII---KEPfNTHNMYTMRERNEKVEELLARVGLH--P 151
Cdd:PRK11288 67 -----------EMRFASTTAALAagvaiiyqelhlvPEMTVAENLylgQLP-HKGGIVNRRLLNYEAREQLEHLGVDidP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 152 SFAGRYpheFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRV 231
Cdd:PRK11288 135 DTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAI 210
|
..
gi 2181075557 232 GV 233
Cdd:PRK11288 211 TV 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
38-205 |
1.07e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDI--SNLSEE----------KLRKSVRKNIQmvFQ 105
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddPDVAEAchylghrnamKPALTVAENLE--FW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 DPFaslnprktlrsiikepFNTHNmytmrernEKVEELLARVGLHPSFAGRYpHEFSGGQRQRIGIARALTLNPELIIAD 185
Cdd:PRK13539 98 AAF----------------LGGEE--------LDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180
....*....|....*....|
gi 2181075557 186 EPVSALDVSIQAQVINLMEE 205
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRA 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-231 |
2.34e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnl 87
Cdd:COG0488 314 KVLELEGLSKSY-----------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 88 seeklrkSVRKNIQMVF--QDpFASLNPRKTLRSIIKEpfnthnmYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQ 165
Cdd:COG0488 373 -------KLGETVKIGYfdQH-QEELDPDKTVLDELRD-------GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGE 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 166 RQRIGIARALTLNPELIIADEPVSALDVsiqaQVINLMEELQEEFNLTYLFISHDLSVVRHISDRV 231
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRI 499
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
38-203 |
3.09e-17 |
|
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: 78.69 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlseeKLRKSVRKNIQMVFQDPF--ASLNPRK 115
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-----FQRDSIARGLLYLGHAPGikTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRsiIKEPFNThnmytmrerNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSI 195
Cdd:cd03231 93 NLR--FWHADHS---------DEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 2181075557 196 QAQVINLM 203
Cdd:cd03231 161 VARFAEAM 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
34-251 |
2.16e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLY---KPTEGQILFKGQDISNlsEEKLRKSVRKN---IQMVFQDp 107
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQR--EGRLARDIRKSranTGYIFQQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 FASLNPRKTLRSII-----KEPF-NTHNMYTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPEL 181
Cdd:PRK09984 95 FNLVNRLSVLENVLigalgSTPFwRTCFSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 182 IIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMeLTGKFELYDN 251
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF-YDGSSQQFDN 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-265 |
2.19e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.41 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSvrknIQMVFQDP--FASlnprk 115
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPvlFSG----- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIkEPFNTHNMYTMRERNEK--VEELLAR--VGLHPS-FAGryPHEFSGGQRQRIGIARALTLNPELIIADEPVSA 190
Cdd:PLN03232 1325 TVRFNI-DPFSEHNDADLWEALERahIKDVIDRnpFGLDAEvSEG--GENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 191 LDVSIQAQVinlMEELQEEF-NLTYLFISHDLSVVRHiSDRVGVMYLGKMMELTGKFELYDNPLHPYTQALLSSVP 265
Cdd:PLN03232 1402 VDVRTDSLI---QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-247 |
2.73e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.50 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTagrtMIRL---YKPTEGQILFKGQDISNLSEEklrkSVRKNIQMVFQDPfaSLnPRK 115
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTS----LLNAllgFLPYQGSLKINGIELRELDPE----SWRKHLSWVGQNP--QL-PHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIKepFNTHNMytmreRNEKVEELLARVGLHpSFAGRYPH-----------EFSGGQRQRIGIARALTLNPELIIA 184
Cdd:PRK11174 438 TLRDNVL--LGNPDA-----SDEQLQQALENAWVS-EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 185 DEPVSALDVSIQAQVinlMEELQEE-FNLTYLFISHDLSVVRHIsDRVGVMYLGKMMElTGKFE 247
Cdd:PRK11174 510 DEPTASLDAHSEQLV---MQALNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ-QGDYA 568
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
31-245 |
3.26e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksVRKNIQMVFQdpfas 110
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI---MREAVAIVPE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 lNPRKTLRSIIKEPFNTHNMYTMR----ERNEKVEELLARvgLHPSFAGRyPHEFSGGQRQRIGIARALTLNPELIIADE 186
Cdd:PRK11614 88 -GRRVFSRMTVEENLAMGGFFAERdqfqERIKWVYELFPR--LHERRIQR-AGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 187 PVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM-MELTGK 245
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvLEDTGD 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-205 |
7.60e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 37 DGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLR-----------KSVrkniqmvfq 105
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylghqpgiKTE--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 dpfasLNPRKTLRsiikepFNT--HNMYTmrerNEKVEELLARVGLhpsfAGR--YP-HEFSGGQRQRIGIARALTLNPE 180
Cdd:PRK13538 89 -----LTALENLR------FYQrlHGPGD----DEALWEALAQVGL----AGFedVPvRQLSAGQQRRVALARLWLTRAP 149
|
170 180
....*....|....*....|....*
gi 2181075557 181 LIIADEPVSALDVSIQAQVINLMEE 205
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-250 |
8.18e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirSGlfqrkvgdVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLS 88
Cdd:PRK15439 11 LLCARSISKQY---SG--------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 EEKLRKSvrkNIQMVFQDPFasLNPRKTLRSIIkepfnTHNMYTMRERNEKVEELLARVGLHPSfagryPHEFSG----G 164
Cdd:PRK15439 80 PAKAHQL---GIYLVPQEPL--LFPNLSVKENI-----LFGLPKRQASMQKMKQLLAALGCQLD-----LDSSAGslevA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 165 QRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMMeLTG 244
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA-LSG 222
|
....*.
gi 2181075557 245 KFELYD 250
Cdd:PRK15439 223 KTADLS 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
38-205 |
1.05e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.32 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEE--------------KLRKSVRKNIQmv 103
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphenilylghlpglKPELSALENLH-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 104 FQDPFASLNPRKtlrsiikepfnthnmytmrernekVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELII 183
Cdd:TIGR01189 96 FWAAIHGGAQRT------------------------IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180
....*....|....*....|..
gi 2181075557 184 ADEPVSALDVSIQAQVINLMEE 205
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRA 172
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
31-231 |
1.28e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILfkgqdisnlSEEKLRksvrknIQMVFQdpfaS 110
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR------IGYVPQ----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLrsiikePFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYP-HEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:PRK09544 76 LYLDTTL------PLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2181075557 190 ALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRV 231
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-233 |
2.36e-15 |
|
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: 74.37 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 42 SLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIL-------FKGQDISNLSEEKLRKSVRKNIQMVFQDPFaslnpr 114
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEieldtvsYKPQYIKADYEGTVRDLLSSITKDFYTHPY------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 ktlrsiikepFNTHNMYTMrerneKVEELLARvglhpsfagRYPhEFSGGQRQRIGIARALTLNPELIIADEPVSALDVS 194
Cdd:cd03237 95 ----------FKTEIAKPL-----QIEQILDR---------EVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 2181075557 195 IQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGV 233
Cdd:cd03237 150 QRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
34-240 |
2.80e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 34 KAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeekLRKSVRKNIQMVFQDpfASLNP 113
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQE--ASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLhPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2181075557 194 SIQAQVINLMEELQeEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK10895 171 ISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-242 |
3.14e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 5 NQETILELRDVKKYfpirsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDI 84
Cdd:PRK09700 261 AHETVFEVRNVTSR-------------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEeklRKSVRKNIQMV--------FQDPFASLNPRKTLRSIIKEPFN-THNMYTMRERNEKVEELLARVGLHPSFAG 155
Cdd:PRK09700 328 SPRSP---LDAVKKGMAYItesrrdngFFPNFSIAQNMAISRSLKDGGYKgAMGLFHEVDEQRTAENQRELLALKCHSVN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 156 RYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMY 235
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFC 483
|
....*..
gi 2181075557 236 LGKMMEL 242
Cdd:PRK09700 484 EGRLTQI 490
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
31-192 |
4.79e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSeeklrKSVRKNIQMVFQdpFAS 110
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-----RLARARIGVVPQ--FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLRSIIKEPFNTHNMYTmRERNEKVEELLARVGLHPSFAGRYPhEFSGGQRQRIGIARALTLNPELIIADEPVSA 190
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMST-REIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
..
gi 2181075557 191 LD 192
Cdd:PRK13536 203 LD 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-222 |
4.89e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.52 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksvRKNIQMVFQDPFasL 111
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPF--L 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 NPRKTLRSI-IKEPFNTHnmytmrernEKVEEL--LARVglHPSFAgRYPHEF-----------SGGQRQRIGIARALTL 177
Cdd:PRK10789 401 FSDTVANNIaLGRPDATQ---------QEIEHVarLASV--HDDIL-RLPQGYdtevgergvmlSGGQKQRISIARALLL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2181075557 178 NPELIIADEPVSALDVSIQAQVI-NLMEELQEEfnlTYLFISHDLS 222
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILhNLRQWGEGR---TVIISAHRLS 511
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
35-240 |
7.95e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnlseeklRKSVRKN-IQMVFQDPFASLNP 113
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT--------RQALQKNlVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLRSIIKEPFNTHnMYTMR----ERNEKVEELLARVGLHpSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:PRK15056 94 PVLVEDVVMMGRYGH-MGWLRrakkRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 190 ALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVgVMYLGKMM 240
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-192 |
9.10e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:PRK13537 5 VAPIDFRNVEKRY-----------GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 LSeeklrKSVRKNIQMVFQdpFASLNPRKTLRSIIKePFNTHNMYTMRERNEKVEELLARVGLHpSFAGRYPHEFSGGQR 166
Cdd:PRK13537 74 RA-----RHARQRVGVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLE-NKADAKVGELSGGMK 144
|
170 180
....*....|....*....|....*.
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALD 192
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-246 |
1.57e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGcgkstAGRT--MIRLY---KPTEGQILFKGQDISN-------------LSEEK------ 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMG-----AGRTelMKVLYgalPRTSGYVTLDGHEVVTrspqdglangivyISEDRkrdglv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 92 LRKSVRKNIQMVFQDPFASLN-------PRKTLRSIIKEpFNThnmytmrerneKVEELLARVGLhpsfagrypheFSGG 164
Cdd:PRK10762 343 LGMSVKENMSLTALRYFSRAGgslkhadEQQAVSDFIRL-FNI-----------KTPSMEQAIGL-----------LSGG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 165 QRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKmmeLTG 244
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR---ISG 475
|
..
gi 2181075557 245 KF 246
Cdd:PRK10762 476 EF 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
42-233 |
1.72e-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: 74.05 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 42 SLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQ------ILFKGQDISNLSEEklrkSVRKNIQMVFQDPFASlnprK 115
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkISYKPQYISPDYDG----TVEEFLRSANTDDFGS----S 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIKEPFNTHNMYtmrERNekVEELlarvglhpsfagryphefSGGQRQRIGIARALTLNPELIIADEPVSALDVSI 195
Cdd:COG1245 434 YYKTEIIKPLGLEKLL---DKN--VKDL------------------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 2181075557 196 QAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGV 233
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
40-219 |
1.85e-14 |
|
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: 69.88 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnlseeklRKSVRKNIQMVFQDPFAslnPRKTLRS 119
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------GMPEGEDLLFLPQRPYL---PLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 120 IIkepfnthnmytmrernekveellarvglhpsfagRYP--HEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQA 197
Cdd:cd03223 83 QL----------------------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 2181075557 198 QvinLMEELQEEFnLTYLFISH 219
Cdd:cd03223 129 R---LYQLLKELG-ITVISVGH 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-192 |
1.86e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 28 RKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTagrTM---IRLYKPTEGQILFKGQ--DISNLSeekLRK-------- 94
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST---TMkmlTGLLPASEGEAWLFGQpvDAGDIA---TRRrvgymsqa 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 95 -------SVRKNIQM---VFQDPFASLNPRktlrsiikepfnthnmytmrernekVEELLARVGLHPsFAGRYPHEFSGG 164
Cdd:NF033858 348 fslygelTVRQNLELharLFHLPAAEIAAR-------------------------VAEMLERFDLAD-VADALPDSLPLG 401
|
170 180
....*....|....*....|....*...
gi 2181075557 165 QRQRIGIARALTLNPELIIADEPVSALD 192
Cdd:NF033858 402 IRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-226 |
3.39e-14 |
|
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: 70.44 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 32 DVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFAsL 111
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 NPRKTLRSIIKEPFNthnmytmRERNEKVEE---LLARVGLHP----SFAGRYPHEFSGGQRQRIGIARALTLNPELIIA 184
Cdd:cd03290 92 NATVEENITFGSPFN-------KQRYKAVTDacsLQPDIDLLPfgdqTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2181075557 185 DEPVSALDVSIQAQVIN--LMEELQEEfNLTYLFISHDLSVVRH 226
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLPH 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
40-233 |
3.45e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSL-------KKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnlsEEKLRKSVRKniQMVFQDPFASLn 112
Cdd:PRK13409 352 DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPELKISYKP--QYIKPDYDGTV- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 pRKTLRSIiKEPFNTHNMYTmrernekveELLARVGLHPSFaGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALD 192
Cdd:PRK13409 418 -EDLLRSI-TDDLGSSYYKS---------EIIKPLQLERLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2181075557 193 VSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGV 233
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-241 |
5.59e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGET--------------LGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVrkni 100
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 101 QMVFQDPF---ASLNPRKTLRSIIKEpfnthnmytmrernEKVEELLARV-----------GLHpSFAGRYPHEFSGGQR 166
Cdd:PRK10790 418 AMVQQDPVvlaDTFLANVTLGRDISE--------------EQVWQALETVqlaelarslpdGLY-TPLGEQGNNLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHiSDRVGVMYLGKMME 241
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-248 |
8.14e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.21 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 30 VGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMI--RLYKPTEGQILFKGQDISNLSEEKlrkSVRKNIQMVFQDP 107
Cdd:PRK09580 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED---RAGEGIFMAFQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 108 F------------ASLNPRKTLRSiiKEPFNTHNMYTMRErnEKV------EELLAR---VGlhpsfagrypheFSGGQR 166
Cdd:PRK09580 88 VeipgvsnqfflqTALNAVRSYRG--QEPLDRFDFQDLME--EKIallkmpEDLLTRsvnVG------------FSGGEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHIS-DRVGVMYLGKMMElTGK 245
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVK-SGD 229
|
...
gi 2181075557 246 FEL 248
Cdd:PRK09580 230 FTL 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-238 |
1.23e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 11 ELRDVKKYFPIRSGLFQRKVgdvkaVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKgqdisnlsee 90
Cdd:COG2401 26 RVAIVLEAFGVELRVVERYV-----LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 91 klrksvrkniqmVFQDPFaslnPRKtlRSIIKepfnthNMYTMRERNEKVEeLLARVGLH-PSFAGRYPHEFSGGQRQRI 169
Cdd:COG2401 91 ------------VPDNQF----GRE--ASLID------AIGRKGDFKDAVE-LLNAVGLSdAVLWLRRFKELSTGQKFRF 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 170 GIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVgVMYLGK 238
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDL-LIFVGY 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-231 |
3.67e-13 |
|
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: 65.93 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnlse 89
Cdd:cd03221 1 IELENLSKTY-----------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklrksvrkniqmvfqdpfaslnprktlrsiikepfnthnmytmrERNEKVeellaRVGlhpsfagrYPHEFSGGQRQRI 169
Cdd:cd03221 58 ---------------------------------------------TWGSTV-----KIG--------YFEQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 170 GIARALTLNPELIIADEPVSALDV-SIQAqvinLMEELQeEFNLTYLFISHDLSVVRHISDRV 231
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALK-EYPGTVILVSHDRYFLDQVATKI 137
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-238 |
4.26e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 12 LRDVKKYFPirsglfqrkvgDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsNLSEEK 91
Cdd:PRK10982 1 MSNISKSFP-----------GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 92 lrKSVRKNIQMVFQDpfasLNPRKTlRSII----------KEPFNTHN-MYtmRERNEKVEELLARVGLHPSFAgryphE 160
Cdd:PRK10982 69 --EALENGISMVHQE----LNLVLQ-RSVMdnmwlgryptKGMFVDQDkMY--RDTKAIFDELDIDIDPRAKVA-----T 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 161 FSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGK 238
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-240 |
7.92e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKST-----AGRTmirlykPTEGQILFKGQDISNLSEEKLRK-------SVRKNIQM- 102
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTllarmAGLL------PGQGEILLNGRPLSDWSAAELARhraylsqQQSPPFAMp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 103 VFQdpFASLNPRKTLRSiikepfnthnmytmrERNEK-VEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARAL-----T 176
Cdd:COG4138 86 VFQ--YLALHQPAGASS---------------EAVEQlLAQLAEALGLED-KLSRPLTQLSGGEWQRVRLAAVLlqvwpT 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 177 LNPE--LIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLS-VVRHiSDRVGVMYLGKMM 240
Cdd:COG4138 148 INPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNhTLRH-ADRVWLLKQGKLV 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
38-206 |
1.25e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKST-----AGRTMIRLYKptEGQILFKGQDIsNLSEEKLRKSvrkniqMVFQDP--FAS 110
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGMPI-DAKEMRAISA------YVQQDDlfIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLrsIIKEPFNTHNMYTMRERNEKVEELLARVGLHPS------FAGRYpHEFSGGQRQRIGIARALTLNPELIIA 184
Cdd:TIGR00955 114 LTVREHL--MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCantrigVPGRV-KGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180
....*....|....*....|..
gi 2181075557 185 DEPVSALDVSIQAQVINLMEEL 206
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGL 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-239 |
1.48e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKST-----AGRTmirlykPTEGQILFKGQDISNLSEEKLRK-------SVRKNIQM-VFQ 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarmAGLL------PGSGSIQFAGQPLEAWSAAELARhraylsqQQTPPFAMpVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 dpFASLNprktlrsiikEPFNTHNmytmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARAL-----TLNPE 180
Cdd:PRK03695 89 --YLTLH----------QPDKTRT----EAVASALNEVAEALGLDD-KLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 181 --LIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKM 239
Cdd:PRK03695 152 gqLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-235 |
2.64e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.85 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSL------KKGETLGIVGESGCGKSTAGR--------------------TMIRLYKPTEGQILFKgqdisNLSEEKLR 93
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALKilagklkpnlgkfddppdwdEILDEFRGSELQNYFT-----KLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 94 KSVRKniQMVFQDPfaslnprKTLRSiikepfNTHNMYTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIAR 173
Cdd:cd03236 89 VIVKP--QYVDLIP-------KAVKG------KVGELLKKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 174 ALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNlTYLFISHDLSVVRHISDRVGVMY 235
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
38-234 |
7.54e-12 |
|
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: 63.64 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdISNLSEEK--LRKSVRKNIqmVFQDPFaslnprk 115
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVSQEPwiQNGTIRENI--LFGKPF------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 tlrsiikepfnthnmytmreRNEKVEELLARVGLHPSFAgRYPH-------E----FSGGQRQRIGIARALTLNPELIIA 184
Cdd:cd03250 93 --------------------DEERYEKVIKACALEPDLE-ILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 185 DEPVSALDVSIQAQVIN--LMEELQEefNLTYLFISHDLSVVRHiSDRVGVM 234
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
39-233 |
8.72e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYK-PTEGQILFKGQDISNLSEEKLRK-SVRKNIQMVFQDPFAS------ 110
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNEHTNDMTNEQDYQgDEEQNVGMKNVNEFSLtkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 ------------------------LNPRKTLRSII-KEP--FNT---HNMYTMRER---------------NEKVEELLA 145
Cdd:PTZ00265 1267 gedstvfknsgkilldgvdicdynLKDLRNLFSIVsQEPmlFNMsiyENIKFGKEDatredvkrackfaaiDEFIESLPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 146 RvglHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVR 225
Cdd:PTZ00265 1347 K---YDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
....*...
gi 2181075557 226 HiSDRVGV 233
Cdd:PTZ00265 1424 R-SDKIVV 1430
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-250 |
9.13e-12 |
|
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: 66.12 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 21 IRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdISNLSEEKLRK--SVRK 98
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAWIQndSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 99 NIqmVFQDPfasLNPrKTLRSIIKEPfnthnmytmrernekveELLARVGLHPSF----AGRYPHEFSGGQRQRIGIARA 174
Cdd:TIGR00957 718 NI--LFGKA---LNE-KYYQQVLEAC-----------------ALLPDLEILPSGdrteIGEKGVNLSGGQKQRVSLARA 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 175 LTLNPELIIADEPVSALDV----SIQAQVINLMEELQeefNLTYLFISHDLSVVRHIsDRVGVMYLGKMMELTGKFELYD 250
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAhvgkHIFEHVIGPEGVLK---NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-252 |
9.66e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 38 GVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRK--------------SVRKNIqmv 103
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRqfsmipqdpvlfdgTVRQNV--- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 104 fqDPFASLNPRKTLRSIikepfnthNMYTMRER----NEKVEELLARVGLHpsfagrypheFSGGQRQRIGIARA-LTLN 178
Cdd:PTZ00243 1405 --DPFLEASSAEVWAAL--------ELVGLRERvaseSEGIDSRVLEGGSN----------YSVGQRQLMCMARAlLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 179 PELIIADEPVS----ALDVSIQAQVINLMEelqeefNLTYLFISHDLSVVRHIsDRVGVMYLGKMMELTGKFELYDNP 252
Cdd:PTZ00243 1465 SGFILMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
43-235 |
2.80e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 43 LKKGETLGIVGESGCGKSTAGR--------------------TMIRLYKPTEGQILFKgqdisNLSEEKLRkSVRKnIQM 102
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKilsgelipnlgdyeeepswdEVLKRFRGTELQNYFK-----KLYNGEIK-VVHK-PQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 103 VFQDPfaslnprKTLRSIIKEPFNTHNmytmrERNeKVEELLARVGLHPSFaGRYPHEFSGGQRQRIGIARALTLNPELI 182
Cdd:PRK13409 169 VDLIP-------KVFKGKVRELLKKVD-----ERG-KLDEVVERLGLENIL-DRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 183 IADEPVSALDVSIQAQVINLMEELQEefNLTYLFISHDLSVVRHISDRVGVMY 235
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
35-241 |
3.11e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKST-----AGRTMirlykPTEGQILFKGQD----ISNLSEEKLrkSVRKNIQMvfq 105
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTlsnliAGVTM-----PNKGTVDIKGSAaliaISSGLNGQL--TGIENIEL--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 106 dpfaslnprKTLrsiikepfnthnmyTMRERNEKVEELLARVglhPSFA--GRYPHE----FSGGQRQRIGIARALTLNP 179
Cdd:PRK13545 109 ---------KGL--------------MMGLTKEKIKEIIPEI---IEFAdiGKFIYQpvktYSSGMKSRLGFAISVHINP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 180 ELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
36-289 |
3.60e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTagrtmirLYKPTEGQIL---FKGQDISNlsEEKLRKSVRKNIQMVFQDP--FAS 110
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKST-------LLNALAGRIQgnnFTGTILAN--NRKPTKQILKRTGFVTQDDilYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 111 LNPRKTLR--SIIKEPfnthNMYTMRERNEKVEELLARVGL----HPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIA 184
Cdd:PLN03211 155 LTVRETLVfcSLLRLP----KSLTKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 185 DEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGV------MYLGKMMELTGKFELYDN----PLH 254
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVlsegrcLFFGKGSDAMAYFESVGFspsfPMN 310
|
250 260 270
....*....|....*....|....*....|....*
gi 2181075557 255 PYTQALLSSVPVTRKRGSVKRERIVLKGELPSPAN 289
Cdd:PLN03211 311 PADFLLDLANGVCQTDGVSEREKPNVKQSLVASYN 345
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
39-225 |
5.12e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnlseEKLRKSVRKniQMVFQDPFASLNPRKTLR 118
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQK--QLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 119 SIIKepFNTHNMYTMRERNE-----KVEELLarvglhpsfagRYP-HEFSGGQRQRIGIARALTLNPELIIADEPVSALD 192
Cdd:PRK13540 93 ENCL--YDIHFSPGAVGITElcrlfSLEHLI-----------DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|...
gi 2181075557 193 VSIQAQVINLMEELQEEFNLTYLFISHDLSVVR 225
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
31-226 |
7.34e-11 |
|
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: 63.23 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVkAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMI--------RLYKPTEGQILFkgqdisnlseeklrksvrkniqm 102
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----------------------- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 103 VFQDPFASLnprKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHP--------SFAGRYPHEFSGGQRQRIGIARA 174
Cdd:TIGR00954 520 VPQRPYMTL---GTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARL 596
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2181075557 175 LTLNPELIIADEPVSALDVSIQAQvinlMEELQEEFNLTYLFISHDLSVVRH 226
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGY----MYRLCREFGITLFSVSHRKSLWKY 644
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-235 |
8.43e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 40 SFSL------KKGETLGIVGESGCGKSTA------------GR--------TMIRLYKPTEGQILFKgqdisNLSEEKLR 93
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTAlkilsgelkpnlGDydeepswdEVLKRFRGTELQDYFK-----KLANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 94 KSVRknIQMVFQDP-FASLNPRKTLRSIikepfnthnmytmRERNeKVEELLARVGLHPSFaGRYPHEFSGGQRQRIGIA 172
Cdd:COG1245 162 VAHK--PQYVDLIPkVFKGTVRELLEKV-------------DERG-KLDELAEKLGLENIL-DRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 173 RALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMY 235
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
39-252 |
9.84e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksvRKNIQMVFQDP--FASlnprkT 116
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPvlFSG-----S 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 117 LRSIIkEPFNTHNmytmrerNEKVEELLARVGLHpSFAGRYP----HE-------FSGGQRQRIGIARALTLNPELIIAD 185
Cdd:TIGR00957 1376 LRMNL-DPFSQYS-------DEEVWWALELAHLK-TFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 186 EPVSALDVS----IQAQVINLMEelqeefNLTYLFISHDLSVvrhISDRVGVMYLGKmmeltGKFELYDNP 252
Cdd:TIGR00957 1447 EATAAVDLEtdnlIQSTIRTQFE------DCTVLTIAHRLNT---IMDYTRVIVLDK-----GEVAEFGAP 1503
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-234 |
1.64e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 21 IRSGLFqrKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSV---- 96
Cdd:PRK10938 6 ISQGTF--RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVsdew 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 97 -RKNIQMVFQDPFaslNPRKTLRSIIKEpfNTHNmytmrerNEKVEELLARVGLHPSFAGRYPHeFSGGQRQRIGIARAL 175
Cdd:PRK10938 84 qRNNTDMLSPGED---DTGRTTAEIIQD--EVKD-------PARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2181075557 176 TLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVM 234
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-187 |
2.64e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKST-----AGRTMIRlykptEGQILFKGQDISNLSEEK------------LR 93
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSllsliAGARKIQ-----QGRVEVLGGDMADARHRRavcpriaympqgLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 94 K------SVRKNIQmvFqdpFASLnprktlrsiikepFNtHNMytmRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQ 167
Cdd:NF033858 87 KnlyptlSVFENLD--F---FGRL-------------FG-QDA---AERRRRIDELLRATGLAP-FADRPAGKLSGGMKQ 143
|
170 180
....*....|....*....|
gi 2181075557 168 RIGIARALTLNPELIIADEP 187
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEP 163
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-249 |
2.72e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKgQD--ISNLSEEKLR--------------- 93
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARLQQDPPRnvegtvydfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 94 ------KSVRKNIQMVFQDPFAS-LNPRKTLRSIIkepfNTHNMYTMRERnekVEELLARVGLHPSFAgryPHEFSGGQR 166
Cdd:PRK11147 93 eqaeylKRYHDISHLVETDPSEKnLNELAKLQEQL----DHHNLWQLENR---INEVLAQLGLDPDAA---LSSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 167 QRIGIARALTLNPELIIADEPVSALDVsiqaQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKF 246
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNY 238
|
...
gi 2181075557 247 ELY 249
Cdd:PRK11147 239 DQY 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-277 |
2.92e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.57 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 1 MTAANQETILELRDVKKYFPIRSGlfqrkvgdvKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFK 80
Cdd:TIGR01257 1929 ISGGNKTDILRLNELTKVYSGTSS---------PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA 1999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDI-SNLSEeklrksVRKNiqMVFQDPFASLNPRKTLRSiikepfntHNMYTMRERNEKVEEL-------LARVGLhPS 152
Cdd:TIGR01257 2000 GKSIlTNISD------VHQN--MGYCPQFDAIDDLLTGRE--------HLYLYARLRGVPAEEIekvanwsIQSLGL-SL 2062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 153 FAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLfISHDLSVVRHISDRVG 232
Cdd:TIGR01257 2063 YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLA 2141
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 233 VMY------LGKMMELTGKF---------------ELYDNpLHPYTQALLSSVPvtrkrGSVKRER 277
Cdd:TIGR01257 2142 IMVkgafqcLGTIQHLKSKFgdgyivtmkikspkdDLLPD-LNPVEQFFQGNFP-----GSVQRER 2201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-244 |
5.30e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSglFqrkvgdvkAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlse 89
Cdd:PRK10522 323 LELRNVTFAYQDNG--F--------SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 EKLRKSVRKNIQMVFQD--PFAS-LNPRKTlrsiIKEPfnthnmytmrernEKVEELLARVGLHPSFA---GRYPH-EFS 162
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDfhLFDQlLGPEGK----PANP-------------ALVEKWLERLKMAHKLEledGRISNlKLS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 163 GGQRQRIGIARALTLNPELIIADEpvSALDVSIQAQVI---NLMEELQEEfNLTYLFISHDLSVVRHiSDRVGVMYLGKM 239
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDE--WAADQDPHFRREfyqVLLPLLQEM-GKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
....*
gi 2181075557 240 MELTG 244
Cdd:PRK10522 528 SELTG 532
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
10-245 |
5.32e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTaGRTMIRLYKPTEGQILFKGQD-ISNls 88
Cdd:NF000106 14 VEVRGLVKHF-----------GEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TwCAN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 eeklRKSVRKNIqmvfqdpfaslNPRKTLRSIIKEPFN-THNMYTM--------RERNEKVEELLARVGLHPSfAGRYPH 159
Cdd:NF000106 80 ----RRALRRTI-----------G*HRPVR*GRRESFSgRENLYMIgr*ldlsrKDARARADELLERFSLTEA-AGRAAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 160 EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLF---------ISHDLSVVrhisDR 230
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTtqymeeaeqLAHELTVI----DR 219
|
250
....*....|....*
gi 2181075557 231 VGVMYLGKMMELTGK 245
Cdd:NF000106 220 GRVIADGKVDELKTK 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-234 |
1.19e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 11 ELRDVKKYFPirsglfqRKVGDV----KAVDG------VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFK 80
Cdd:PRK11288 241 EIGDIYGYRP-------RPLGEVrlrlDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 81 GQDISNLSEeklRKSVRKNIQMVFQDpfaslnpRKT-----LRSIiKEPFNT----HNMYTMRERNEKVEELLARVGLHp 151
Cdd:PRK11288 314 GKPIDIRSP---RDAIRAGIMLCPED-------RKAegiipVHSV-ADNINIsarrHHLRAGCLINNRWEAENADRFIR- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 152 SFAGRYPH------EFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVR 225
Cdd:PRK11288 382 SLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVL 460
|
....*....
gi 2181075557 226 HISDRVGVM 234
Cdd:PRK11288 461 GVADRIVVM 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
35-241 |
1.30e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGqDISNLSEEklrksvrkniqmvfqdpfASLNPR 114
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAIS------------------AGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 KTLRSIIKepfntHNMYTMRERNEKVEELLARVgLHPSFAGRYPHE----FSGGQRQRIGIARALTLNPELIIADEPVSA 190
Cdd:PRK13546 100 LTGIENIE-----FKMLCMGFKRKEIKAMTPKI-IEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 191 LDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVGVMYLGKMME 241
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-231 |
1.86e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 6 QETILELRDVKKYFPIrsglfQRKVgdvkaVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILF-KGQDI 84
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPP-----KKEI-----LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 85 SNLSEE-KL--RKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPfnTHNMYTMRERNEKVEELLARVGLH--------PSF 153
Cdd:TIGR03719 71 GYLPQEpQLdpTKTVRENVEEGVAEIKDALDRFNEISAKYAEP--DADFDKLAAEQAELQEIIDAADAWdldsqleiAMD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 154 AGRYP------HEFSGGQRQRIGIARALTLNPELIIADEPVSALDvsiqAQVINLMEELQEEFNLTYLFISHDlsvvRHI 227
Cdd:TIGR03719 149 ALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD----RYF 220
|
....
gi 2181075557 228 SDRV 231
Cdd:TIGR03719 221 LDNV 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
43-235 |
2.00e-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: 56.04 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 43 LKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISnlseeklrksvrkniqmvfqdpfasLNPRKTlrsiik 122
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-------------------------YKPQYI------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 123 epfnthnmytmrernekveellarvglhpsfagryphEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINL 202
Cdd:cd03222 71 -------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|...
gi 2181075557 203 MEELQEEFNLTYLFISHDLSVVRHISDRVGVMY 235
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-239 |
6.07e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVkkyfpirSGLFQRKVGDVkavdgvSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISN 86
Cdd:PRK10982 248 EVILEVRNL-------TSLRQPSIRDV------SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 87 -------------LSEEKLRKSVRKNIQMVFQDPFASLNPRKTlrsiikePFNTHNMYTMRERNEKV-EELLARVGLHPS 152
Cdd:PRK10982 315 hnaneainhgfalVTEERRSTGIYAYLDIGFNSLISNIRNYKN-------KVGLLDNSRMKSDTQWViDSMRVKTPGHRT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 153 FAGryphEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTYLFISHDLSVVRHISDRVG 232
Cdd:PRK10982 388 QIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
....*..
gi 2181075557 233 VMYLGKM 239
Cdd:PRK10982 463 VMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-220 |
6.42e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 30 VGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnlseeklrkSVRKNIQMVFQDPF- 108
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCGTKLEVAYFDQHr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 109 ASLNPRKTLRSIIKEPFNThNMYTMRERNekVEELLARVGLHPSFAgRYP-HEFSGGQRQRIGIARaLTLNP-ELIIADE 186
Cdd:PRK11147 392 AELDPEKTVMDNLAEGKQE-VMVNGRPRH--VLGYLQDFLFHPKRA-MTPvKALSGGERNRLLLAR-LFLKPsNLLILDE 466
|
170 180 190
....*....|....*....|....*....|....
gi 2181075557 187 PVSALDVsiqaQVINLMEELQEEFNLTYLFISHD 220
Cdd:PRK11147 467 PTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-311 |
6.47e-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: 57.33 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 35 AVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDI-SNLSeeklrkSVRKNIQMVFQDP--FASL 111
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLD------AVRQSLGMCPQHNilFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 112 NprktlrsiIKEPFNTHNMYTMRERNE---KVEELLARVGLHPSfAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPV 188
Cdd:TIGR01257 1019 T--------VAEHILFYAQLKGRSWEEaqlEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 189 SALDVSIQAQVINLMeeLQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMeLTGKFELYDNPLHpyTQALLSSVpvtR 268
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLY-CSGTPLFLKNCFG--TGFYLTLV---R 1161
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2181075557 269 KRGSVKRERivlKGELPSPANPPKGcvFHTRCPV-AKPICKEQI 311
Cdd:TIGR01257 1162 KMKNIQSQR---GGCEGTCSCTSKG--FSTRCPArVDEITPEQV 1200
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-231 |
6.94e-09 |
|
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: 53.92 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 45 KGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFkgqdisnlseeklrksvrkniqmvfqdpfasLNPRKTLRSiikep 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------------------------------IDGEDILEE----- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 125 fnthnmytmrernekveellARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVI---- 200
Cdd:smart00382 45 --------------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLllee 104
|
170 180 190
....*....|....*....|....*....|....*..
gi 2181075557 201 -NLMEELQEEFNLTYLFISHDLSV-----VRHISDRV 231
Cdd:smart00382 105 lRLLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRR 141
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-231 |
9.86e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 9 ILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnls 88
Cdd:TIGR03719 322 VIEAENLTKAF-----------GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI----------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 89 eeklrkSVRKNIQMVFQDPF-ASLNPRKTLRSIIKEPFNTHNM--YTMRER------NEKVEELLARVGlhpsfagryph 159
Cdd:TIGR03719 380 ------EIGETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKLgkREIPSRayvgrfNFKGSDQQKKVG----------- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 160 EFSGGQRQRIGIARALTLNPELIIADEPVSALDV-SIQAqvinlMEELQEEFNLTYLFISHDlsvvRHISDRV 231
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD----RWFLDRI 506
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
36-240 |
1.20e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMI-RLYKPTE-------GQILFKGQDISNLSEEKL---RKSVRKNIQMVF 104
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 105 qdPFASlnprKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPsFAGRYPHEFSGGQRQRIGIARAL--------- 175
Cdd:PRK13547 97 --AFSA----REIVLLGRYPHARRAGALTHRDGEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181075557 176 TLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMM 240
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
162-247 |
3.48e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVIN--LMEELQeefNLTYLFISHDLSVVRHIsDRVGVMYLGKM 239
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELR---GKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
....*...
gi 2181075557 240 MElTGKFE 247
Cdd:PLN03130 818 KE-EGTYE 824
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-106 |
4.52e-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: 54.42 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSG--LFQrkVGDVkavdgvSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDIsnl 87
Cdd:COG4615 328 LELRGVTYRYPGEDGdeGFT--LGPI------DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV--- 396
|
90
....*....|....*....
gi 2181075557 88 sEEKLRKSVRKNIQMVFQD 106
Cdd:COG4615 397 -TADNREAYRQLFSAVFSD 414
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-199 |
5.49e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdISNLSEEK--LRKSVRKNIQM-VFQDPFaslnprk 115
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSwiMPGTIKDNIIFgLSYDEY------- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 116 TLRSIIKEPFNTHNMYTMRERNEKVeelLARVGLhpsfagryphEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSI 195
Cdd:TIGR01271 517 RYTSVIKACQLEEDIALFPEKDKTV---LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
....
gi 2181075557 196 QAQV 199
Cdd:TIGR01271 584 EKEI 587
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-246 |
6.48e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 7 ETILELRDVKKYFPIRSglfQRKVgdvkaVDGVSFSLKKGETLGIVGESGcgkstAGRTMI------RLY-KPTEGQILF 79
Cdd:NF040905 255 EVVFEVKNWTVYHPLHP---ERKV-----VDDVSLNVRRGEIVGIAGLMG-----AGRTELamsvfgRSYgRNISGTVFK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 80 KGQ--DISNLSE----------EKlRK--------SVRKNIQMvfqdpfASLnPRKTLRSIIkepfNTHNMYTMRER--- 136
Cdd:NF040905 322 DGKevDVSTVSDaidaglayvtED-RKgyglnlidDIKRNITL------ANL-GKVSRRGVI----DENEEIKVAEEyrk 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 137 --NEKVEELLARVGlhpsfagryphEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEfNLTY 214
Cdd:NF040905 390 kmNIKTPSVFQKVG-----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGV 457
|
250 260 270
....*....|....*....|....*....|..
gi 2181075557 215 LFISHDLSVVRHISDRVGVMYLGKmmeLTGKF 246
Cdd:NF040905 458 IVISSELPELLGMCDRIYVMNEGR---ITGEL 486
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
36-239 |
1.56e-07 |
|
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: 51.11 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKST---AGRTMIRLYKPTEGQILFKGQDIsnlseeklrksvrkniqmvfqDPFASLN 112
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPY---------------------KEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 PRktlrSIIKEPFNTHNMYTMrerneKVEELLarvglhpSFAGR-----YPHEFSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:cd03233 82 PG----EIIYVSEEDVHFPTL-----TVRETL-------DFALRckgneFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181075557 188 VSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSV-VRHISDRVGVMYLGKM 239
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQ 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
43-196 |
1.66e-07 |
|
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: 51.45 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 43 LKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLrksvRKNIQMVFQDPFA-------SLNP-R 114
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQDPILfsgsirfNLDPeC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 115 KTLRSIIKEPFNTHNMYTMrernekVEELLARVGLHPSFAGrypHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVS 194
Cdd:cd03288 120 KCTDDRLWEALEIAQLKNM------VKSLPGGLDAVVTEGG---ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
..
gi 2181075557 195 IQ 196
Cdd:cd03288 191 TE 192
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
39-199 |
3.16e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQdISNLSEEK--LRKSVRKNIQmvfqdpFASLNPRKT 116
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSwiMPGTIKENII------FGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 117 LRSIIKEPFNTHNMYTMRERNEKVeelLARVGLhpsfagryphEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQ 196
Cdd:cd03291 129 YKSVVKACQLEEDITKFPEKDNTV---LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
...
gi 2181075557 197 AQV 199
Cdd:cd03291 196 KEI 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-246 |
4.77e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTagrtMIRLYK------------PTEGQILFKGQDISNLSEEKLRKSV---RKNI 100
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKST----LLALLKneisadggsytfPGNWQLAWVNQETPALPQPALEYVIdgdREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 101 QMvfQDPFASLNPRKTLRSI--IKEPFNTHNMYTMRERnekVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLN 178
Cdd:PRK10636 93 QL--EAQLHDANERNDGHAIatIHGKLDAIDAWTIRSR---AASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181075557 179 PELIIADEPVSALDVSiqaQVINLmEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKF 246
Cdd:PRK10636 168 SDLLLLDEPTNHLDLD---AVIWL-EKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNY 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
36-200 |
6.38e-07 |
|
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: 49.85 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 36 VDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKpTEGQILFKGQDISNLSEEKLRKSVRKNIQMV--FQDPFaslnp 113
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVfiFSGTF----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 114 RKTLrsiikEPFNTHNmytmrerNEKVEELLARVGLHpSFAGRYPHE-----------FSGGQRQRIGIARALTLNPELI 182
Cdd:cd03289 94 RKNL-----DPYGKWS-------DEEIWKVAEEVGLK-SVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKIL 160
|
170
....*....|....*...
gi 2181075557 183 IADEPVSALDvSIQAQVI 200
Cdd:cd03289 161 LLDEPSAHLD-PITYQVI 177
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-193 |
8.32e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 21 IRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIrLYK----PTEGQIL-----FKGQDISNL---- 87
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAidgiPKNCQILhveqeVVGDDTTALqcvl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 88 -SEEKLRKSVRKNIQMVFQD-----PFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVE---------ELLARVGLHPS 152
Cdd:PLN03073 257 nTDIERTQLLEEEAQLVAQQrelefETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDaytaearaaSILAGLSFTPE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2181075557 153 FAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV 193
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-219 |
1.06e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKpTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFqdpfaslnprkTLR 118
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVF-----------IFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 119 SIIKEPFNTHNMYTMRERNEKVEEllarVGLHpSFAGRYPHE-----------FSGGQRQRIGIARALTLNPELIIADEP 187
Cdd:TIGR01271 1306 GTFRKNLDPYEQWSDEEIWKVAEE----VGLK-SVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190
....*....|....*....|....*....|...
gi 2181075557 188 VSALDvSIQAQVINlmEELQEEF-NLTYLFISH 219
Cdd:TIGR01271 1381 SAHLD-PVTLQIIR--KTLKQSFsNCTVILSEH 1410
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
162-207 |
1.58e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.58e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2181075557 162 SGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVIN--LMEELQ 207
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK 789
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-231 |
6.42e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 8 TILELRDVKKYFpirsglfqrkvGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnl 87
Cdd:PRK11819 323 KVIEAENLSKSF-----------GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI---------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 88 seeKLRKSVrkniQMVFQDPF-ASLNPRKTLRSIIKEPFNTHNM--YTMRER------NEKVEELLARVGlhpsfagryp 158
Cdd:PRK11819 382 ---KIGETV----KLAYVDQSrDALDPNKTVWEEISGGLDIIKVgnREIPSRayvgrfNFKGGDQQKKVG---------- 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181075557 159 hEFSGGQRQRIGIARALTLNPELIIADEPVSALDV-SIQAqvinlMEELQEEFNLTYLFISHDlsvvRHISDRV 231
Cdd:PRK11819 445 -VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLRA-----LEEALLEFPGCAVVISHD----RWFLDRI 508
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-249 |
1.62e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 31 GDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQI-LFKGQDISNLSEEKLrKSVRkniqmvfqdpfA 109
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQL-EFLR-----------A 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 110 SLNPRKTLRSIIKepfnthnmytmRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVS 189
Cdd:PRK10636 391 DESPLQHLARLAP-----------QELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 190 ALDVSI-QAqvinLMEELQeEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKFELY 249
Cdd:PRK10636 460 HLDLDMrQA----LTEALI-DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
33-231 |
1.79e-05 |
|
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: 44.62 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 33 VKAVDGVSFSLKKGETLGIVGESGCGKSTagrtmirlykptegqILFKGqdisnlSEEKLRKSVRKNIQMVFQDPFASLn 112
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEG------LYASGKARLISFLPKFSRNKLIFI- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 113 prKTLRSIIKepfnthnmytmrernekveellarVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPE--LIIADEPVSA 190
Cdd:cd03238 66 --DQLQFLID------------------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2181075557 191 LDVSIQAQVINLMEELQEEFNlTYLFISHDLSVVRHiSDRV 231
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSS-ADWI 158
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
139-219 |
2.84e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 139 KVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFIS 218
Cdd:PRK10938 380 LAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVS 459
|
.
gi 2181075557 219 H 219
Cdd:PRK10938 460 H 460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-249 |
3.43e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 10 LELRDVKKYFPIRSgLFQrkvgdvkavdGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQIlfkgqdisnlse 89
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFK----------NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 90 eklRKSVRKNIQMVFQDPFASLNPRKTLrsiikepfnthnMYTMRE-RNEKVEELLARvglhpSFAGRY----------P 158
Cdd:PRK15064 377 ---KWSENANIGYYAQDHAYDFENDLTL------------FDWMSQwRQEGDDEQAVR-----GTLGRLlfsqddikksV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 159 HEFSGGQRQRIGIARALTLNPELIIADEPVSALDV-SIQAQVINLmeelqEEFNLTYLFISHDLSVVRHISDRVGVMYLG 237
Cdd:PRK15064 437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIESLNMAL-----EKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
250
....*....|..
gi 2181075557 238 KMMELTGKFELY 249
Cdd:PRK15064 512 GVVDFSGTYEEY 523
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-238 |
5.16e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 27 QRKVGDVKAVDGVsfsLKKGETLGIVGESGCGKST-----AGRTmIRLYKPTEGQILFKGqdisnLSEEKLRKSVRKNIQ 101
Cdd:TIGR00956 71 TKTFDILKPMDGL---IKPGELTVVLGRPGSGCSTllktiASNT-DGFHIGVEGVITYDG-----ITPEEIKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 102 MVFQDP--FASLNPRKTLRSII--KEPFNTHNMYTMRERNEKVEELLARV-GLHPSFAGRYPHEF----SGGQRQRIGIA 172
Cdd:TIGR00956 142 YNAETDvhFPHLTVGETLDFAArcKTPQNRPDGVSREEYAKHIADVYMATyGLSHTRNTKVGNDFvrgvSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181075557 173 RALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSV-VRHISDRVGVMYLGK 238
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGY 288
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
39-200 |
8.55e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 39 VSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKgQDISNLSEEK--LRKSVRKNIqmVFQDPFASLNPRKT 116
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAwiMNATVRGNI--LFFDEEDAARLADA 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 117 LRsiikepfnthnmytmrernekVEELLARV-----GLHPSFaGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSAL 191
Cdd:PTZ00243 756 VR---------------------VSQLEADLaqlggGLETEI-GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
....*....
gi 2181075557 192 DVSIQAQVI 200
Cdd:PTZ00243 814 DAHVGERVV 822
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
138-253 |
1.84e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 138 EKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDV-SIQAQVINLMeelqeEFNLTYLF 216
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLV-----LFQGGVLM 679
|
90 100 110
....*....|....*....|....*....|....*..
gi 2181075557 217 ISHDLSVVRHISDRVGVMYLGKMMELTGKFELYDNPL 253
Cdd:PLN03073 680 VSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTL 716
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-200 |
1.89e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 14 DVKKYFPIRSGLFQRKVGD--VKAVDGVSFSLKKGETLGIVGESGCGKST-----AGRTM-------IRLYKPTEGQILF 79
Cdd:PLN03140 872 DVNYFVDMPAEMKEQGVTEdrLQLLREVTGAFRPGVLTALMGVSGAGKTTlmdvlAGRKTggyiegdIRISGFPKKQETF 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181075557 80 KgqDISNLSEE--------------------KLRKSVRKNIQMVFQDPFASLNPRKTLRSIIkepfnthnmytmrernek 139
Cdd:PLN03140 952 A--RISGYCEQndihspqvtvresliysaflRLPKEVSKEEKMMFVDEVMELVELDNLKDAI------------------ 1011
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181075557 140 veellarVGLhPSFAGrypheFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVI 200
Cdd:PLN03140 1012 -------VGL-PGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
168-229 |
2.65e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181075557 168 RIGIARALTLNPELIIADEPVSALDVSiqaqVINLMEELQEEFNLTYLFISHDL----SVVRHISD 229
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDIN----TIRWLEDVLNERNSTMIIISHDRhflnSVCTHMAD 224
|
|
|