|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-265 |
6.94e-172 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 479.23 E-value: 6.94e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVG------KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSK 75
Cdd:COG4608 9 EVRDLKKHFPVRgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 76 AQKqRFRRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKnDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRI 155
Cdd:COG4608 89 ELR-PLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLAS-KAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIY 235
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
250 260 270
....*....|....*....|....*....|
gi 2784741926 236 AHPLHDYTASLLSAVPVPDPeyERARQQIP 265
Cdd:COG4608 247 ARPLHPYTQALLSAVPVPDP--ERRRERIV 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-256 |
9.79e-145 |
|
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: 417.38 E-value: 9.79e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:COG1123 262 EVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL-SRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAkNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:COG1123 341 RRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLL-SRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
250
....*....|....*
gi 2784741926 242 YTASLLSAVPVPDPE 256
Cdd:COG1123 500 YTRALLAAVPSLDPA 514
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-265 |
3.30e-142 |
|
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: 403.66 E-value: 3.30e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEP---TSGKIIFKGEDVSKLrSKAQK 78
Cdd:COG0444 3 EVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL-SEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 79 QRFR-RDMQMIFQDPYASLNPRMKVKDIVAEGIDInHLAKNDADRTKQVEDLLETVGLN--KDHSSRYPHEFSGGQRQRI 155
Cdd:COG0444 81 RKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRI-HGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIY 235
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270
....*....|....*....|....*....|
gi 2784741926 236 AHPLHDYTASLLSAVPVPDPEYERaRQQIP 265
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRR-LIPIP 268
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-254 |
7.91e-132 |
|
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: 385.19 E-value: 7.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGK------ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLyEPTSGKIIFKGEDVSKLRS 74
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 75 KAQkQRFRRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQR 154
Cdd:COG4172 355 RAL-RPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250 260
....*....|....*....|
gi 2784741926 235 YAHPLHDYTASLLSAVPVPD 254
Cdd:COG4172 514 FDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-262 |
1.94e-121 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 351.32 E-value: 1.94e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNV--------GKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKL 72
Cdd:PRK15079 9 LEVADLKVHFDIkdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 73 rSKAQKQRFRRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQR 152
Cdd:PRK15079 89 -KDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 153 QRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSD 232
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270
....*....|....*....|....*....|
gi 2784741926 233 EIYAHPLHDYTASLLSAVPVPDPEYERARQ 262
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLERNKT 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-229 |
6.51e-119 |
|
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: 341.02 E-value: 6.51e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRf 81
Cdd:cd03257 3 EVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIA 229
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-260 |
7.69e-111 |
|
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: 321.37 E-value: 7.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrF 81
Cdd:COG1124 3 EVRNLSVSYGQG-GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAkndaDRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:COG1124 78 RRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP----DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|....*....
gi 2784741926 242 YTASLLSAVpvpdPEYERA 260
Cdd:COG1124 234 YTRELLAAS----LAFERA 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-261 |
1.33e-103 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 306.12 E-value: 1.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 6 LKQYFNV-----GKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQR 80
Cdd:PRK11308 11 LKKHYPVkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 fRRDMQMIFQDPYASLNPRMKVKDIVAEGIDIN-HLAKndADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIAR 159
Cdd:PRK11308 91 -RQKIQIVFQNPYGSLNPRKKVGQILEEPLLINtSLSA--AERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPL 239
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
250 260
....*....|....*....|..
gi 2784741926 240 HDYTASLLSAVPVPDPEYERAR 261
Cdd:PRK11308 248 HPYTQALLSATPRLNPDDRRER 269
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-255 |
6.78e-89 |
|
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: 275.02 E-value: 6.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEP----TSGKIIFKGEDVSKLrSKA 76
Cdd:COG4172 7 LSVEDLSVAFGQG-GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGL-SER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQRFR-RDMQMIFQDPYASLNPRMKVKDIVAEGIDInHLAKNDADRTKQVEDLLETVGLNKDHS--SRYPHEFSGGQRQ 153
Cdd:COG4172 85 ELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRL-HRGLSGAAARARALELLERVGIPDPERrlDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260
....*....|....*....|..
gi 2784741926 234 IYAHPLHDYTASLLSAVPVPDP 255
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPRGDP 265
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-288 |
9.16e-88 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 274.81 E-value: 9.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRFRRDMQMIFQDPYASL 96
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL-SPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 NPRMKVKDIVAEGIDINHLAKNDADRtKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISA 176
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAA-ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 177 LDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPVPDPE 256
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPS 573
|
250 260 270
....*....|....*....|....*....|....*...
gi 2784741926 257 YERARQQIPYD--PS----REFDGKPRQLVEIVPHHWV 288
Cdd:PRK10261 574 RQRPQRVLLSDdlPSnihlRGEEVAAVSLQCVGPGHYV 611
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-249 |
1.03e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 242.82 E-value: 1.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGK----ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEdvsKLRSKAQ 77
Cdd:COG4167 6 EVRNLSKTFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 78 KQRFRRdMQMIFQDPYASLNPRMKVKDIVAEGIDIN-HLakNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIG 156
Cdd:COG4167 83 KYRCKH-IRMIFQDPNTSLNPRLNIGQILEEPLRLNtDL--TAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|...
gi 2784741926 237 HPLHDYTASLLSA 249
Cdd:COG4167 240 NPQHEVTKRLIES 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-248 |
7.34e-77 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 243.84 E-value: 7.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKA------DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYePTSGKIIFKGEDVSKLRS 74
Cdd:PRK15134 276 LDVEQLQVAFPIRKGilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 75 KaQKQRFRRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQR 154
Cdd:PRK15134 355 R-QLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
250
....*....|....
gi 2784741926 235 YAHPLHDYTASLLS 248
Cdd:PRK15134 514 FAAPQQEYTRQLLA 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-283 |
3.31e-73 |
|
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: 234.03 E-value: 3.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPT---SGKIIFKGEDVSKLRSKAQk 78
Cdd:COG1123 6 EVRDLSVRY---PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 79 qrfRRDMQMIFQDPYASLNPrMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIA 158
Cdd:COG1123 82 ---GRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSR--AEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 239 lhdytaSLLSAVPVPDPEYERARQQIPYDP--------SREFDGKPRQLVEIV 283
Cdd:COG1123 235 ------QALAAVPRLGAARGRAAPAAAAAEpllevrnlSKRYPVRGKGGVRAV 281
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-258 |
4.82e-72 |
|
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: 223.53 E-value: 4.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 12 VGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRsKAQKQRFRRDMQMIFQD 91
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD-RKQRRAFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 PYASLNPRMKVKDIVAEGIDiNHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:TIGR02769 97 SPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLE--IASSDEIYAHPL-HDYTASLLS 248
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEecDVAQLLSFKHPAgRNLQSAVLP 255
|
250
....*....|
gi 2784741926 249 AVPVPDPEYE 258
Cdd:TIGR02769 256 EHPVRRSITT 265
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-247 |
2.94e-70 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 221.51 E-value: 2.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHL-KQYfnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqr 80
Cdd:COG3842 7 ELENVsKRY------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:COG3842 75 EKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGVPK--AEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHD----LSMvkyiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVGTPEEIYE 225
|
250
....*....|.
gi 2784741926 237 HPLHDYTASLL 247
Cdd:COG3842 226 RPATRFVADFI 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-262 |
1.21e-69 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 217.25 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 12 VGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRFRRDMQMIFQD 91
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL-NRAQRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 PYASLNPRMKVKDIVAEgiDINHLAK-NDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIA 170
Cdd:PRK10419 98 SISAVNPRKTVREIIRE--PLRHLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 171 DEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEiassDEIYAHPL---HDYTASLL 247
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE----TQPVGDKLtfsSPAGRVLQ 251
|
250
....*....|....*
gi 2784741926 248 SAVPVPDPEYERARQ 262
Cdd:PRK10419 252 NAVLPAFPVRRRTTE 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-268 |
1.61e-67 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 213.82 E-value: 1.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADeVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEP---TSGKIIFKGEDVSKLRSKaQ 77
Cdd:PRK09473 13 LDVKDLRVTFSTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEK-E 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 78 KQRFR-RDMQMIFQDPYASLNPRMKVKDIVAEGIDIN-HLAKNDAdrtkqVED---LLETVGL--NKDHSSRYPHEFSGG 150
Cdd:PRK09473 91 LNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEA-----FEEsvrMLDAVKMpeARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 151 QRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIAS 230
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 2784741926 231 SDEIYAHPLHDYTASLLSAVPVPDPEYErARQQIPYDP 268
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLDAEGE-SLLTIPGNP 282
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-270 |
7.11e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 212.63 E-value: 7.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:COG1135 3 ELENLSKTFPTKGG-PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAL-SERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpyASLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:COG1135 81 RRKIGMIFQH--FNLLSSRTVAENVALPLEIAGVPK--AEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250 260 270
....*....|....*....|....*....|
gi 2784741926 242 YTASLLSAVPVPD-PEYERARQQIPYDPSR 270
Cdd:COG1135 236 LTRRFLPTVLNDElPEELLARLREAAGGGR 265
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-238 |
1.07e-65 |
|
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: 205.89 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:cd03258 3 ELKNVSKVFG-DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL-SGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpYASLNPRmKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSR-TVFENVALPLEIAGVPK--AEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-252 |
2.61e-62 |
|
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: 198.64 E-value: 2.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 14 KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDpy 93
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:cd03294 111 FALLPHRTVLENVAFGLEVQGVPR--AEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 174 ISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPV 252
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDR 266
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-251 |
3.42e-62 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 199.97 E-value: 3.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYE-P---TSGKIIFKGEDVSKLRSKA 76
Cdd:PRK11022 4 LNVDKLSVHFGDESA-PFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQRFRRDMQMIFQDPYASLNPRMKVKDIVAEGIDInHLAKNDADRTKQVEDLLETVGLnKDHSSR---YPHEFSGGQRQ 153
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKV-HQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*...
gi 2784741926 234 IYAHPLHDYTASLLSAVP 251
Cdd:PRK11022 241 IFRAPRHPYTQALLRALP 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-256 |
1.95e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 198.39 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgKADEVR-AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYePT------SGKIIFKGEDVskLR 73
Cdd:PRK15134 6 LAIENLSVAFR--QQQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESL--LH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 74 SKAQKQRFRR--DMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKNDADRTkQVEDLLETVGLN--KDHSSRYPHEFSG 149
Cdd:PRK15134 81 ASEQTLRGVRgnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARG-EILNCLDRVGIRqaAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 150 GQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIA 229
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|....*..
gi 2784741926 230 SSDEIYAHPLHDYTASLLSAVPVPDPE 256
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-249 |
4.44e-59 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 190.00 E-value: 4.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYF----NVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKA 76
Cdd:PRK15112 5 LEVRNLSKTFryrtGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQRFRrdmqMIFQDPYASLNPRMKVKDIVAEGIDINhLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIG 156
Cdd:PRK15112 85 RSQRIR----MIFQDPSTSLNPRQRISQILDFPLRLN-TDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|...
gi 2784741926 237 HPLHDYTASLLSA 249
Cdd:PRK15112 240 SPLHELTKRLIAG 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-268 |
5.47e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 192.32 E-value: 5.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:PRK11153 3 ELKNISKVFPQGGR-TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAL-SEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpYASLNPRmKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:PRK11153 81 RRQIGMIFQH-FNLLSSR-TVFDNVALPLELAGTPK--AEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
250 260
....*....|....*....|....*...
gi 2784741926 242 YTASLLSAV-PVPDPEYERARQQIPYDP 268
Cdd:PRK11153 236 LTREFIQSTlHLDLPEDYLARLQAEPTT 263
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-251 |
1.58e-58 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 190.89 E-value: 1.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEP----TSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDPY 93
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASLNPRMKVKDIVAEGIDI----NHLAKNDADRTKQVEDLLETVGLnKDHS---SRYPHEFSGGQRQRIGIARALAVQPE 166
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIPSwtfkGKWWQRFKWRKKRAIELLHRVGI-KDHKdimNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASL 246
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKAL 258
|
....*
gi 2784741926 247 LSAVP 251
Cdd:COG4170 259 LRSMP 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-247 |
7.47e-58 |
|
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: 185.90 E-value: 7.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqrF 81
Cdd:cd03300 2 ELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:cd03300 71 KRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKLPKAEIKE--RVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
....*.
gi 2784741926 242 YTASLL 247
Cdd:cd03300 226 FVADFI 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-247 |
4.10e-57 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 186.45 E-value: 4.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGK--ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMI 88
Cdd:COG1125 6 NVTKryPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDL----DPVELRRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 89 FQDpyASLNPRMKVKDIVAEgidINHLAKNDADRTKQ-VEDLLETVGLN-KDHSSRYPHEFSGGQRQRIGIARALAVQPE 166
Cdd:COG1125 82 IQQ--IGLFPHMTVAENIAT---VPRLLGWDKERIRArVDELLELVGLDpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLS-MVKyISDRIGVMHYGRMLEIASSDEIYAHPLHDYTAS 245
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDeALK-LGDRIAVMREGRIVQYDTPEEILANPANDFVAD 235
|
..
gi 2784741926 246 LL 247
Cdd:COG1125 236 FV 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-224 |
7.37e-57 |
|
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: 182.69 E-value: 7.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:cd03255 2 ELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL-SEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRD-MQMIFQDPYasLNPRMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:cd03255 80 RRRhIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKERRE--RAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGR 224
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-286 |
9.79e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 186.51 E-value: 9.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsKLRSKAQKqrf 81
Cdd:COG1118 4 EVRNISKRF-----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 rRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:COG1118 75 -RRVGFVFQH-YA-LFPHMTVAENIAFGLRVRPPSK--AEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2784741926 242 YTASLLSAVPVPDPEYERARQQIPYDPSREFDGKPRQLVEIV--PHH 286
Cdd:COG1118 229 FVARFLGCVNVLRGRVIGGQLEADGLTLPVAEPLPDGPAVAGvrPHD 275
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-249 |
1.32e-56 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 182.89 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKAdevrAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRF 81
Cdd:cd03295 2 EFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ----DPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpyASLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLNKDH-SSRYPHEFSGGQRQRIGIARA 160
Cdd:cd03295 74 RRKIGYVIQQ--IGLFPHMTVEENIALVPKLLKWPK--EKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLH 240
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*....
gi 2784741926 241 DYTASLLSA 249
Cdd:cd03295 230 DFVAEFVGA 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-229 |
1.53e-56 |
|
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: 181.95 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrfRRDMQMIF 89
Cdd:cd03259 5 GLSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE------RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDPyaSLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKLRGVPK--AEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIA 229
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-251 |
6.10e-56 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 191.22 E-value: 6.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIF-------KGEDVSKLR--SKAQKQRFR-RDMQ 86
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrRSRQVIELSeqSAAQMRHVRgADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 87 MIFQDPYASLNPRMKVKDIVAEGIDInHLAKNDADRTKQVEDLLETVGLNKDHS--SRYPHEFSGGQRQRIGIARALAVQ 164
Cdd:PRK10261 108 MIFQEPMTSLNPVFTVGEQIAESIRL-HQGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 165 PEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTA 244
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
....*..
gi 2784741926 245 SLLSAVP 251
Cdd:PRK10261 267 ALLAAVP 273
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-242 |
9.08e-56 |
|
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: 180.56 E-value: 9.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:COG1127 7 EVRNLTKSFG-----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL-SEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDP--YASLNprmkVKDIVA----EgidinHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRI 155
Cdd:COG1127 81 RRRIGMLFQGGalFDSLT----VFENVAfplrE-----HTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIY 235
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
250
....*....|
gi 2784741926 236 A--HP-LHDY 242
Cdd:COG1127 231 AsdDPwVRQF 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-220 |
1.32e-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: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHL-KQYFNVGKAdeVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrskaqkQ 79
Cdd:cd03293 1 LEVRNVsKTYGGGGGA--VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---------T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 RFRRDMQMIFQDPyaSLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIAR 159
Cdd:cd03293 70 GPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPK--AEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVM 220
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-247 |
2.65e-55 |
|
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: 179.46 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqr 80
Cdd:cd03296 3 IEVRNVSKRFG-----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 fRRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHLAK--NDADRTKQVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIA 158
Cdd:cd03296 73 -ERNVGFVFQH-YA-LFRHMTVFDNVAFGLRVKPRSErpPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....*....
gi 2784741926 239 LHDYTASLL 247
Cdd:cd03296 229 ASPFVYSFL 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-238 |
1.08e-54 |
|
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: 177.69 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:cd03261 2 ELRGLTKSF-----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGL-SEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpyASLNPRMKVKDIVA----EgidinHLAKNDADRTKQVEDLLETVGLNKDHsSRYPHEFSGGQRQRIGI 157
Cdd:cd03261 76 RRRMGMLFQS--GALFDSLTVFENVAfplrE-----HTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
.
gi 2784741926 238 P 238
Cdd:cd03261 228 D 228
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-252 |
1.88e-54 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 177.30 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrfRRDMQMIFQDpYAsLNPR 99
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR------DRKIGFVFQH-YA-LFKH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIDInhLAKNDADRTKQVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:TIGR00968 87 LTVRDNIAFGLEI--RKHPKAKIKARVEELLELVQLEG-LGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 180 SIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPV 252
Cdd:TIGR00968 164 KVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-227 |
2.41e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 176.39 E-value: 2.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTtgraIIH----LYEPTSGKIIFKGEDVSKLrSKA 76
Cdd:COG1136 5 LELRNLTKSYGTGEG-EVTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNilggLDRPTSGEVLIDGQDISSL-SER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQRFRRD-MQMIFQDPYasLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRI 155
Cdd:COG1136 79 ELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVSR--KERRERARELLERVGL-GDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLE 227
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-247 |
3.24e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 180.27 E-value: 3.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrfRRDMQMIF 89
Cdd:COG3839 8 NVSKSyGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK------DRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDpYAsLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:COG3839 82 QS-YA-LYPHMTVYENIAFPLKLRKVPK--AEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHD----LSMvkyiSDRIGVMHYGRMLEIASSDEIYAHPLHDYTAS 245
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPANLFVAG 232
|
..
gi 2784741926 246 LL 247
Cdd:COG3839 233 FI 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-250 |
3.53e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 176.72 E-value: 3.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklRSKAQKQRF 81
Cdd:COG1126 3 EIENLHKSF-----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQdpyaSLN--PRMKVKDIVAEG-IDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIA 158
Cdd:COG1126 76 RRKVGMVFQ----QFNlfPHLTVLENVTLApIKVKKMSKAEA--EERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|..
gi 2784741926 239 LHDYTASLLSAV 250
Cdd:COG1126 228 QHERTRAFLSKV 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-242 |
8.56e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.64 E-value: 8.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHL-KQYfnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqr 80
Cdd:COG1131 2 EVRGLtKRY------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 fRRDMQMIFQDPyaSLNPRMKVKDIvaegidINHLAK----NDADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIG 156
Cdd:COG1131 72 -RRRIGYVPQEP--ALYPDLTVREN------LRFFARlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
....*.
gi 2784741926 237 HPLHDY 242
Cdd:COG1131 221 RLLEDV 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-228 |
1.05e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 176.05 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRskaqkqrf 81
Cdd:COG1116 9 ELRGVSKRFPTGG-GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 rRDMQMIFQDPyaSLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARAL 161
Cdd:COG1116 80 -PDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPK--AERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 162 AVQPEFIIADEPISALDV----SIQaqvvNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVM--HYGRMLEI 228
Cdd:COG1116 154 ANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-241 |
1.86e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.86 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHL-KQYfnvgkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqKQR 80
Cdd:COG3638 4 ELRNLsKRY-----PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRA-LRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYasLNPRMKVKDIVAEGidinHLAK-----------NDADRTKqVEDLLETVGLnKDHSSRYPHEFSG 149
Cdd:COG3638 78 LRRRIGMIFQQFN--LVPRLSVLTNVLAG----RLGRtstwrsllglfPPEDRER-ALEALERVGL-ADKAYQRADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 150 GQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM---- 225
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVvfdg 229
|
250 260
....*....|....*....|
gi 2784741926 226 ----LEIASSDEIYAHPLHD 241
Cdd:COG3638 230 ppaeLTDAVLREIYGGEAEE 249
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-229 |
2.13e-51 |
|
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: 168.59 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqr 80
Cdd:cd03301 1 VELENVTKRF-----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 fRRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIARA 160
Cdd:cd03301 71 -DRDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVPKDEIDE--RVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIA 229
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-238 |
4.01e-50 |
|
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: 165.97 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPYAS 95
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE----LRRKVGLVFQNPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LnprmkVKDIVAEgiDI-----NhLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIA 170
Cdd:COG1122 88 L-----FAPTVEE--DVafgpeN-LGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 171 DEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-224 |
6.73e-50 |
|
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: 163.51 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRskAQKQR 80
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE--DELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPyaSLNPRMKVKDIVAEGIdinhlakndadrtkqvedlletvglnkdhssryphefSGGQRQRIGIARA 160
Cdd:cd03229 74 LRRRIGMVFQDF--ALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-238 |
1.18e-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: 162.22 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqKQRF 81
Cdd:cd03219 2 EVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPyaSLNPRMKVKD--IVA------EGIDINHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQ 153
Cdd:cd03219 74 RLGIGRTFQIP--RLFPELTVLEnvMVAaqartgSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 2784741926 234 IYAHP 238
Cdd:cd03219 230 VRNNP 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-241 |
2.57e-48 |
|
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: 161.58 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKadevRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQrF 81
Cdd:cd03256 2 EVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQ-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPyaSLNPRMKVKDIVAEGIDINH-----LAKN--DADRTKQVEdLLETVGLNKDHSSRyPHEFSGGQRQR 154
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLENVLSGRLGRRstwrsLFGLfpKEEKQRALA-ALERVGLLDKAYQR-ADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
....*..
gi 2784741926 235 YAHPLHD 241
Cdd:cd03256 233 TDEVLDE 239
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-283 |
3.99e-48 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 164.64 E-value: 3.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDpyASLNPR 99
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQ--FALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIDInhLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:TIGR01186 86 MTILQNTSLGPEL--LGWPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 180 SIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPVPDP-EYE 258
Cdd:TIGR01186 163 LIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVfDAE 242
|
250 260
....*....|....*....|....*.
gi 2784741926 259 RARQQIPYDPSREFDGK-PRQLVEIV 283
Cdd:TIGR01186 243 RIAQRMNTGPITKTADKgPRSALQLM 268
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-224 |
5.74e-48 |
|
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: 159.62 E-value: 5.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrSKAQKQRF 81
Cdd:cd03262 2 EIKNLHKSFG-----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD--DKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDpyASLNPRMKVKDIVAEG-IDINHLAKNDADRTkqVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:cd03262 75 RQKVGMVFQQ--FNLFPHLTVLENITLApIKVKGMSKAEAEER--ALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-293 |
8.57e-48 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 162.66 E-value: 8.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 36 LVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskaQKQRFRRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHL 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 116 AKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRE 195
Cdd:TIGR01187 73 PR--AEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 196 RDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPVPD-PEYERARQQIPYDPSREFDG 274
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEaTVIERKSEQVVLAGVEGRRC 229
|
250 260
....*....|....*....|..
gi 2784741926 275 KPRQLVEI---VPHHWVRASED 293
Cdd:TIGR01187 230 DIYTDVPVekdQPLHVVLRPEK 251
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-234 |
1.14e-47 |
|
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: 159.27 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAI-----IHLYEPTSGKIIFKGEDVSKLRSK 75
Cdd:cd03260 1 IELRDLNVYYG-----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 76 AQkqRFRRDMQMIFQDPyaslNP-RMKVKDIVAEGIDInHLAKNDADRTKQVEDLLETVGLNKDHSSR-YPHEFSGGQRQ 153
Cdd:cd03260 76 VL--ELRRRVGMVFQKP----NPfPGSIYDNVAYGLRL-HGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErdLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 2784741926 234 I 234
Cdd:cd03260 227 I 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-224 |
3.55e-47 |
|
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: 157.63 E-value: 3.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLkqYFNVGKADEVrAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqRF 81
Cdd:cd03225 1 ELKNL--SFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK----EL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPYASLnprmkVKDIVAEgiDI----NHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGI 157
Cdd:cd03225 74 RRKVGLVFQNPDDQF-----FGPTVEE--EVafglENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-227 |
8.29e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.44 E-value: 8.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 8 QYFNVGK--ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQkQRFRRDM 85
Cdd:COG2884 3 RFENVSKryPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI-PYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 86 QMIFQDpyASLNPRMKVKDIVAegidinhLA-----KNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:COG2884 82 GVVFQD--FRLLPDRTVYENVA-------LPlrvtgKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIA-HDLSMVKYISDRIGVMHYGRMLE 227
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIAtHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
21-255 |
8.35e-46 |
|
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: 158.62 E-value: 8.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEP--TSGKIIFKGEDVSKLRSkaqkqrFRRDMQMIFQDpYAsLNP 98
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPP------HKRGLALLFQN-YA-LFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:TIGR03258 93 HLKVEDNVAFGLRAQKMPK--ADIAERVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 179 VSIQAQVVNLLKRLQRE-RDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPVPDP 255
Cdd:TIGR03258 170 ANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-251 |
8.78e-46 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 157.66 E-value: 8.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHL----YEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDPY 93
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASLNPRMKVKDIVAEGID----INHLAKNDADRTKQVEDLLETVGLnKDHS---SRYPHEFSGGQRQRIGIARALAVQPE 166
Cdd:PRK15093 100 SCLDPSERVGRQLMQNIPgwtyKGRWWQRFGWRKRRAIELLHRVGI-KDHKdamRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASL 246
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQAL 258
|
....*
gi 2784741926 247 LSAVP 251
Cdd:PRK15093 259 IRAIP 263
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-249 |
1.23e-45 |
|
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: 154.42 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrfRRDMQMIFQDpYAsLNPRM 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISYVPQN-YA-LFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAEGIdiNHLAKNDADRTKQVEDLLETVGLnkDHS-SRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:cd03299 87 TVYKNIAYGL--KKRKVDKKEIERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 180 SIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSA 249
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGF 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-250 |
1.85e-45 |
|
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: 154.43 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLkqyfNVGkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqr 80
Cdd:COG1120 2 LEAENL----SVG-YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLNprMKVKDIVAEGIdINHLAK----NDADRTKqVEDLLETVGLnKDHSSRYPHEFSGGQRQRIG 156
Cdd:COG1120 73 LARRIAYVPQEPPAPFG--LTVRELVALGR-YPHLGLfgrpSAEDREA-VEEALERTGL-EHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIya 236
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV-- 225
|
250
....*....|....
gi 2784741926 237 hplhdYTASLLSAV 250
Cdd:COG1120 226 -----LTPELLEEV 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-241 |
1.88e-45 |
|
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: 154.25 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrf 81
Cdd:COG4555 3 EVENLSKKYG-----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPYasLNPRMKVKDIVAEGIDINHLakNDADRTKQVEDLLETVGLNKDHSSRYpHEFSGGQRQRIGIARAL 161
Cdd:COG4555 73 RRQIGVLPDERG--LYDRLTVRENIRYFAELYGL--FDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHD 241
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-173 |
1.92e-45 |
|
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: 151.26 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPyaSLNPRM 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS----LRKEIGYVFQDP--QLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 101 KVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGL---NKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDA--RAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-238 |
4.64e-45 |
|
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: 153.66 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTT-----TGraiihLYEPTSGKIIFKGEDVSKLRSKa 76
Cdd:COG0411 6 EVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTlfnliTG-----FYRPTSGRILFDGRDITGLPPH- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 qkQRFRRDMQMIFQDPyaSLNPRMKVKD-------------IVAEGIDINHLAKNDADRTKQVEDLLETVGLnKDHSSRY 143
Cdd:COG0411 75 --RIARLGIARTFQNP--RLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGL-ADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 144 PHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYG 223
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250
....*....|....*
gi 2784741926 224 RMLEIASSDEIYAHP 238
Cdd:COG0411 230 RVIAEGTPAEVRADP 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-252 |
9.97e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 156.15 E-value: 9.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqr 80
Cdd:PRK11607 20 LEIRNLTKSF-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpYAsLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:PRK11607 89 YQRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPK--AEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 161 LAVQPEFIIADEPISALDVSI----QAQVVNLLKRLqrerDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
250
....*....|....*.
gi 2784741926 237 HPLHDYTASLLSAVPV 252
Cdd:PRK11607 240 HPTTRYSAEFIGSVNV 255
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
11-245 |
1.47e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 155.49 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrsKAQKqrfrRDMQMIF 89
Cdd:PRK09452 19 GISKSfDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAEN----RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDpYAsLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:PRK09452 93 QS-YA-LFPHMTVFENVAFGLRMQKTPA--AEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHD----LSMvkyiSDRIGVMHYGRMLEIASSDEIYAHPLHDYTAS 245
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGTPREIYEEPKNLFVAR 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-225 |
7.88e-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: 147.54 E-value: 7.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrf 81
Cdd:cd03230 2 EVRNLSKRY-----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPyaSLNPRMKVKDIVaegidinhlakndadrtkqvedlletvglnkdhssryphEFSGGQRQRIGIARAL 161
Cdd:cd03230 72 KRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-237 |
1.26e-43 |
|
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: 149.37 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKAdevrAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqKQR 80
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ----ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKK-LRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpyASLNPRMKVKDIVAEG---------IDINHLAKNDADRTKQvedLLETVGLNKDHSSRyPHEFSGGQ 151
Cdd:TIGR02315 77 LRRRIGMIFQH--YNLIERLTVLENVLHGrlgykptwrSLLGRFSEEDKERALS---ALERVGLADKAYQR-ADQLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASS 231
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
....*.
gi 2784741926 232 DEIYAH 237
Cdd:TIGR02315 231 SELDDE 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-238 |
3.95e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 151.39 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQR 80
Cdd:PRK10851 3 IEIANIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FrrdmqmIFQDpYAsLNPRMKVKDIVAEGIDI--NHLAKNDADRTKQVEDLLETVGLnkDH-SSRYPHEFSGGQRQRIGI 157
Cdd:PRK10851 78 F------VFQH-YA-LFRHMTVFDNIAFGLTVlpRRERPNAAAIKAKVTQLLEMVQL--AHlADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
.
gi 2784741926 238 P 238
Cdd:PRK10851 228 P 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-252 |
2.43e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 150.57 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDpyASLNPR 99
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:PRK10070 121 MTVLDNTAFGMELAGINA--EERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 180 SIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAVPV 252
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-247 |
3.27e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 148.71 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlRSKAQkqrfrRDMQMIFQDpYAsLNPRM 100
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQ-----RDICMVFQS-YA-LFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:PRK11432 94 SLGENVGYGLKMLGVPK--EERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 181 IQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLL 247
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-238 |
1.05e-40 |
|
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: 142.98 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTtgrAIIH---LYEPTSGKIIFKGEDVSKLRSKAQK 78
Cdd:TIGR04521 2 KLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKST---LIQHlngLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 79 QrFRRDMQMIFQDPYASLnprmkVKDIVAEgiDI-----NhLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQ 153
Cdd:TIGR04521 79 D-LRKKVGLVFQFPEHQL-----FEETVYK--DIafgpkN-LGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
....*
gi 2784741926 234 IYAHP 238
Cdd:TIGR04521 230 VFSDV 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-217 |
1.07e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 140.75 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSK----AQKQRFRRDMqmifqd 91
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyvPQRRSIDRDF------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 pyaslnpRMKVKDIVAEGID--INHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:cd03235 84 -------PISVRDVVLMGLYghKGLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRI 217
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-250 |
4.33e-40 |
|
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: 140.74 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLR----SKAQKQRF-RRDMQMIFQDPYASLn 97
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlSEAERRRLmRTEWGFVHQNPRDGL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 pRMKVK---DIVAEGIDINhlAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:TIGR02323 100 -RMRVSagaNIGERLMAIG--ARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 175 SALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAV 250
Cdd:TIGR02323 177 GGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-250 |
5.08e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 140.45 E-value: 5.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKAdevraVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKL----RSKA 76
Cdd:PRK11701 7 LSVRGLTKLYGPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyaLSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQR-FRRDMQMIFQDPYASLnpRMKV-------KDIVAEGidinhlAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFS 148
Cdd:PRK11701 82 ERRRlLRTEWGFVHQHPRDGL--RMQVsaggnigERLMAVG------ARHYGDIRATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 149 GGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEI 228
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|..
gi 2784741926 229 ASSDEIYAHPLHDYTASLLSAV 250
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-240 |
1.48e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSK----AQKQRFRRDMqmifqd 91
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvPQRAEVDWDF------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 pyaslnPrMKVKDIVAEGID-----INHLAKNDADRtkqVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPE 166
Cdd:COG1121 91 ------P-ITVRDVVLMGRYgrrglFRRPSRADREA---VDEALERVGL-EDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRI-----GVMHYGRMLEIASSD---EIYAHP 238
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVlllnrGLVAHGPPEEVLTPEnlsRAYGGP 238
|
..
gi 2784741926 239 LH 240
Cdd:COG1121 239 VA 240
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-225 |
1.81e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.64 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkQRFRRDMQMIFQDPYAslnPRMK 101
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP----PEWRRQVAYVPQEPAL---WGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEGIDINHLAKNDADrtkqVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSI 181
Cdd:COG4619 90 VRDNLPFPFQLRERKFDRER----ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2784741926 182 QAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:COG4619 166 TRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-224 |
2.06e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.84 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQkqrf 81
Cdd:cd00267 1 EIENLSFRYG-----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQdpyaslnprmkvkdivaegidinhlakndadrtkqvedlletvglnkdhssrypheFSGGQRQRIGIARAL 161
Cdd:cd00267 72 RRRIGYVPQ--------------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-238 |
7.07e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.15 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVskLRSKAQKQRFRRDMQMIFQDPYasLNPRMK 101
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERLIRQEAGMVFQQFY--LFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEG-IDINHLAKNDADrtKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:PRK09493 94 ALENVMFGpLRVRGASKEEAE--KQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 181 IQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK09493 171 LRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-249 |
7.22e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 137.52 E-value: 7.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEP----TSGKIIFKGEDV--SKLRSkaqkqrfrRDMQMIFQDPYA 94
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapCALRG--------RKIATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 SLNPrmkVKDIVAEGIDiNHLAKNDADRTKQVEDLLETVGLNKDHS--SRYPHEFSGGQRQRIGIARALAVQPEFIIADE 172
Cdd:PRK10418 91 AFNP---LHTMHTHARE-TCLALGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 173 PISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSA 249
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-227 |
8.31e-39 |
|
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: 136.33 E-value: 8.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADeVRAVDDITFDVYQGETFGLVGESGSGKTTtgraIIHLY----EPTSGKIIFKGEDVSKLrSKA 76
Cdd:TIGR02211 2 LKCENLGKRYQEGKLD-TRVLKGVSLSIGKGEIVAIVGSSGSGKST----LLHLLggldNPTSGEVLFNGQSLSKL-SSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQRFR-RDMQMIFQdpYASLNPRMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLnKDHSSRYPHEFSGGQRQRI 155
Cdd:TIGR02211 76 ERAKLRnKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKSVKEAKE--RAYEMLEKVGL-EHRINHRPSELSGGERQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYIsDRIGVMHYGRMLE 227
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-227 |
1.61e-38 |
|
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: 135.04 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKqrf 81
Cdd:cd03268 2 KTNDLTKTYG-----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 rrdMQMIFQDPyaSLNPRMKVKD---IVAEGIDINHlakndadrtKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIA 158
Cdd:cd03268 74 ---IGALIEAP--GFYPNLTAREnlrLLARLLGIRK---------KRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLE 227
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-242 |
4.05e-38 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 143.05 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRskaqKQRFRRDMQMIFQDPY-- 93
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID----PASLRRQIGVVLQDVFlf 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 -ASlnprmkvkdiVAEGIdinHLAKNDADRtKQVEDLLETVGLNKD---HSSRYPHE-------FSGGQRQRIGIARALA 162
Cdd:COG2274 562 sGT----------IRENI---TLGDPDATD-EEIIEAARLAGLHDFieaLPMGYDTVvgeggsnLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 163 VQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYGRMLEIASSDEIYAHPLHDY 242
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-226 |
2.65e-37 |
|
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: 131.02 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLkqYFNVGKadeVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrF 81
Cdd:cd03214 1 EVENL--SVGYGG---RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQdpyaslnprmkvkdiVAEGIDINHLAKndadrtKQVEDLletvglnkdhssryphefSGGQRQRIGIARAL 161
Cdd:cd03214 72 ARKIAYVPQ---------------ALELLGLAHLAD------RPFNEL------------------SGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-237 |
2.71e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLK-QYfnvgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGedvsKLRSKAQKQ 79
Cdd:PRK13635 6 IRVEHISfRY----PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG----MVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 RFRRDMQMIFQdpyaslNPRMK-----VKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQR 154
Cdd:PRK13635 78 DVRRQVGMVFQ------NPDNQfvgatVQDDVAFGLENIGVPREEM--VERVDQALRQVGM-EDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
...
gi 2784741926 235 YAH 237
Cdd:PRK13635 228 FKS 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-234 |
3.80e-37 |
|
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: 132.11 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskaQKQR 80
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-----EPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPyaSLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:cd03265 71 VRRRIGIVFQDL--SVDDELTGWENLYIHARLYGVPG--AERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-235 |
1.36e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 132.48 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrSKAQKQR 80
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD--KKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLNPRMKVKDIvAEGIdiNHLAKNDADRTKQVEDLLETVGLNKD-HSSRYPHEFSGGQRQRIGIAR 159
Cdd:PRK13637 81 IRKKVGLVFQYPEYQLFEETIEKDI-AFGP--INLGLSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIY 235
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-229 |
2.07e-36 |
|
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: 129.72 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVyQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDpyASLNPRMKV 102
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDInhlaKNDADRTKQVEDLLETVGLnkDH-SSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSI 181
Cdd:cd03297 93 RENLAFGLKR----KRNREDRISVDELLDLLGL--DHlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2784741926 182 QAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIA 229
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-234 |
2.11e-36 |
|
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: 129.93 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqr 80
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 fRRDMQMIFQDpyASLNPRMKVKDivaegidinHL-------AKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQ 153
Cdd:cd03263 74 -RQSLGYCPQF--DALFDELTVRE---------HLrfyarlkGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
.
gi 2784741926 234 I 234
Cdd:cd03263 219 L 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-234 |
2.15e-36 |
|
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: 136.47 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 7 KQYFNVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFK-GE---DVSKLRSKaQKQRFR 82
Cdd:TIGR03269 287 KRYISVDRG-VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPD-GRGRAK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 83 RDMQMIFQDpyASLNPRMKVKDIVAEGIDI---NHLAKNDADRTkqvedlLETVGLNKDHS----SRYPHEFSGGQRQRI 155
Cdd:TIGR03269 365 RYIGILHQE--YDLYPHRTVLDNLTEAIGLelpDELARMKAVIT------LKMVGFDEEKAeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-232 |
4.38e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.75 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGE--DVSKLRSKAQKQRFRRDMQMIFQDpYaSLN 97
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRELRRNVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEG-IDINHLAKNDAdrTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISA 176
Cdd:PRK11124 95 PHLTVQQNLIEApCRVLGLSKDQA--LARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 177 LDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSD 232
Cdd:PRK11124 172 LDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-237 |
5.97e-36 |
|
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: 135.66 E-value: 5.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 15 ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPYa 94
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WRRQIAWVPQNPY- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 sLnprmkVKDIVAEGIDinhLAKNDADRTkQVEDLLETVGLNkDHSSRYPH-------E----FSGGQRQRIGIARALAV 163
Cdd:COG4988 422 -L-----FAGTIRENLR---LGRPDASDE-ELEAALEAAGLD-EFVAALPDgldtplgEggrgLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 164 QPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-224 |
7.31e-36 |
|
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: 127.11 E-value: 7.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPYas 95
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL----DLESLRKNIAYVPQDPF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 lnprmKVKDIVAEGIdinhlakndadrtkqvedlletvglnkdhssrypheFSGGQRQRIGIARALAVQPEFIIADEPIS 175
Cdd:cd03228 87 -----LFSGTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2784741926 176 ALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYGR 224
Cdd:cd03228 126 ALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-236 |
7.40e-36 |
|
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: 128.89 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVS--KLRSkaqkqrFRRDMQMIFQDPY 93
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLAS------LRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 AslnprmkVKDIVAEGIDInhlAKNDADRtKQVEDLLETVGLnkdhssrypHEF-------------------SGGQRQR 154
Cdd:cd03251 87 L-------FNDTVAENIAY---GRPGATR-EEVEEAARAANA---------HEFimelpegydtvigergvklSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEI 234
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
..
gi 2784741926 235 YA 236
Cdd:cd03251 224 LA 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-249 |
1.40e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.33 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqrFRRDMQMIFQDpyASLNPRMKVK 103
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP------AERPVSMLFQE--NNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 104 DIVAEGIDINhLAKNDADRtKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQA 183
Cdd:COG3840 90 QNIGLGLRPG-LKLTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 184 QVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSA 249
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-248 |
3.67e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.56 E-value: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvGKadevRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQR 80
Cdd:PRK11264 4 IEVKNLVKKFH-GQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQ----MIFQDpyASLNPRMKVKDIVAEG-IDINHLAKNDAdrTKQVEDLLETVGLNKDHSSrYPHEFSGGQRQRI 155
Cdd:PRK11264 79 LIRQLRqhvgFVFQN--FNLFPHRTVLENIIEGpVIVKGEPKEEA--TARARELLAKVGLAGKETS-YPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIY 235
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|...
gi 2784741926 236 AHPLHDYTASLLS 248
Cdd:PRK11264 233 ADPQQPRTRQFLE 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-237 |
4.71e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 133.37 E-value: 4.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPYas 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES----LRRQIGVVPQDTF-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 lnprmKVKDIVAEGIDinhLAKNDADRtKQVEDLLETVGLnkdhssrypHEF-------------------SGGQRQRIG 156
Cdd:COG1132 425 -----LFSGTIRENIR---YGRPDATD-EEVEEAAKAAQA---------HEFiealpdgydtvvgergvnlSGGQRQRIA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYGRMLEIASSDE--- 233
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIR-NADRILVLDDGRIVEQGTHEElla 563
|
....*..
gi 2784741926 234 ---IYAH 237
Cdd:COG1132 564 rggLYAR 570
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-225 |
2.15e-34 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 124.44 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKqRFRRDMQMIFQDpyASLN 97
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIP-YLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREI--RKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2784741926 178 DVSIQAQVVNLLKRLQReRDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:cd03292 168 DPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
2.57e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.53 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAI--IHLYEP---TSGKIIFKGEDVskLRSK 75
Cdd:COG1117 12 IEVRNLNVYY-----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGEDI--YDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 76 AQKQRFRRDMQMIFQDPyaslNP-RMKVKDIVAEGIDINHLaKNDADRTKQVEDLLETVGLN---KDHSSRYPHEFSGGQ 151
Cdd:COG1117 85 VDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGI-KSKSELDEIVEESLRKAALWdevKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQreRDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASS 231
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPT 237
|
250
....*....|...
gi 2784741926 232 DEIYAHPLHDYTA 244
Cdd:COG1117 238 EQIFTNPKDKRTE 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-225 |
4.42e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 123.54 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrSKAQKQR 80
Cdd:cd03269 1 LEVENVTKRFG-----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 F-----RRdmqmifqdpyaSLNPRMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLnKDHSSRYPHEFSGGQRQRI 155
Cdd:cd03269 72 IgylpeER-----------GLYPKMKVIDQLVYLAQLKGLKKEEARR--RIDEWLERLEL-SEYANKRVEELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVsIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-236 |
7.06e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.23 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKqyFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEdvskLRSKAQKQR 80
Cdd:PRK13650 5 IEVKNLT--FKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD----LLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLnPRMKVKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:PRK13650 79 IRHKIGMVFQNPDNQF-VGATVEDDVAFGLENKGIPHEEM--KERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKyISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
8.85e-34 |
|
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: 123.31 E-value: 8.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRF 81
Cdd:COG4181 10 ELRGLTKTVGTG-AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRD-MQMIFQdpyaS--LNPRMKVKDIVA---EgidinhLAkNDADRTKQVEDLLETVGLNK--DHssrYPHEFSGGQRQ 153
Cdd:COG4181 88 RARhVGFVFQ----SfqLLPTLTALENVMlplE------LA-GRRDARARARALLERVGLGHrlDH---YPAQLSGGEQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 154 RIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDE 233
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-217 |
8.89e-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: 122.75 E-value: 8.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskaQKQRFRRdMQMIFQDPYASLnp 98
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERRKS-IGYVMQDVDYQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 rmkVKDIVAEGIDINhlAKNDADRTKQVEDLLETVGLNKDHSsRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:cd03226 85 ---FTDSVREELLLG--LKELDAGNEQAETVLKDLDLYALKE-RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2784741926 179 VSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRI 217
Cdd:cd03226 159 YKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRV 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-234 |
1.94e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.45 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrSKAQKQRF 81
Cdd:COG4152 3 ELKGLTKRF-----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 ------RrdmqmifqdpyaSLNPRMKVKDIvaegidINHLA------KNDADRtkQVEDLLETVGLnKDHSSRYPHEFSG 149
Cdd:COG4152 74 gylpeeR------------GLYPKMKVGEQ------LVYLArlkglsKAEAKR--RADEWLERLGL-GDRANKKVEELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 150 GQRQRIGIARALAVQPEFIIADEPISALD-VSiqaqvVNLLKRL---QRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
....*....
gi 2784741926 226 LEIASSDEI 234
Cdd:COG4152 208 VLSGSVDEI 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-214 |
2.48e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.23 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQdpYASLNPRMKV 102
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDINHlaKNDADRTKQVEDLLETVGLNKDHSSRyPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQ 182
Cdd:PRK11629 105 LENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|..
gi 2784741926 183 AQVVNLLKRLQRERDLTYLFIAHDLSMVKYIS 214
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-226 |
2.77e-33 |
|
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: 121.53 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGeTFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskaQKQRFRRDMQMIFQDPyaSLNP 98
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-----QPQKLRRRIGYLPQEF--GVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDIVAegidinHLAK----NDADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:cd03264 86 NFTVREFLD------YIAWlkgiPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 175 SALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-238 |
3.31e-33 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 125.22 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDpyASLNPRMKV 102
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGidinhLAKNDADRTKQVED-LLETVGLnkDH-SSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:TIGR02142 93 RGNLRYG-----MKRARPSERRISFErVIELLGI--GHlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 181 IQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-238 |
3.43e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.04 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGE--DVSKLRSKAQKQRFRRDMQMIFQDpYaSLN 97
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQKVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEG-IDINHLAKNDAdrTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISA 176
Cdd:COG4161 95 PHLTVMENLIEApCKVLGLSKEQA--REKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 177 LDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSdEIYAHP 238
Cdd:COG4161 172 LDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQP 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
24-238 |
1.56e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 121.06 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSK---------AQKQRFRRDMQMIFQdpya 94
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadrRQLQRIRTRLGMVFQ---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 SLN--PRMKVKDIVAEG-IDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:COG4598 103 SFNlwSHMTVLENVIEApVHVLGRPKAEA--IERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLQRE-RdlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:COG4598 180 EPTSALDPELVGEVLKVMRDLAEEgR--TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-206 |
2.51e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 120.35 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 13 GKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqrfrrDMQMIFQDp 92
Cdd:COG4525 15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---------DRGVVFQK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 93 yASLNPRMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADE 172
Cdd:COG4525 85 -DALLPWLNVLDNVAFGLRLRGVPK--AERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 2784741926 173 PISALDVSIQAQVVNLLKRLQRERDLTYLFIAHD 206
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-237 |
6.64e-32 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 124.44 E-value: 6.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkQRFRRDMQMIFQDPyas 95
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL----ASLRRQVALVSQDV--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 lnprMKVKDIVAEgiDINHLAKNDADRtKQVEDLLETVGLnKDHSSRYPHEF-----------SGGQRQRIGIARALAVQ 164
Cdd:TIGR02203 416 ----VLFNDTIAN--NIAYGRTEQADR-AEIERALAAAYA-QDFVDKLPLGLdtpigengvllSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 165 PEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-225 |
9.04e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.99 E-value: 9.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskaqkqrfrrdmqmiFQDPYASLn 97
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------------FASPRDAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 prmkvkdivAEGIdinhlakndadrtkqvedllETVglnkdhssrypHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:cd03216 74 ---------RAGI--------------------AMV-----------YQLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2784741926 178 DVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:cd03216 114 TPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-234 |
1.74e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQRFRRDMQMIFQDP-----YA 94
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK----ENLKEIRKKIGIIFQNPdnqfiGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 SlnprmkVKDIVAEGIDINHLAKNDADrtKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:PRK13632 100 T------VEDDIAFGLENKKVPPKKMK--DIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 175 SALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVkYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-238 |
2.58e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.76 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 31 GETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRS---------KAQKQRFRRDMQMIFQdpYASLNPRMK 101
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadKNQLRLLRTRLTMVFQ--HFNLWSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEG-IDINHLAKNDAdRTKQVEdLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:PRK10619 109 VLENVMEApIQVLGLSKQEA-RERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 181 IQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
8-235 |
3.35e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 8 QYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVS------KLRSKAQkqrf 81
Cdd:PRK13633 13 KYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwDIRNKAG---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 rrdmqMIFQDPYASLnprmkVKDIVAEGIDI--NHLAKNDADRTKQVEDLLETVGLN--KDHSsryPHEFSGGQRQRIGI 157
Cdd:PRK13633 89 -----MVFQNPDNQI-----VATIVEEDVAFgpENLGIPPEEIRERVDESLKKVGMYeyRRHA---PHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIY 235
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-239 |
7.28e-31 |
|
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: 115.72 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskAQKQRFRRDMQMIFQDpyASLNP 98
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKRARLGIGYLPQE--ASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKD---IVAEGIDinhlaKNDADRTKQVEDLLETVGLNKDHSSRYPHeFSGGQRQRIGIARALAVQPEFIIADEPIS 175
Cdd:cd03218 89 KLTVEEnilAVLEIRG-----LSKKEREEKLEELLEEFHITHLRKSKASS-LSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 176 ALD-VSIQaQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPL 239
Cdd:cd03218 163 GVDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-233 |
8.66e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 115.40 E-value: 8.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPYAslnpr 99
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI----SRKSLRSMIGVVLQDTFL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 mkVKDIVAEGIDINHLAKNDADrtkqVEDLLETVGLNkDHSSRYP-----------HEFSGGQRQRIGIARALAVQPEFI 168
Cdd:cd03254 89 --FSGTIMENIRLGRPNATDEE----VIEAAKEAGAH-DFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 169 IADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDE 233
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-243 |
1.13e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.78 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRA---IIHLY-EP-TSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQD 91
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYpEArVSGEVYLDGQDIFKM----DVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 PYASlnPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGL---NKDHSSRYPHEFSGGQRQRIGIARALAVQPEFI 168
Cdd:PRK14247 91 PNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 169 IADEPISALDVSIQAQVVNLLkrLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYT 243
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-226 |
1.13e-30 |
|
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: 114.77 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskaQKQR 80
Cdd:cd03266 2 ITADALTKRFRD-VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-----EPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpyASLNPRMKVKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:cd03266 76 ARRRLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDEL--TARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
1.32e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYfnvGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFkGEDVSKLRSKAQK-QR 80
Cdd:PRK13634 7 KVEHRYQY---KTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLNPRMKVKDIvAEGiDINHLAKnDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEETVEKDI-CFG-PMNFGVS-EEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-269 |
1.65e-30 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 114.87 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrskaqkQRFRRDMQMIFQDpyASLNPRM 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---------TEPGPDRMVVFQN--YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 181 IQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEiyahplhdytasllsaVPVPDPeyeRA 260
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILE----------------VPFPRP---RD 209
|
....*....
gi 2784741926 261 RQQIPYDPS 269
Cdd:TIGR01184 210 RLEVVEDPS 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-238 |
2.20e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 115.09 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqKQRFRRDMQMIFQDpyASLNPR 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG---HQIARMGVVRTFQH--VRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKD--IVAEGIDINH-----LAKNDADRTKQVEDL------LETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPE 166
Cdd:PRK11300 95 MTVIEnlLVAQHQQLKTglfsgLLKTPAFRRAESEALdraatwLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-236 |
5.72e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 113.74 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 14 KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQRFRRDMQMIFQ--- 90
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL----ADPAWLRRQVGVVLQenv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 -------DPYASLNPRMKVKDIVAEGidinHLAKNDADRTKQVEDLLETVGLNKDhssryphEFSGGQRQRIGIARALAV 163
Cdd:cd03252 87 lfnrsirDNIALADPGMSMERVIEAA----KLAGAHDFISELPEGYDTIVGEQGA-------GLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 164 QPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-238 |
8.88e-30 |
|
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: 118.33 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQkqrfRRDMQMIFQDPY---ASl 96
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL----RRRIAVVPQRPHlfdTT- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 nprmkvkdiVAEGIdinHLAKNDADRTkQVEDLLETVGLnKDHSSRYPH-------E----FSGGQRQRIGIARALAVQP 165
Cdd:COG4987 425 ---------LRENL---RLARPDATDE-ELWAALERVGL-GDWLAALPDgldtwlgEggrrLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 166 EFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYIsDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-236 |
1.38e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.65 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLkqYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQR 80
Cdd:PRK13642 5 LEVENL--VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----ENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLnPRMKVKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:PRK13642 79 LRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGIPREEM--IKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-238 |
1.40e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.63 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklRSKAQKQRFRRDMQMIFQDPYAS 95
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--YDKKSLLEVRKTVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 L-NPRmkVKDIVAEGiDINhLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:PRK13639 91 LfAPT--VEEDVAFG-PLN-LGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 175 SALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-261 |
1.63e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 115.20 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDvskLRSKAQKQRF---RRDMQMIFQDpyASLNPR 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFLpphRRRIGYVFQE--ARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIdinHLAKNDADRTkQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:COG4148 92 LSVRGNLLYGR---KRAPRAERRI-SFDEVVELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 180 SIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP-----LHDYTA-SLLSAVPV- 252
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPdllplAGGEEAgSVLEATVAa 246
|
....*....
gi 2784741926 253 PDPEYERAR 261
Cdd:COG4148 247 HDPDYGLTR 255
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-236 |
2.04e-29 |
|
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: 112.25 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkQRFRRDMQMIFQDP---Y 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL----RWLRSQIGLVSQEPvlfD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASlnprmkvkdiVAEGIdinHLAKNDADrtkqVEDLLETVGLNKDHS--SRYPHEF-----------SGGQRQRIGIARA 160
Cdd:cd03249 91 GT----------IAENI---RYGKPDAT----DEEVEEAAKKANIHDfiMSLPDGYdtlvgergsqlSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-256 |
2.45e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDV-SKLRSKAQKQRFRRDMQMIFQDPYAS 95
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LNPRMKVKDIVAEGIdinHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPIS 175
Cdd:PRK13645 103 LFQETIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 176 ALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHplhdytASLLSAVPVPDP 255
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKIEIDPP 253
|
.
gi 2784741926 256 E 256
Cdd:PRK13645 254 K 254
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
4.68e-29 |
|
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: 110.60 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqKQRF 81
Cdd:cd03224 2 EVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP---HERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQMIFQDPyaSLNPRMKVKD--IVAEGidinhlAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIAR 159
Cdd:cd03224 74 RAGIGYVPEGR--RIFPELTVEEnlLLGAY------ARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-237 |
5.06e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 14 KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQRFRRDMQMIFQDPY 93
Cdd:PRK13648 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD----DNFEKLRKHIGIVFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASLNPRMkVKDIVAEGIDiNHLAKNDaDRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:PRK13648 94 NQFVGSI-VKYDVAFGLE-NHAVPYD-EMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 174 ISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-265 |
7.20e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.59 E-value: 7.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrfRRDMQMIF 89
Cdd:PRK11000 8 NVTKAyGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDpYAsLNPRMKVKDIVAEGIDINHLAKNDAD-RTKQVEDLLETVGLnkdhSSRYPHEFSGGQRQRIGIARALAVQPEFI 168
Cdd:PRK11000 82 QS-YA-LYPHLSVAENMSFGLKLAGAKKEEINqRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 169 IADEPISALD----VSIQAQVVNLLKRLQRerdlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTA 244
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
|
250 260
....*....|....*....|....*...
gi 2784741926 245 SLLSA-------VPVPDPEYERARQQIP 265
Cdd:PRK11000 232 GFIGSpkmnflpVKVTATAIEQVQVELP 259
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-237 |
7.80e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTgRAIIH-LYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPyasln 97
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTL-INLLQrVFDPQSGRILIDGTDIRTV----TRASLRRNIAVVFQDA----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 prMKVKDIVAEGIDINHLAKNDAD-----RTKQVEDLLET--VGLNKDHSSRyPHEFSGGQRQRIGIARALAVQPEFIIA 170
Cdd:PRK13657 419 --GLFNRSIEDNIRVGRPDATDEEmraaaERAQAHDFIERkpDGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 171 DEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-248 |
8.55e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 111.28 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTS-----GKIIFKGEDVSKLRskAQKQRFRRDMQMIFQ 90
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERR--VNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 DPyaSLNPrMKVKDIVAEGI------------DINHLAKNDADRTKQVEdlletvglNKDHSSRYphEFSGGQRQRIGIA 158
Cdd:PRK14258 96 KP--NLFP-MSVYDNVAYGVkivgwrpkleidDIVESALKDADLWDEIK--------HKIHKSAL--DLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMH-----YGRMLEIASSDE 233
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKK 242
|
250
....*....|....*....
gi 2784741926 234 IYAHPL----HDYTASLLS 248
Cdd:PRK14258 243 IFNSPHdsrtREYVLSRLG 261
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-225 |
8.82e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.96 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaQKQRFRRDMQMIFQDPYASLNp 98
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR-EVPFLRRQIGMIFQDHHLLMD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 rMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:PRK10908 94 -RTVYDNVAIPLIIAGASGDDIRR--RVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2784741926 179 VSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:PRK10908 170 DALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-248 |
1.08e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.64 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKAdevraVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYE-----PTSGKIIFKGEDVSKLRSK 75
Cdd:PRK14239 6 LQVSDLSVYYNKKKA-----LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 76 AQKqrFRRDMQMIFQDPyaslNP-RMKVKDIVAEGIDINHLaKNDADRTKQVEDLLETVGL---NKDHSSRYPHEFSGGQ 151
Cdd:PRK14239 81 TVD--LRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGI-KDKQVLDEAVEKSLKGASIwdeVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQreRDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASS 231
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
250
....*....|....*..
gi 2784741926 232 DEIYAHPLHDYTASLLS 248
Cdd:PRK14239 232 KQMFMNPKHKETEDYIS 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-225 |
1.76e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.35 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSkLRS--KAQKQRfrrdMQMIFQDPyaS 95
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSprDAQAAG----IAIIHQEL--N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LNPRMKvkdiVAEGIDINHLAK-----NDADRTKQVEDLLETVGLNKDhssryPH----EFSGGQRQRIGIARALAVQPE 166
Cdd:COG1129 90 LVPNLS----VAENIFLGREPRrggliDWRAMRRRARELLARLGLDID-----PDtpvgDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-249 |
1.92e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.69 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQR 80
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLNPRMKVKDIvaEGIDINHLAKNDADRTKQVEdLLETVGLNKDHSSRYPHEFSGGQRQRIGIARA 160
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDV--EFGPKNFGFSEDEAKEKALK-WLKKVGLSEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA---- 236
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSdkew 238
|
250
....*....|....*.
gi 2784741926 237 ---HPLHDYTASLLSA 249
Cdd:PRK13641 239 lkkHYLDEPATSRFAS 254
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-225 |
2.06e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 108.80 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 28 VYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqrFRRDMQMIFQDpyASLNPRMKVKDIVA 107
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP------YQRPVSMLFQE--NNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 108 EGIdiNHLAKNDADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVN 187
Cdd:TIGR01277 93 LGL--HPGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2784741926 188 LLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
2.46e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.10 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKI----IFKGEDVSKLR--- 73
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHElit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 74 SKAQKQ-----RFRRDMQMIFQDPYASLNPRMKVKDI----VAEGIdinhlAKNDAdrTKQVEDLLETVGLNKDHSSRYP 144
Cdd:PRK13631 102 NPYSKKiknfkELRRRVSMVFQFPEYQLFKDTIEKDImfgpVALGV-----KKSEA--KKLAKFYLNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 145 HEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|....
gi 2784741926 225 MLEIASSDEIYAHP 238
Cdd:PRK13631 254 ILKTGTPYEIFTDQ 267
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
4.25e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.16 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvGKADEVRAVDditFDVYQGETFGLVGESGSGKTTTGRAIIHLYE-----PTSGKIIFKGEDVskLRSK 75
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNI--YSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 76 AQKQRFRRDMQMIFQdpYASLNPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGL---NKDHSSRYPHEFSGGQR 152
Cdd:PRK14267 78 VDPIEVRREVGMVFQ--YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 153 QRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQreRDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSD 232
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
250
....*....|....*...
gi 2784741926 233 EIYAHPLHDYTASLLSAV 250
Cdd:PRK14267 234 KVFENPEHELTEKYVTGA 251
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-225 |
9.51e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 107.29 E-value: 9.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 14 KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDP- 92
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL----DPADLRRNIGYVPQDVt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 93 --YASLNprmkvkdivaEGIDINHLAKNDADrtkqVEDLLETVGLNkDHSSRYPHEF-----------SGGQRQRIGIAR 159
Cdd:cd03245 89 lfYGTLR----------DNITLGAPLADDER----ILRAAELAGVT-DFVNKHPNGLdlqigergrglSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYGRM 225
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-238 |
1.03e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 110.32 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 7 KQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrfrRDMQ 86
Cdd:PRK11650 11 KSYDG-----KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD------RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 87 MIFQDpYAsLNPRMKVKDIVAEGIDINHLAK-------NDADRTKQVEDLLEtvglnkdhssRYPHEFSGGQRQRIGIAR 159
Cdd:PRK11650 80 MVFQN-YA-LYPHMSVRENMAYGLKIRGMPKaeieervAEAARILELEPLLD----------RKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-243 |
1.16e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 10 FNVGK----ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYE------PTSGKIIFKGEDVSKLRSKaqkq 79
Cdd:PRK14246 11 FNISRlylyINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 RFRRDMQMIFQDPYASlnPRMKVKDIVAEGIDiNHLAKNDADRTKQVEDLLETVGLNKDHSSRY---PHEFSGGQRQRIG 156
Cdd:PRK14246 87 KLRKEVGMVFQQPNPF--PHLSIYDNIAYPLK-SHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErdLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
....*..
gi 2784741926 237 HPLHDYT 243
Cdd:PRK14246 242 SPKNELT 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-227 |
1.17e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 107.46 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAI--IHLYEPTSGKIIFKGEDVSKLrskAQKQRFRRDMQMIFQDPYASlnPR 99
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILEL---SPDERARAGIFLAFQYPVEI--PG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIDINHLAKNDA-DRTKQVEDLLETVGLNKDHSSRYPHE-FSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSArEFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 178 DV---SIQAQVVNLLkrlqRERDLTYLFIAHDLSMVKYIS-DRIGVMHYGRMLE 227
Cdd:COG0396 172 DIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVK 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-224 |
1.55e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqr 80
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQM--IFQDPYASLNPRMKVkdivAEgidiN-HLAKN-----------DADRTKQVEDLLETVGLNKDHSSRYPHE 146
Cdd:COG1101 76 YKRAKYIgrVFQDPMMGTAPSMTI----EE----NlALAYRrgkrrglrrglTKKRRELFRELLATLGLGLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 147 F-SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLS-MVKYiSDRIGVMHYGR 224
Cdd:COG1101 148 LlSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDY-GNRLIMMHEGR 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
17-236 |
1.68e-27 |
|
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: 112.10 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRskaqKQRFRRDMQMIFQDP---Y 93
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLD----PAELRARMALVPQDPvlfA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASL--NPRMKVKDIVAEGIDinhlaknDADRTKQVEDLLetvglnkdhsSRYPHEF-----------SGGQRQRIGIARA 160
Cdd:TIGR02204 428 ASVmeNIRYGRPDATDEEVE-------AAARAAHAHEFI----------SALPEGYdtylgergvtlSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:TIGR02204 491 ILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-206 |
2.15e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.02 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqRFRRDMQMIF 89
Cdd:COG4133 7 NLSCRrGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-----DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 qdPYASLNPRMKVkdivAEGIDINHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:COG4133 82 --HADGLKPELTV----RENLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRlQRERDLTYLFIAHD 206
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-225 |
4.15e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 105.27 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFD--VYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrfRRDMQMIFQDpyASLNPRMK 101
Cdd:cd03298 15 MHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEGIDINhLAKNDADRtKQVEDLLETVGL-NKDhsSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:cd03298 87 VEQNVGLGLSPG-LKLTAEDR-QAIEVALARVGLaGLE--KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2784741926 181 IQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-239 |
5.15e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 5.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHL-KQYfnvGKAdevRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskAQKQR 80
Cdd:COG1137 5 EAENLvKSY---GKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL---PMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPyaSLNPRMKVKD---IVAEGIDINHlakndADRTKQVEDLLETVGLNKDHSSRyPHEFSGGQRQRIGI 157
Cdd:COG1137 76 ARLGIGYLPQEA--SIFRKLTVEDnilAVLELRKLSK-----KEREERLEELLEEFGITHLRKSK-AYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 158 ARALAVQPEFIIADEPISALD---VS-IQAQVVNLlkrlqRERDLTYLFIAHD----LSmvkyISDRIGVMHYGRMLEIA 229
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVLITDHNvretLG----ICDRAYIISEGKVLAEG 218
|
250
....*....|
gi 2784741926 230 SSDEIYAHPL 239
Cdd:COG1137 219 TPEEILNNPL 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-224 |
8.85e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.05 E-value: 8.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 25 TFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQkqrfrRDMQMIFQDpyASLNPRMKVKD 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT-PPSR-----RPVSMLFQE--NNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 105 IVAEGIDINhlAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQ 184
Cdd:PRK10771 91 NIGLGLNPG--LKLNAAQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2784741926 185 VVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-234 |
9.19e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.91 E-value: 9.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkQRF 81
Cdd:TIGR03410 2 EVSNLNVYY-----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH---ERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDM------QMIFqdpyaslnPRMKVKD---IVAEGIdinhlakndADRTKQV-EDLLETVGLNKDHSSRYPHEFSGGQ 151
Cdd:TIGR03410 74 RAGIayvpqgREIF--------PRLTVEEnllTGLAAL---------PRRSRKIpDEIYELFPVLKEMLGRRGGDLSGGQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASS 231
Cdd:TIGR03410 137 QQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAG 216
|
...
gi 2784741926 232 DEI 234
Cdd:TIGR03410 217 DEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-236 |
1.02e-26 |
|
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: 105.00 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDP--- 92
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV----TLDSLRRAIGVVPQDTvlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 93 ---------YASLNprmkvkdivAEGIDINHLAK--NDADRTKQVEDLLETV----GLnkdhssryphEFSGGQRQRIGI 157
Cdd:cd03253 88 ndtigynirYGRPD---------ATDEEVIEAAKaaQIHDKIMRFPDGYDTIvgerGL----------KLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVkYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-237 |
1.30e-26 |
|
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: 103.76 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHL--YEPTSGKIIFKGEDVSKLrskAQKQRFRRDMQMIFQDPy 93
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL---PPEERARLGIFLAFQYP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 aslnPRMkvkdivaEGIdinhlakndadrtkQVEDLLETVGLNkdhssrypheFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:cd03217 87 ----PEI-------PGV--------------KNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 174 ISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYI-SDRIGVMHYGRMLEIASS---DEIYAH 237
Cdd:cd03217 132 DSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKelaLEIEKK 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-230 |
2.69e-26 |
|
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: 103.34 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRskaqKQRFRRDMQMIFQDPY------ 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG----LHDLRSRISIIPQDPVlfsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 -ASLNPRMKVKDivAEGIDINHLAKNDaDRTKQVEDLLETV----GLNkdhssrypheFSGGQRQRIGIARALAVQPEFI 168
Cdd:cd03244 95 rSNLDPFGEYSD--EELWQALERVGLK-EFVESLPGGLDTVveegGEN----------LSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 169 IADEPISALDVSIQAQVVNLLKRlqRERDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIAS 230
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-236 |
3.51e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDV-SKLRSKAQKQrFRRDMQMIFQDPYAS 95
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP-VRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LnprmkVKDIVAEGIDINhlAKNDADRTKQVED----LLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PRK13646 98 L-----FEDTVEREIIFG--PKNFKMNLDEVKNyahrLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-225 |
6.31e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrsKAQKQRFRRDM--QmifqdpYASLNP 98
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW--SPAELARRRAVlpQ------HSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDIVAEGIDINHLAKNDADRTkqVEDLLETVGLnkDH-SSRYPHEFSGGQRQRIGIARALA------VQPEFIIAD 171
Cdd:PRK13548 90 PFTVEEVVAMGRAPHGLSRAEDDAL--VAAALAQVDL--AHlAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-236 |
8.40e-26 |
|
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: 107.35 E-value: 8.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLK-QYfnvgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQR 80
Cdd:TIGR03797 453 EVDRVTfRY----RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL----DVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpyASLNPRMKVKDIVAeGIDINHlakndadrtKQVEDLLETVGLNKD--------HS--SRYPHEFSGG 150
Cdd:TIGR03797 525 VRRQLGVVLQN--GRLMSGSIFENIAG-GAPLTL---------DEAWEAARMAGLAEDirampmgmHTviSEGGGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 151 QRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQrerdLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIAS 230
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
....*.
gi 2784741926 231 SDEIYA 236
Cdd:TIGR03797 668 YDELMA 673
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-217 |
9.69e-26 |
|
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: 102.13 E-value: 9.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYF---NVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGE----DVSKLrS 74
Cdd:COG4778 6 EVENLSKTFtlhLQGGK-RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQA-S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 75 KAQKQRFRRDMqmIfqdPYAS--LN--PRMKVKDIVAE-----GIDinhlaKNDADRtkQVEDLLETVGLNKDHSSRYPH 145
Cdd:COG4778 84 PREILALRRRT--I---GYVSqfLRviPRVSALDVVAEpllerGVD-----REEARA--RARELLARLNLPERLWDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 146 EFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQReRDLTYLFIAHDLSMVKYISDRI 217
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRV 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-206 |
1.07e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAII-HLYEP--TSGKIIFKGEDVSKLrsKAQkqrfRRDMQMIFQDPYasLN 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTAL--PAE----QRRIGILFQDDL--LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEGIDiNHLAKndADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:COG4136 89 PHLSVGENLAFALP-PTIGR--AQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180
....*....|....*....|....*....
gi 2784741926 178 DVSIQAQVVNLLKRLQRERDLTYLFIAHD 206
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-234 |
2.21e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.17 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVyqGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQD-PYASlnpRMKV 102
Cdd:PRK10575 32 LTFPA--GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA----FARKVAYLPQQlPAAE---GMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDINH--LAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:PRK10575 103 RELVAIGRYPWHgaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 181 IQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-236 |
2.52e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKqr 80
Cdd:PRK13636 6 LKVEELNYNY----SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYASLNPRMKVKDIVAEGIDINhLAKNDADRtkQVEDLLETVGLnkDHSSRYP-HEFSGGQRQRIGIAR 159
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFGAVNLK-LPEDEVRK--RVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-238 |
3.20e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTS---GKIIFKGedvSKLRSKAQ 77
Cdd:PRK13640 6 VEFKHVSFTY---PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG---ITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 78 KQrFRRDMQMIFQDPYASLnPRMKVKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGI 157
Cdd:PRK13640 80 WD-IREKVGIVFQNPDNQF-VGATVGDDVAFGLENRAVPRPEM--IKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKyISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 2784741926 238 P 238
Cdd:PRK13640 234 V 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-234 |
4.45e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRfrrdMQMIFQDpyASL 96
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR----VASVPQD--TSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 NPRMKVKDIVAEGiDINHLAK----NDADRTKqVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADE 172
Cdd:PRK09536 89 SFEFDVRQVVEMG-RTPHRSRfdtwTETDRAA-VERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 173 PISALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-225 |
4.82e-25 |
|
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: 98.83 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQ--MIFqdpyaslnp 98
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQddELF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 rmkvKDIVAEGIdinhlakndadrtkqvedlletvglnkdhssrypheFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:cd03246 89 ----SGSIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2784741926 179 VSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKyISDRIGVMHYGRM 225
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-250 |
5.68e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.33 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 36 LVGESGSGKTTTGRAIIHLYEPTSG-----KIIFKGEDVSKLRSKAQkqrFRRDMQMIFQDPyaslNP-RMKVKDIVAEG 109
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLE---FRRRVGMLFQRP----NPfPMSIMDNVLAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 110 IDINHLAKNDADRTKQVEDLLEtVGL---NKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVV 186
Cdd:PRK14271 125 VRAHKLVPRKEFRGVAQARLTE-VGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 187 NLLKRLQRErdLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPLHDYTASLLSAV 250
Cdd:PRK14271 204 EFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-224 |
1.07e-24 |
|
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: 104.18 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDP--- 92
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD----LRRNIGYVPQDPrlf 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 93 YASLnprmkvkdivAEGIDINHLAKNDadrtkqvEDLLETV---GLN---KDHSSRYPH-------EFSGGQRQRIGIAR 159
Cdd:TIGR03375 552 YGTL----------RDNIALGAPYADD-------EEILRAAelaGVTefvRRHPDGLDMqigergrSLSGGQRQAVALAR 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 160 ALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYGR 224
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGR 676
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-217 |
1.56e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 99.75 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKADEVRAV-DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIifkgedvskLRSKAQKQRFRRDMQMIF 89
Cdd:PRK11247 17 AVSKRYGERTVlNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDpyASLNPRMKVKDIVAEGidinhLAKNDADRTKQVedlLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:PRK11247 88 QD--ARLLPWKKVIDNVGLG-----LKGQWRDAALQA---LAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRI 217
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
14-236 |
1.62e-24 |
|
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: 103.67 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 14 KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQRFRRDMQMIFQ--- 90
Cdd:TIGR01846 466 APDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI----ADPAWLRRQMGVVLQenv 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 -------DPYASLNPRMKVKDIVAegidinhlakndADRTKQVEDLLetvglnkdhsSRYPHEF-----------SGGQR 152
Cdd:TIGR01846 542 lfsrsirDNIALCNPGAPFEHVIH------------AAKLAGAHDFI----------SELPQGYntevgekganlSGGQR 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 153 QRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSD 232
Cdd:TIGR01846 600 QRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGR--TVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHE 676
|
....
gi 2784741926 233 EIYA 236
Cdd:TIGR01846 677 ELLA 680
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-238 |
1.92e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPyasLNPRMKV 102
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY----LHRQVALVGQEP---VLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPH--EFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 181 IQAQVVNLLKRlqreRDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:TIGR00958 652 CEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-210 |
2.01e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.16 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGED------------ 68
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 69 ------VSKLRSKAQKQ--RFRRDMQMIFQDPYASLNPRMKVKDI----VAEGIDinhlaKNDADrtKQVEDLLETVGLN 136
Cdd:PRK13651 83 vleklvIQKTRFKKIKKikEIRRRVGVVFQFAEYQLFEQTIEKDIifgpVSMGVS-----KEEAK--KRAAKYIELVGLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 137 KDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMV 210
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNV 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-207 |
2.18e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.00 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrSKAQKQrfrrdmqMIFQDpyASLNP 98
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERG-------VVFQN--EGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDIVAEGIDINHLAKndADRTKQVEDLLETVGLNKDHSsRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:PRK11248 84 WRNVQDNVAFGLQLAGVEK--MQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*....
gi 2784741926 179 VSIQAQVVNLLKRLQRERDLTYLFIAHDL 207
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-226 |
2.49e-24 |
|
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: 98.56 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 4 EHLKQYFNvGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskaQKQRFRR 83
Cdd:cd03267 21 GSLKSLFK-RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-----RRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 84 DMQMIFqdpyaslNPRMKVK-DI-VAEGIDINHLAKN--DADRTKQVEDLLETVGLNK--DHSSRyphEFSGGQRQRIGI 157
Cdd:cd03267 95 RIGVVF-------GQKTQLWwDLpVIDSFYLLAAIYDlpPARFKKRLDELSELLDLEEllDTPVR---QLSLGQRMRAEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-238 |
2.68e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQRFRRDMQMIFQDPYASLN 97
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK----ENIREVRKFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEGIDinhLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:PRK13652 93 SPTVEQDIAFGPIN---LGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 178 DVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
21-236 |
4.07e-24 |
|
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: 102.33 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDvsklRSKAQKQRFRRDMQMIFQDpyASL---- 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP----REEIPREVLANSVAMVDQD--IFLfegt 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 --------NPRMKVKDIVAegidinhlAKNDA-------DRTKQVEDLLETVGLNkdhssrypheFSGGQRQRIGIARAL 161
Cdd:TIGR03796 569 vrdnltlwDPTIPDADLVR--------ACKDAaihdvitSRPGGYDAELAEGGAN----------LSGGQRQRLEIARAL 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRlqreRDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWA 700
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
1-217 |
8.48e-24 |
|
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: 96.69 E-value: 8.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVR--AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFK--GEDVSKLRSKA 76
Cdd:TIGR02324 2 LEVEDLSKTFTLHQQGGVRlpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRheGAWVDLAQASP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 77 QKQRFRRDMQMIFQDPYASLNPRMKVKDIVAEGIDINHLAKNDAdrTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIG 156
Cdd:TIGR02324 82 REVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAA--RARARELLARLNIPERLWHLPPATFSGGEQQRVN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERdLTYLFIAHDLSMVKYISDRI 217
Cdd:TIGR02324 160 IARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARG-AALIGIFHDEEVRELVADRV 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-228 |
9.93e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 96.45 E-value: 9.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 5 HLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaqkqrfrrd 84
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 85 mqmifqDPYASLNPRMKVKdivaEGIDINHLAKN--DADRTKQVEDLLETVGLNKDHSSRYPHeFSGGQRQRIGIARALA 162
Cdd:cd03220 90 ------GLGGGFNPELTGR----ENIYLNGRLLGlsRKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 163 VQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEI 228
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-220 |
1.14e-23 |
|
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: 100.82 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqrFRRDmqmifQDPYASLNPR 99
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-----SWRD-----QIAWVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MkVKDIVAEGIdinHLAKNDADRTkQVEDLLETVGLNKDHSSR----------YPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:TIGR02857 407 L-FAGTIAENI---RLARPDASDA-EIREALERAGLDEFVAALpqgldtpigeGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSmVKYISDRIGVM 220
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLA-LAALADRIVVL 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-235 |
1.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.50 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDPYASLNP 98
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDiVAEGIDINHLAKNDADrtKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:PRK13643 100 ETVLKD-VAFGPQNFGIPKEKAE--KIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 179 VSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIY 235
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-225 |
1.80e-23 |
|
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: 94.81 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrskaqkqrfrrdmqmifqdpyaslnP 98
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV----------------------------T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDIVAEGIdiNHLAkndADRTKQvedlletvGLNKDHSSRY----PHEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:cd03215 66 RRSPRDAIRAGI--AYVP---EDRKRE--------GLVLDLSVAEnialSSLLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 175 SALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:cd03215 133 RGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-226 |
3.08e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.80 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQD---- 91
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRyhll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 PYASLNPRMKVKDIVAegidinhlAKNDADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PRK10535 99 SHLTAAQNVEVPAVYA--------GLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDlSMVKYISDRIGVMHYGRML 226
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-225 |
7.18e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrskaqkqRFR--RD-MQ----MIFQ 90
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV----------RIRspRDaIAlgigMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 DPyaSLNPRMKVKDIVAEGIDINHLAKNDADR-TKQVEDLLETVGLNKDhSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:COG3845 88 HF--MLVPNLTVAENIVLGLEPTKGGRLDRKAaRARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 170 ADEPISALDvsiQAQVVNLLKRLQRERD--LTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:COG3845 165 LDEPTAVLT---PQEADELFEILRRLAAegKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-248 |
1.06e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.85 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYE-----PTSGKIIFKGEDVSKlrSKAQKQRFRRDMQMIFQDPya 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA--PDVDPVEVRRRIGMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 slNPRMK-VKDIVAEGIDINHLaKNDADRTkqVEDLLETVGL---NKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIA 170
Cdd:PRK14243 101 --NPFPKsIYDNIAYGARINGY-KGDMDEL--VERSLRQAALwdeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 171 DEPISALDVSIQAQVVNLLKRLQreRDLTYLFIAHDLSMVKYISDRIGVMH---------YGRMLEIASSDEIYAHPLHD 241
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQ 253
|
....*..
gi 2784741926 242 YTASLLS 248
Cdd:PRK14243 254 ATRDYVS 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-206 |
1.13e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.08 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYfnVGKAD-EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQ 79
Cdd:PRK10584 7 VEVHHLKKS--VGQGEhELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 RFRRDMQMIFQDpyaslnpRMKVKDIVA-EGIDINHLAKNDADRT--KQVEDLLETVGLNK--DHssrYPHEFSGGQRQR 154
Cdd:PRK10584 85 LRAKHVGFVFQS-------FMLIPTLNAlENVELPALLRGESSRQsrNGAKALLEQLGLGKrlDH---LPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHD 206
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-238 |
1.14e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDV---SKLrskaqkQRFRRDMQMIFQDP 92
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKL------QGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 93 YASLNPRmKVKDIVAEGIDinHLAKNDADRTKQVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADE 172
Cdd:PRK13644 87 ETQFVGR-TVEEDLAFGPE--NLCLPPIEIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 173 PISALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVkYISDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-238 |
1.55e-22 |
|
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: 93.51 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkQRF 81
Cdd:COG0410 5 EVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH---RIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDM------QMIFqdpyaslnPRMKVKDivaegidiN-----HLAKNDADRTKQVEDLLEtvglnkdhssRYP--HEF- 147
Cdd:COG0410 77 RLGIgyvpegRRIF--------PSLTVEE--------NlllgaYARRDRAEVRADLERVYE----------LFPrlKERr 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 148 -------SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVM 220
Cdd:COG0410 131 rqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVL 209
|
250
....*....|....*...
gi 2784741926 221 HYGRMLEIASSDEIYAHP 238
Cdd:COG0410 210 ERGRIVLEGTAAELLADP 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-267 |
1.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.42 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTgraIIHL---YEPTSGKIIFKGEDVSKlrskAQ 77
Cdd:PRK13647 5 IEVEDLHFRYK----DGTKALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLngiYLPQRGRVKVMGREVNA----EN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 78 KQRFRRDMQMIFQDPYASLNPrMKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGI 157
Cdd:PRK13647 74 EKWVRSKVGLVFQDPDDQVFS-STVWDDVAFGPVNMGLDKDEVER--RVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGRML-----EIASSD 232
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLaegdkSLLTDE 228
|
250 260 270
....*....|....*....|....*....|....*
gi 2784741926 233 EIYAHPlhDYTASLLSAVPVPDPEYERARqqIPYD 267
Cdd:PRK13647 229 DIVEQA--GLRLPLVAQIFEDLPELGQSK--LPLT 259
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-234 |
2.22e-22 |
|
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: 97.50 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKqyFNVGKADEVraVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQR 80
Cdd:TIGR01193 474 IVINDVS--YSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI----DRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPYaslnprmkvkdIVAEGIDINHLAKNDADRTKQ-VEDLLETVGLNKD--------HSSRYPHEF--SG 149
Cdd:TIGR01193 546 LRQFINYLPQEPY-----------IFSGSILENLLLGAKENVSQDeIWAACEIAEIKDDienmplgyQTELSEEGSsiSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 150 GQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQrerDLTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIA 229
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
....*
gi 2784741926 230 SSDEI 234
Cdd:TIGR01193 691 SHDEL 695
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-237 |
3.08e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.63 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVS--KLRSkaqkqrFRRDMQMIFQDPYA 94
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLAS------LRNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 slnprmkVKDIVAEGI-----------DINHLAK--NDADRTKQVEDLLETV-GLNKDhssryphEFSGGQRQRIGIARA 160
Cdd:PRK11176 429 -------FNDTIANNIayarteqysreQIEEAARmaYAMDFINKMDNGLDTViGENGV-------LLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 161 LAVQPEFIIADEPISALDV----SIQAQvvnlLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK11176 495 LLRDSPILILDEATSALDTeserAIQAA----LDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
.
gi 2784741926 237 H 237
Cdd:PRK11176 568 Q 568
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-224 |
3.41e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 4 EHLKQYFNVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAI--IHLYEPTSGKIIFKGEdvsKLRSKAQKQR 80
Cdd:PRK13549 3 EYLLEMKNITKTfGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGE---ELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpyaslnpRMKVKDI-VAEGI----DINHLAKNDADR-TKQVEDLLETVGLNKDHSSRYpHEFSGGQRQR 154
Cdd:PRK13549 80 ERAGIAIIHQE-------LALVKELsVLENIflgnEITPGGIMDYDAmYLRAQKLLAQLKLDINPATPV-GNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 155 IGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQReRDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-224 |
3.83e-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: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 12 VGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAI--IHLYEPTSGKIIFKGEDvskLRSKAQKQRFRRDMQMIF 89
Cdd:TIGR02633 8 VKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgVYPHGTWDGEIYWSGSP---LKASNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDpyASLNPRMKVKDIVAEGIDINHLAK--NDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEF 167
Cdd:TIGR02633 85 QE--LTLVPELSVAENIFLGNEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 168 IIADEPISALDVSIQAQVVNLLKRLQReRDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-237 |
9.31e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 6 LKQYFNVGK---ADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaqkqrfr 82
Cdd:COG1134 24 LKELLLRRRrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 83 rDMQMIFqDPYAS------LNPRM----------KVKDIV--AEgidinhlakndadrtkqVEDLLET-VGlnkdhssRY 143
Cdd:COG1134 94 -ELGAGF-HPELTgreniyLNGRLlglsrkeideKFDEIVefAE-----------------LGDFIDQpVK-------TY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 144 phefSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYG 223
Cdd:COG1134 148 ----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|....
gi 2784741926 224 RMLEIASSDEIYAH 237
Cdd:COG1134 223 RLVMDGDPEEVIAA 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-237 |
1.67e-21 |
|
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: 94.34 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 13 GKADEVRavdDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDp 92
Cdd:TIGR01842 329 GKKPTLR---GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW----DRETFGKHIGYLPQD- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 93 yASLNPRMKVKDIVAEGIDINHLAKNDADRTKQVEDLL-------ETVgLNKDHSSrypheFSGGQRQRIGIARALAVQP 165
Cdd:TIGR01842 401 -VELFPGTVAENIARFGENADPEKIIEAAKLAGVHELIlrlpdgyDTV-IGPGGAT-----LSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 166 EFIIADEPISALDVSIQAQVVNLLKRLQReRDLTYLFIAHDLSMVKYIsDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEVLAK 543
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-217 |
1.80e-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: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 26 FDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSK----AQKQRFRRDMQMIFQdpYASLNPRMK 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHigyvPQRHEFAWDFPISVA--HTVMSGRTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VkdivaegidINHLAKNDADRTKQVEDLLETVGLNkdHSSRYP-HEFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:TIGR03771 79 H---------IGWLRRPCVADFAAVRDALRRVGLT--ELADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2784741926 181 IQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRI 217
Cdd:TIGR03771 148 TQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-237 |
4.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDPYASL 96
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 NPRMKVKDiVAEGIDINHLAKNDADRTkqVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISA 176
Cdd:PRK13649 99 FEETVLKD-VAFGPQNFGVSQEEAEAL--AREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 177 LDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK13649 176 LDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-250 |
5.07e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 8 QYFNVGKADEvRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFR----- 82
Cdd:PRK11231 6 ENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAllpqh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 83 ---------RDMQMIFQDPYASLNPRMKVKD--IVAEGID---INHLAKndadrtKQVEDLletvglnkdhssryphefS 148
Cdd:PRK11231 85 hltpegitvRELVAYGRSPWLSLWGRLSAEDnaRVNQAMEqtrINHLAD------RRLTDL------------------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 149 GGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYGRMLEI 228
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
250 260
....*....|....*....|..
gi 2784741926 229 ASSDEIyahplhdYTASLLSAV 250
Cdd:PRK11231 220 GTPEEV-------MTPGLLRTV 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-227 |
6.26e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVG-KADEVRAVDDITFDVYQGEtFGLV-GESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQK 78
Cdd:PRK10247 2 QENSPLLQLQNVGyLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL----KP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 79 QRFRRDMQMIFQDPyaslnprMKVKDIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIA 158
Cdd:PRK10247 77 EIYRQQVSYCAQTP-------TLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVM-HYGRMLE 227
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQpHAGEMQE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-236 |
1.03e-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: 92.17 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTtgraIIHL------YEPTSGKII----------- 63
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVlrgmdqYEPTSGRIIyhvalcekcgy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 64 -----FKGEDVSKL-------------RSKAQKQRFRRDMQMIFQDPYAsLNPRMKVKDIVAEGI-DINHLAKNDADRTK 124
Cdd:TIGR03269 72 verpsKVGEPCPVCggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALeEIGYEGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 125 qveDLLETVGLnkdhSSRYPH---EFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYL 201
Cdd:TIGR03269 151 ---DLIEMVQL----SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV 223
|
250 260 270
....*....|....*....|....*....|....*
gi 2784741926 202 FIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:TIGR03269 224 LTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-234 |
1.11e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHL-KQYfnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSK--AQ 77
Cdd:COG4604 2 IEIKNVsKRY------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 78 KqrfrrdMQMIFQDPyaSLNPRMKVKDIVA-------EGidinHLakNDADRTKqVEDLLETVGLNkDHSSRYPHEFSGG 150
Cdd:COG4604 76 R------LAILRQEN--HINSRLTVRELVAfgrfpysKG----RL--TAEDREI-IDEAIAYLDLE-DLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 151 QRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIAS 230
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
....
gi 2784741926 231 SDEI 234
Cdd:COG4604 220 PEEI 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-230 |
1.26e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 87.85 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQR 80
Cdd:cd03369 7 IEVENLSVRY---APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI----PLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDPyaslnprmkvkdIVAEGIDINHLAKNDADRTKQVEDLLETV--GLNkdhssrypheFSGGQRQRIGIA 158
Cdd:cd03369 80 LRSSLTIIPQDP------------TLFSGTIRSNLDPFDEYSDEEIYGALRVSegGLN----------LSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAqvvnLLKRLQRE--RDLTYLFIAHDL-SMVKYisDRIGVMHYGRMLEIAS 230
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDA----LIQKTIREefTNSTILTIAHRLrTIIDY--DKILVMDAGEVKEYDH 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-226 |
1.33e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNVGKAD----------------EVRAVDDITFDVYQGETFGLVGESGSGKTTT-----GraIIHlyePTSG 60
Cdd:COG4586 3 EVENLSKTYRVYEKEpglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltG--ILV---PTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 61 KIIFKGEDVSKlrskaQKQRFRRDMQMIF------------QDPYAsLNprmkvKDIVaeGIDinhlaknDADRTKQVED 128
Cdd:COG4586 78 EVRVLGYVPFK-----RRKEFARRIGVVFgqrsqlwwdlpaIDSFR-LL-----KAIY--RIP-------DAEYKKRLDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 129 LLETVGLnkdhssrypHEF--------SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTY 200
Cdd:COG4586 138 LVELLDL---------GELldtpvrqlSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTI 208
|
250 260
....*....|....*....|....*.
gi 2784741926 201 LFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:COG4586 209 LLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-215 |
1.66e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.05 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRFRRDMQMIFQDpyASLNPRMK 101
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM-SRSRLYTVRKRMSMLFQS--GALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEGIDiNHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSI 181
Cdd:PRK11831 101 VFDNVAYPLR-EHTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190
....*....|....*....|....*....|....
gi 2784741926 182 QAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISD 215
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-234 |
1.87e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLkqyfNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrf 81
Cdd:COG3845 259 EVENL----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 RRDMQM--IFQDPYAS-LNPRMKVKD-IVAEGIDINHLAKNDADRTKQVEDLleTVGLNKDHSSRYPHE------FSGGQ 151
Cdd:COG3845 330 RRRLGVayIPEDRLGRgLVPDMSVAEnLILGRYRRPPFSRGGFLDRKAIRAF--AEELIEEFDVRTPGPdtparsLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASS 231
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPA 486
|
...
gi 2784741926 232 DEI 234
Cdd:COG3845 487 AEA 489
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-207 |
2.00e-20 |
|
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: 88.22 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKII------FKGEDVSKLRSK------AQKQRFRR 83
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELRKRiglvspALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 84 DMqmifqdpyaslnprmKVKDIVAEG----IDI-NHLakNDADRtKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIA 158
Cdd:COG1119 94 DE---------------TVLDVVLSGffdsIGLyREP--TDEQR-ERARELLELLGL-AHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDL 207
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-236 |
2.31e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklRSKAQKQRFRRDMQMIFQDPyaslNPRMKVK 103
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLLALRQQVATVFQDP----EQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 104 DIVAE-GIDINHLAKNDADRTKQVEDLLETVglNKDHSSRYPHE-FSGGQRQRIGIARALAVQPEFIIADEPISALDVSI 181
Cdd:PRK13638 94 DIDSDiAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 182 QAQVVNLLKRLQRERDLTyLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-236 |
2.88e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqRFRRDMQMIF 89
Cdd:PRK10895 8 NLAKAyKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA---RARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDpyASLNPRMKVKDIVAEGIDINHlAKNDADRTKQVEDLLETVGLNKDHSSrYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:PRK10895 85 QE--ASIFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHIEHLRDS-MGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 170 ADEPISALDvsiQAQVVNLLKRLQRERD--LTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK10895 161 LDEPFAGVD---PISVIDIKRIIEHLRDsgLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-227 |
4.00e-20 |
|
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: 90.65 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPyaSL-Nprm 100
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV----TQASLRAAIGIVPQDT--VLfN--- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 kvkDIVAEGI-----DINHLAKNDADRTKQVEDL-------LETV----GLnkdhssryphEFSGGQRQRIGIARALAVQ 164
Cdd:COG5265 446 ---DTIAYNIaygrpDASEEEVEAAARAAQIHDFieslpdgYDTRvgerGL----------KLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 165 PEFIIADEPISALDV----SIQAQvvnlLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLE 227
Cdd:COG5265 513 PPILIFDEATSALDSrterAIQAA----LREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-234 |
4.18e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVgkadeVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQr 80
Cdd:PRK09700 6 ISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 frRDMQMIFQ-----DPYASLNP----RMKVKDIVaeGIDINHLAKndadRTKQVEDLLETVGLNKDHSSRYPhEFSGGQ 151
Cdd:PRK09700 80 --LGIGIIYQelsviDELTVLENlyigRHLTKKVC--GVNIIDWRE----MRVRAAMMLLRVGLKVDLDEKVA-NLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVKYISDRIGVMHYG-----RML 226
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGssvcsGMV 229
|
....*...
gi 2784741926 227 EIASSDEI 234
Cdd:PRK09700 230 SDVSNDDI 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-189 |
4.25e-20 |
|
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: 86.26 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFrrdmqmifqdpYAS 95
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL-----------YLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LNPRMKVKDIVAEGIDINHLAKNDADRTkqVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPIS 175
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170
....*....|....
gi 2784741926 176 ALDVSIQAQVVNLL 189
Cdd:TIGR01189 157 ALDKAGVALLAGLL 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-225 |
8.08e-20 |
|
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: 85.99 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkqRFRRDMQMIFQDPyaSLNPRmKV 102
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK----YLHSKVSLVGQEP--VLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGidinhLAKNDADRTKQVEDLLETVGLNKDHSSRYPHE-------FSGGQRQRIGIARALAVQPEFIIADEPIS 175
Cdd:cd03248 105 QDNIAYG-----LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2784741926 176 ALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRM 225
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-237 |
2.09e-19 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 88.27 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRskaqKQRFRRDMQMIFQDPyaSLNPrm 100
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD----REELGRHIGYLPQDV--ELFD-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 kvkDIVAEGIdinhlAK-NDADRTKqVEDLLETVGLnkdhssrypHEF-------------------SGGQRQRIGIARA 160
Cdd:COG4618 420 ---GTIAENI-----ARfGDADPEK-VVAAAKLAGV---------HEMilrlpdgydtrigeggarlSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKyISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-239 |
4.67e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 34 FGLvgeSGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQDpyASLNPRMKVKDIVAEGIdin 113
Cdd:PRK11144 30 FGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQD--ARLFPHYKVRGNLRYGM--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 114 hlAKNDADRTKQVEDLLetvGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQ 193
Cdd:PRK11144 102 --AKSMVAQFDKIVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2784741926 194 RERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAHPL 239
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-225 |
4.87e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKaqkQRFRR-------DMQM--IFQDPY 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA---QRLARglvylpeDRQSsgLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASLNprmkvkdIVAEGIDINHLAKNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:PRK15439 358 LAWN-------VCALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 174 ISALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-227 |
1.14e-18 |
|
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: 81.59 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRfRRDMQMIFQDPYAslnpr 99
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL----EKAL-SSLISVLNQRPYL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 mkvkdivaegidinhlakndADRTkqvedLLETVGLnkdhssryphEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:cd03247 87 --------------------FDTT-----LRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2784741926 180 SIQAQVVNLLkrLQRERDLTYLFIAHDLSMVKYIsDRIGVMHYGRMLE 227
Cdd:cd03247 132 ITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-234 |
1.37e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLkqyfNVGKAdevraVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsKLRS--KAQK 78
Cdd:COG1129 257 LEVEGL----SVGGV-----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSprDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 79 QRF------RRDmQMIFQDpyASlnprmkvkdiVAEGIDINHLAK-------NDADRTKQVEDLLETVGLnkdhssRYPH 145
Cdd:COG1129 327 AGIayvpedRKG-EGLVLD--LS----------IRENITLASLDRlsrggllDRRRERALAEEYIKRLRI------KTPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 146 ------EFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGV 219
Cdd:COG1129 388 peqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILV 466
|
250
....*....|....*
gi 2784741926 220 MHYGRMLEIASSDEI 234
Cdd:COG1129 467 MREGRIVGELDREEA 481
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-226 |
1.57e-18 |
|
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: 82.70 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 12 VGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAI---IHLYEPTSGKIIFKGEDVSKlrskaqkQRFRRDMQMI 88
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP-------DQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 89 FQDPYasLNPRMKVKDIVAEgidINHLA----KNDADRTKQVEDlletVGLNKDHSSRYPHEF----SGGQRQRIGIARA 160
Cdd:cd03234 87 RQDDI--LLPGLTVRETLTY---TAILRlprkSSDAIRKKRVED----VLLRDLALTRIGGNLvkgiSGGERRRVSIAVQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 161 LAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-207 |
3.03e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 84.72 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 12 VGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQD 91
Cdd:TIGR02868 342 AGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE----VRRRVSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 92 PY---ASL--NPRmkvkdivaegidinhLAKNDADrTKQVEDLLETVGLnKDHSSRYPH-----------EFSGGQRQRI 155
Cdd:TIGR02868 418 AHlfdTTVreNLR---------------LARPDAT-DEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 156 GIARALAVQPEFIIADEPISALDVSIQAQVVNLLkrLQRERDLTYLFIAHDL 207
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-219 |
1.45e-17 |
|
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: 80.14 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 27 DVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskaqkqrfrrdmqmiFQDPYASLNPRMKVKDIV 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------------YKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 107 AEGIDINHLA---KNDADRTKQVEDLLEtvglnkdhssRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQA 183
Cdd:cd03237 83 SSITKDFYTHpyfKTEIAKPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 2784741926 184 QVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGV 219
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-224 |
2.79e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGedvsklrskaQKQRFRRDMQ-------MIFQ 90
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG----------QEMRFASTTAalaagvaIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 DpyASLNPRMKvkdiVAEGIDINHLAK-----NDADRTKQVEDLLETVGLNKDHSSRYPHeFSGGQRQRIGIARALAVQP 165
Cdd:PRK11288 87 E--LHLVPEMT----VAENLYLGQLPHkggivNRRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 166 EFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-226 |
3.91e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskAQKQRFrrdMQMIFQDPYASLNPR 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNL---VAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGI--DINHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:PRK15056 95 VLVEDVVMMGRygHMGWLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2784741926 178 DVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIgVMHYGRML 226
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-227 |
8.29e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTT-----TGraiIHLYEPTSGKIIFKGEdvsklrskaqKQRFR--RDMQ---- 86
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTlmkvlSG---VYPHGSYEGEILFDGE----------VCRFKdiRDSEalgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 87 -MIFQD----PYASlnprmkvkdiVAEGIDI-NHLAKN---DADRT-KQVEDLLETVGLNKDHSSRYPHeFSGGQRQRIG 156
Cdd:NF040905 81 vIIHQElaliPYLS----------IAENIFLgNERAKRgviDWNETnRRARELLAKVGLDESPDTLVTD-IGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 157 IARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLE 227
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-205 |
8.83e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.62 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIifkgedvsklrskaqkqRFRRDMQMIF--QDPY---AS 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-----------------ARPAGARVLFlpQRPYlplGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LnprmkvKDIV-----AEGIDinhlaknDAdrtkQVEDLLETVGLNK-----DHSSRYPHEFSGGQRQRIGIARALAVQP 165
Cdd:COG4178 442 L------REALlypatAEAFS-------DA----ELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2784741926 166 EFIIADEPISALDVSIQAQvvnLLKRLQRE-RDLTYLFIAH 205
Cdd:COG4178 505 DWLFLDEATSALDEENEAA---LYQLLREElPGTTVISVGH 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-212 |
1.08e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 10 FNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKgeDVSKLRSKAQKQrFRRDMQMIF 89
Cdd:PTZ00265 390 FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKW-WRSKIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 QDPYA---SLNPRMK-----VKDIVA-------------EGIDINHLAK-------NDADRTKQVEDLL----------- 130
Cdd:PTZ00265 467 QDPLLfsnSIKNNIKyslysLKDLEAlsnyynedgndsqENKNKRNSCRakcagdlNDMSNTTDSNELIemrknyqtikd 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 131 -ETVGLNK-----DHSSRYPHEF-----------SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQ 193
Cdd:PTZ00265 547 sEVVDVSKkvlihDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
250
....*....|....*....
gi 2784741926 194 RERDLTYLFIAHDLSMVKY 212
Cdd:PTZ00265 627 GNENRITIIIAHRLSTIRY 645
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-223 |
1.71e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVG-KADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskaqkq 79
Cdd:COG2401 25 ERVAIVLEAFGVElRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 rFRRDmqmifqdpyASLnprmkvkdivaegidINHLAKNDAdrTKQVEDLLETVGLNKDHS-SRYPHEFSGGQRQRIGIA 158
Cdd:COG2401 96 -FGRE---------ASL---------------IDAIGRKGD--FKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 159 RALAVQPEFIIADEPISALDVSiQAQVVNL-LKRLQRERDLTYLFIAHDLSMVKYIS-DRIGVMHYG 223
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-224 |
1.79e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.31 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFnvgkaDEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrSKAQKQR 80
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDMQMIFQDpyasLNPRMKVKdivaEGIDI--NHLAKNDADRTKQVEDLLETVGLNKDHSSRYpHEFSGGQRQRIGIA 158
Cdd:PRK13537 80 QRVGVVPQFDN----LDPDFTVR----ENLLVfgRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 159 RALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-238 |
3.79e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.60 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFrrdmQMIFQDPYAslnpr 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL----AVVSQTPFL----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 mkVKDIVAEGIdinHLAKNDADRtKQVEDLLETVGLNKDhSSRYPHEF-----------SGGQRQRIGIARALAVQPEFI 168
Cdd:PRK10789 401 --FSDTVANNI---ALGRPDATQ-QEIEHVARLASVHDD-ILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 169 IADEPISALDVSIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-224 |
4.78e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskAQKQRFRRDMQMIFQdpYASLNPRM 100
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-----ARARLARARIGVVPQ--FDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDivaegidiNHLAKNDADR--TKQVE----DLLETVGLNKDHSSRYPhEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:PRK13536 130 TVRE--------NLLVFGRYFGmsTREIEavipSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2784741926 175 SALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-205 |
5.87e-16 |
|
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: 74.11 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGedvsklrskaqkqrfRRDMQMIFQDPYAslnPRM 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE---------------GEDLLFLPQRPYL---PLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAegidinhlakndadrtkqvedlletvglnkdhssrYP--HEFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:cd03223 79 TLREQLI-----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*..
gi 2784741926 179 VSIQAQVVNLLKrlqrERDLTYLFIAH 205
Cdd:cd03223 124 EESEDRLYQLLK----ELGITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-234 |
8.72e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.09 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPYA-SLNPRMKV 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF----GLTDLRRVLSIIPQSPVLfSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 kDIVAEgidinhlaKNDADRTKQvedlLETVGLnKDHSSRYP-----------HEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PLN03232 1331 -DPFSE--------HNDADLWEA----LERAHI-KDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 172 EPISALDVSIQAqvvnLLKRLQRE--RDLTYLFIAHDLSMVkYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PLN03232 1397 EATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-217 |
1.66e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIifkgEDVSKLRSKAQKQRFRRDMQM-IFQDPYASLN 97
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYLDTTLpLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAegidinhlakndADRTKQVEDLLEtvglnkdhssrYP-HEFSGGQRQRIGIARALAVQPEFIIADEPISA 176
Cdd:PRK09544 94 PGTKKEDILP------------ALKRVQAGHLID-----------APmQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2784741926 177 LDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRI 217
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-219 |
1.86e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 28 VYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKgEDVSklrSKAQkqrfrrdmqmifqdpYASLNPRMKVKDI-- 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS---YKPQ---------------YIKPDYDGTVEDLlr 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 106 -VAEGIDINHLaKNDADRTKQVEDLLEtvglnkdhssRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQ 184
Cdd:PRK13409 423 sITDDLGSSYY-KSEIIKPLQLERLLD----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*
gi 2784741926 185 VVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGV 219
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-234 |
2.47e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.25 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRfrrdMQMIFQDpyASLNPRMK 101
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR----IGLLAQN--ATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEGID-----INHLAKNDADrtkQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISA 176
Cdd:PRK10253 98 VQELVARGRYphqplFTRWRKEDEE---AVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 177 LDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-210 |
3.47e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGedvsKLRSKAQKQRFRRDMQMifqdpyaslnPr 99
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSL----------P- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGI--DINHLAKNDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:NF040873 72 LTVRDLVAMGRwaRRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|...
gi 2784741926 178 DVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMV 210
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELV 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-236 |
4.23e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 75.63 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTtgraIIHL----YEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPY-- 93
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKST----LLQLltraWDPQQGEILLNGQPIADYSEAA----LRQAISVVSQRVHlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 -ASLNPRMKvkdivaegidinhLAKNDADrTKQVEDLLETVGLNKDHSSRYP---------HEFSGGQRQRIGIARALAV 163
Cdd:PRK11160 427 sATLRDNLL-------------LAAPNAS-DEALIEVLQQVGLEKLLEDDKGlnawlgeggRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 164 QPEFIIADEPISALDVSIQAQVVNLLkrLQRERDLTYLFIAHDL----SMvkyisDRIGVMHYGRMLEIASSDEIYA 236
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLtgleQF-----DRICVMDNGQIIEQGTHQELLA 562
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-206 |
1.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIF-KGEDVSKLRskaqkqrfrrdmqmifQDPYasLNPRM 100
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP----------------QEPP--LDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAEGI--------DINHLAKNDADRTK----------------------QVEDLLETVGLNKDHSSRYPHEFSGG 150
Cdd:COG0488 77 TVLDTVLDGDaelraleaELEELEAKLAEPDEdlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 151 QRQRIGIARALAVQPEFIIADEPISALDV-SIQaqvvnLLKRLQRERDLTYLFIAHD 206
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-234 |
2.89e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPYA-------SL 96
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF----GLMDLRKVLGIIPQAPVLfsgtvrfNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 NPRMKVKDI-VAEGIDINHLakNDADRTKqvedlleTVGLNKDhSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPIS 175
Cdd:PLN03130 1334 DPFNEHNDAdLWESLERAHL--KDVIRRN-------SLGLDAE-VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 176 ALDVSIQAqvvnLLKRLQRE--RDLTYLFIAHDLSMVkyI-SDRIGVMHYGRMLEIASSDEI 234
Cdd:PLN03130 1404 AVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENL 1459
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-219 |
4.27e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.51 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 27 DVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKgedvSKLRSKAQkqRFRRDMQMIFQDPYASLNPRM----KV 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYKPQ--YISPDYDGTVEEFLRSANTDDfgssYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDINHLakndadRTKQVEDLletvglnkdhssryphefSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQ 182
Cdd:COG1245 436 KTEIIKPLGLEKL------LDKNVKDL------------------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 2784741926 183 AQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGV 219
Cdd:COG1245 492 LAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-225 |
1.71e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.62 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPT-SGKIIFKGEDVSkLRSKAQKq 79
Cdd:TIGR02633 258 LEARNLTCWDVINP--HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVD-IRNPAQA- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 rFRRDMQMIFQD-PYASLNPRMKVkdivAEGIDINHLAK-------NDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQ 151
Cdd:TIGR02633 334 -IRAGIAMVPEDrKRHGIVPILGV----GKNITLSVLKSfcfkmriDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-224 |
1.81e-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: 66.32 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKADEVRAV-DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIfkgedvsklrskaqkqrfrrdmqmif 89
Cdd:cd03221 5 NLSKTYGGKLLlKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 qdpyaslnprmkvkdiVAEGIDINHLAKndadrtkqvedlletvglnkdhssrypheFSGGQRQRIGIARALAVQPEFII 169
Cdd:cd03221 59 ----------------WGSTVKIGYFEQ-----------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLQRerdlTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-232 |
1.84e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAII-H-LYEPTSGKIIFKGEDVSKLRSKaqk 78
Cdd:CHL00131 8 LEIKNLHASVN-----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHpAYKILEGDILFKGESILDLEPE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 79 QRFRRDMQMIFQDPY------------ASLNPRMKvkdivaegidinHLAKNDADRTKQVE---DLLETVGLNKDHSSRY 143
Cdd:CHL00131 80 ERAHLGIFLAFQYPIeipgvsnadflrLAYNSKRK------------FQGLPELDPLEFLEiinEKLKLVGMDPSFLSRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 144 PHE-FSGGQRQRIGIARALAVQPEFIIADEPISALDVS---IQAQVVNLLKRLQRerdlTYLFIAHDLSMVKYIS-DRIG 218
Cdd:CHL00131 148 VNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVH 223
|
250
....*....|....
gi 2784741926 219 VMHYGRMLEIASSD 232
Cdd:CHL00131 224 VMQNGKIIKTGDAE 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-189 |
2.72e-13 |
|
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: 67.52 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFrrdmqmifqdpYASLNPRMKVK 103
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL-----------YLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 104 DIVAEGIDINHlaknDADRTKQVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQA 183
Cdd:cd03231 88 LSVLENLRFWH----ADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*.
gi 2784741926 184 QVVNLL 189
Cdd:cd03231 163 RFAEAM 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
2.79e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKAdeVRAVDditFDVYQGETFGLVGESGSGKTTTGRaiiHLYEPTSGKIIfKGEDVSKLRSKAQKQ- 79
Cdd:PRK09984 5 IRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKS-AGSHIELLGRTVQREg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 RFRRDMQ-------MIFQDpyASLNPRMKvkdiVAEGIDINHLAKNDADRT-----KQVEDLLETVGLNKDHSSRYPHE- 146
Cdd:PRK09984 76 RLARDIRksrantgYIFQQ--FNLVNRLS----VLENVLIGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAHQr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 147 ---FSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYG 223
Cdd:PRK09984 150 vstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
....*...
gi 2784741926 224 RMLEIASS 231
Cdd:PRK09984 230 HVFYDGSS 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
17-226 |
3.42e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 17 EVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPYASL 96
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW----QTAKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 NpRMKVKDIVAEGidiNHLAKNDA--DRTKQVEDLLETVglnKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPI 174
Cdd:PRK11614 93 S-RMTVEENLAMG---GFFAERDQfqERIKWVYELFPRL---HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 175 SALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-226 |
3.64e-13 |
|
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: 66.81 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAII--HLYEPTSGKIIFKGEDVSKlrskaqkQRFRRDMQMIFQDPYasLNP 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK-------RSFRKIIGYVPQDDI--LHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKdivaegidinhlakndadrtkqvEDLLETVGLNKdhssrypheFSGGQRQRIGIARALAVQPEFIIADEPISALD 178
Cdd:cd03213 96 TLTVR-----------------------ETLMFAAKLRG---------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2784741926 179 VSIQAQVVNLLKRL-QRERdlTYLFIAHDLSMVKYIS-DRIGVMHYGRML 226
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGR--TIICSIHQPSSEIFELfDKLLLLSQGRVI 191
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-227 |
6.41e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAqkqrFRRDMQMIFQDPYAS 95
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV----LRQGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LNprmKVKDIVAEGIDINHlakndadrtKQVEDLLETVGLNkDHSSRYP-----------HEFSGGQRQRIGIARALAVQ 164
Cdd:PRK10790 428 AD---TFLANVTLGRDISE---------EQVWQALETVQLA-ELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 165 PEFIIADEPISALDvSIQAQVVNLLKRLQRERDlTYLFIAHDLSMVkYISDRIGVMHYGRMLE 227
Cdd:PRK10790 495 PQILILDEATANID-SGTEQAIQQALAAVREHT-TLVVIAHRLSTI-VEADTILVLHRGQAVE 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-238 |
8.60e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHlYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPyaSLnP 98
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELREL----DPESWRKHLSWVGQNP--QL-P 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 99 RMKVKDIVAegidinhLAKNDADRTkQVEDLLE-----------TVGLN---KDHSSRypheFSGGQRQRIGIARALAVQ 164
Cdd:PRK11174 436 HGTLRDNVL-------LGNPDASDE-QLQQALEnawvseflpllPQGLDtpiGDQAAG----LSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 165 PEFIIADEPISALDVSIQAQVVNLLKRLQreRDLTYLFIAHDLSMVKYIsDRIGVMHYGRMLEIASSDEIYAHP 238
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-191 |
1.84e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrskaqkqrfrRDMQMIFQDPYasLNPRMKV 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-------------DDPDVAEACHY--LGHRNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDI--VAEGIDINHLAKNDADRtkQVEDLLETVGLnkDHSSRYP-HEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:PRK13539 85 KPAltVAENLEFWAAFLGGEEL--DIAAALEAVGL--APLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|..
gi 2784741926 180 SIQAQVVNLLKR 191
Cdd:PRK13539 161 AAVALFAELIRA 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-225 |
2.10e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrSKAQKQRFRRDMQMIFQDPYAS-LNPR 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV---TRSPQDGLANGIVYISEDRKRDgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKD---IVA------EGIDINHLAKNDAdrtkqVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIA 170
Cdd:PRK10762 345 MSVKEnmsLTAlryfsrAGGSLKHADEQQA-----VSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 171 DEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-233 |
2.31e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRfrrDMQMIFQDpyasLN 97
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA---GIGIIHQE----LN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 --PRMKVkdivAEGI-----DINHLAKNDADRTKQVEDLLETvGLNKDHSSRYP-HEFSGGQRQRIGIARALAVQPEFII 169
Cdd:PRK10762 90 liPQLTI----AENIflgreFVNRFGRIDWKKMYAEADKLLA-RLNLRFSSDKLvGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 170 ADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML---EIASSDE 233
Cdd:PRK10762 165 MDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIaerEVADLTE 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-233 |
3.91e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKADEVRaVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrSKAQKQRFRRDMQMIFQ 90
Cdd:PRK09700 270 NVTSRDRKK-VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS---PRSPLDAVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 D-------PYASLNPRMKVKDIVAEGIDINHLAK-NDADRTKQVEDLLETVGLnKDHS-SRYPHEFSGGQRQRIGIARAL 161
Cdd:PRK09700 346 SrrdngffPNFSIAQNMAISRSLKDGGYKGAMGLfHEVDEQRTAENQRELLAL-KCHSvNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 162 AVQPEFIIADEPISALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDE 233
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-225 |
1.04e-11 |
|
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: 65.81 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrsKAQKQRFRRDMQMIFQdpYASLNPR 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQ--HNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIDINHLAKNDADRtkQVEDLLETVGLNKDHSSRyPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQL--EMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2784741926 180 SIQAQVVNLLKRLQRERdlTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
31-237 |
1.04e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 63.77 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 31 GETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPYA-------SLNPRMKVK 103
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL----PLHTLRSRLSIILQDPILfsgsirfNLDPECKCT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 104 D-IVAEGIDINHLaKNDADRTKQVEDLLETVGlnkdhssryPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQ 182
Cdd:cd03288 123 DdRLWEALEIAQL-KNMVKSLPGGLDAVVTEG---------GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 183 aqvvNLLKR--LQRERDLTYLFIAHDLSMVkYISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:cd03288 193 ----NILQKvvMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-206 |
1.44e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKA-DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFkGEDVsKLRSKAQKQrfrrdmqmif 89
Cdd:COG0488 320 GLSKSyGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-KIGYFDQHQ---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 90 qdpyASLNPRMKVKDIVAEGidinhlakNDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFII 169
Cdd:COG0488 388 ----EELDPDKTVLDELRDG--------APGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190
....*....|....*....|....*....|....*...
gi 2784741926 170 ADEPISALDV-SIQAqVVNLLKrlqrERDLTYLFIAHD 206
Cdd:COG0488 456 LDEPTNHLDIeTLEA-LEEALD----DFPGTVLLVSHD 488
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-223 |
3.48e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.38 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 31 GETFGLVGESGSGKTTTGRAIIHLYEPTSGKiiFKGED-----VSKLRSKAQKQRFRR----DMQMIFQDPYASLNPRmK 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNYFTKllegDVKVIVKPQYVDLIPK-A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEGIdinhlakNDADRTKQVEDLLETVGLNKdHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSI 181
Cdd:cd03236 103 VKGKVGELL-------KKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2784741926 182 QAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMhYG 223
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL-YG 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-237 |
3.52e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 9 YFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMI 88
Cdd:PRK13545 28 FFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 89 FQDPYASLNpRMKVKDIVAEGIDInhlakndADRTKQVEDLLETvglnkdhssrypheFSGGQRQRIGIARALAVQPEFI 168
Cdd:PRK13545 108 LKGLMMGLT-KEKIKEIIPEIIEF-------ADIGKFIYQPVKT--------------YSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2784741926 169 IADEpisALDVSIQAQVVNLLKRLQ--RERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK13545 166 VIDE---ALSVGDQTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-223 |
3.87e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrSKAQKQRFrrDMQMIFQDPYasLN 97
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQL--GIYLVPQEPL--LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEGidinhLAKNdADRTKQVEDLLETVGLNKDhssryPHEFSG----GQRQRIGIARALAVQPEFIIADEP 173
Cdd:PRK15439 99 PNLSVKENILFG-----LPKR-QASMQKMKQLLAALGCQLD-----LDSSAGslevADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 174 ISALdvsIQAQVVNLLKRLQ--RERDLTYLFIAHDLSMVKYISDRIGVMHYG 223
Cdd:PRK15439 168 TASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-221 |
4.68e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMIFQD--PYASLNPRM 100
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNvnEFSLTKEGG 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKD---------IVAEGIDIN-----------------------------HLAKNDADRTK--------QVEDLLETVG 134
Cdd:PTZ00265 1266 SGEDstvfknsgkILLDGVDICdynlkdlrnlfsivsqepmlfnmsiyeniKFGKEDATREDvkrackfaAIDEFIESLP 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 135 LNKD-HSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYi 213
Cdd:PTZ00265 1346 NKYDtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1424
|
....*...
gi 2784741926 214 SDRIGVMH 221
Cdd:PTZ00265 1425 SDKIVVFN 1432
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-192 |
8.06e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSkaqkqRFRRDMQMIFQDP--Y 93
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-----EYHQDLLYLGHQPgiK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ASLNPrmkvkdivAEGIDINHLAKNDADRtKQVEDLLETVGLnkdhsSRY---P-HEFSGGQRQRIGIARALAVQPEFII 169
Cdd:PRK13538 87 TELTA--------LENLRFYQRLHGPGDD-EALWEALAQVGL-----AGFedvPvRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|...
gi 2784741926 170 ADEPISALDVsiqaQVVNLLKRL 192
Cdd:PRK13538 153 LDEPFTAIDK----QGVARLEAL 171
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-224 |
1.05e-10 |
|
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: 60.18 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEdVSklrskaqkqr 80
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 frrdmqmifqdpYASLNP---RMKVKDIVAEGidinhlAKNDADRTKQV-------EDL------LETV----GLNkdhs 140
Cdd:cd03250 70 ------------YVSQEPwiqNGTIRENILFG------KPFDEERYEKVikacalePDLeilpdgDLTEigekGIN---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 141 srypheFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVN--LLKRLQRERdlTYLFIAHDLSMVKYiSDRIG 218
Cdd:cd03250 128 ------LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIV 198
|
....*.
gi 2784741926 219 VMHYGR 224
Cdd:cd03250 199 VLDNGR 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-224 |
2.40e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 18 VRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrSKAQKQRFRRDMQMIFQDpyASLN 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID---FKSSKEALENGISMVHQE--LNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIV------AEGIDINHlaKNDADRTKQVEDLLetvGLNKDHSSRYPhEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PRK10982 86 LQRSVMDNMwlgrypTKGMFVDQ--DKMYRDTKAIFDEL---DIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGR 224
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-234 |
2.71e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSK--LRskaqkqRFRRDMQMIFQDPyaslnprMK 101
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLR------ELRRQFSMIPQDP-------VL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 102 VKDIVAEGIDiNHLAKNDAdrtkQVEDLLETVGLNKDHSSRYP----------HEFSGGQRQRIGIARALAVQPE-FIIA 170
Cdd:PTZ00243 1396 FDGTVRQNVD-PFLEASSA----EVWAALELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLKKGSgFILM 1470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 171 DEPIS----ALDVSIQAQVVNLLKrlqrerDLTYLFIAHDLSMV-KYisDRIGVMHYGRMLEIASSDEI 234
Cdd:PTZ00243 1471 DEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVaQY--DKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-225 |
2.83e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNVGKadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYE-PTSGKIIFKGEDVsKLRSKAQKq 79
Cdd:PRK13549 260 LEVRNLTAWDPVNP--HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV-KIRNPQQA- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 80 rFRRDMQMIFQDPYA-SLNPRMKVkdivAEGIDINHLAK-------NDADRTKQVEDLLETVGLNKDHSSRYPHEFSGGQ 151
Cdd:PRK13549 336 -IAQGIAMVPEDRKRdGIVPVMGV----GKNITLAALDRftggsriDDAAELKTILESIQRLKVKTASPELAIARLSGGN 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 152 RQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-196 |
3.62e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKqrfrrdmQMIFQDPYASLNPRM 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK-------QLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAegIDINHLAKNdadrtKQVEDLLETVGLnkDHSSRYP-HEFSGGQRQRIGIARALAVQPEFIIADEPISALDv 179
Cdd:PRK13540 90 TLRENCL--YDIHFSPGA-----VGITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD- 159
|
170
....*....|....*..
gi 2784741926 180 siQAQVVNLLKRLQRER 196
Cdd:PRK13540 160 --ELSLLTIITKIQEHR 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-233 |
5.63e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKqyfnvgkADEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKlrskaqkqr 80
Cdd:PRK10982 251 LEVRNLT-------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN--------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 frRDMQMIFQDPYASLNPRMKVKDIVAE-GIDINHLAKNdADRTKQVEDLLETVGLNKDHS-----------SRYPH--E 146
Cdd:PRK10982 315 --HNANEAINHGFALVTEERRSTGIYAYlDIGFNSLISN-IRNYKNKVGLLDNSRMKSDTQwvidsmrvktpGHRTQigS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 147 FSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQReRDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
....*..
gi 2784741926 227 EIASSDE 233
Cdd:PRK10982 471 GIVDTKT 477
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-225 |
5.76e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAI---IHLYEPTSGKIIFKGEDvsklrSKAQKQRFRRDMQMIFQDpyasln 97
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIP-----YKEFAEKYPGEIIYVSEE------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 prmkvkdivaegiDInHLAkndadrTKQVEDLLETVGLNKDHssRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:cd03233 92 -------------DV-HFP------TLTVRETLDFALRCKGN--EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2784741926 178 DVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKY-ISDRIGVMHYGRM 225
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGRQ 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-234 |
7.60e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSklrskaqkqrfRRDMQMifqdpyaslnpR 99
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-----------AGDIAT-----------R 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDI-----------VAEGIDIN----HLAknDADRTKQVEDLLETVGLnKDHSSRYPHEFSGGQRQRIGIARALAVQ 164
Cdd:NF033858 339 RRVGYMsqafslygeltVRQNLELHarlfHLP--AAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 165 PEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTylfIahdlsmvkYIS----------DRIGVMHYGRMLEIASSDEI 234
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVT---I--------FISthfmneaercDRISLMHAGRVLASDTPAAL 484
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-227 |
1.01e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAII--HLYEPTSGKIIFKGEDVSKLrskAQKQRFRRDMQMIFQDPY-------- 93
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLEL---SPEDRAGEGIFMAFQYPVeipgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 94 ----ASLNPRMKVKDIVA-EGIDINHLAKNDADRTKQVEDLLeTVGLNKDhssrypheFSGGQRQRIGIARALAVQPEFI 168
Cdd:PRK09580 97 fflqTALNAVRSYRGQEPlDRFDFQDLMEEKIALLKMPEDLL-TRSVNVG--------FSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 169 IADEPISALDV---SIQAQVVNLLKRLQRerdlTYLFIAHDLSMVKYIS-DRIGVMHYGRMLE 227
Cdd:PRK09580 168 ILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-237 |
1.02e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.29 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEdVSKLRSKAQKQRFRRDMQMIFQDPYASLNPR 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAGLSGQLTGIENIEFKMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 100 MKVKDIVAEGIDINHLAkndadrtkqvEDLLETVglnkdhssrypHEFSGGQRQRIGIARALAVQPEFIIADEpisALDV 179
Cdd:PRK13546 118 KEIKAMTPKIIEFSELG----------EFIYQPV-----------KKYSSGMRAKLGFSINITVNPDILVIDE---ALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 180 SIQAQVVNLLKRLQ--RERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIYAH 237
Cdd:PRK13546 174 GDQTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-236 |
1.18e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLrskaQKQRFRRDMQMIFQDPY-------AS 95
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI----GLHDLRFKITIIPQDPVlfsgslrMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LNPRMKVKD-IVAEGIDINHLakndadrtkqvEDLLETVGLNKDHS-SRYPHEFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:TIGR00957 1380 LDPFSQYSDeEVWWALELAHL-----------KTFVSALPDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 174 ISALDVS----IQAQVvnllkRLQRErDLTYLFIAHDLSMVKYISdRIGVMHYGRMLEIASSDEIYA 236
Cdd:TIGR00957 1449 TAAVDLEtdnlIQSTI-----RTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-223 |
2.29e-09 |
|
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: 56.57 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 9 YFNVGKadEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFRRDMQMI 88
Cdd:cd03290 7 YFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 89 FQDPYAsLNPrmKVKDIVAEGIDIN---HLAKNDADRTKQVEDLLeTVGLNKDHSSRYPHeFSGGQRQRIGIARALAVQP 165
Cdd:cd03290 85 AQKPWL-LNA--TVEENITFGSPFNkqrYKAVTDACSLQPDIDLL-PFGDQTEIGERGIN-LSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 166 EFIIADEPISALDVSIQAQVVN--LLKRLQRERDlTYLFIAHDLSMVKYiSDRIGVMHYG 223
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
146-221 |
3.25e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.27 E-value: 3.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784741926 146 EFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMH 221
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-192 |
3.97e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.36 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 29 YQGETFGLVGESGSGKTTTGRAIIHLYEP---TSGKIIFKGEdvsklrsKAQKQRFRR--------DM---------QMI 88
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM-------PIDAKEMRAisayvqqdDLfiptltvreHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 89 FQdpyASLnpRMKvkdivaegidiNHLAKNDadRTKQVEDLLETVGLNKDHSSRYPHE-----FSGGQRQRIGIARALAV 163
Cdd:TIGR00955 122 FQ---AHL--RMP-----------RRVTKKE--KRERVDEVLQALGLRKCANTRIGVPgrvkgLSGGERKRLAFASELLT 183
|
170 180
....*....|....*....|....*....
gi 2784741926 164 QPEFIIADEPISALDVSIQAQVVNLLKRL 192
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-234 |
4.19e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYePTSGKIIFKGEDVSKLRSK---------AQKQRFRRDMQmIFQdpYA 94
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarhraylSQQQTPPFAMP-VFQ--YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 SLnprmkvkdivaegidinHLAK--NDADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARA-LAVQPE----- 166
Cdd:PRK03695 91 TL-----------------HQPDktRTEAVASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpag 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2784741926 167 -FIIADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:PRK03695 153 qLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-228 |
4.78e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 20 AVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVsklrSKAQKQRFRRDMQMIFQDPY---ASL 96
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV----TAEQPEDYRKLFSAVFTDFHlfdQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 NPRMKVKDivaegidinhlakndadrTKQVEDLLETVGLN-----KDHSSRYPhEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PRK10522 414 GPEGKPAN------------------PALVEKWLERLKMAhklelEDGRISNL-KLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 172 EpiSALDVSIQAQVV---NLLKRLqRERDLTYLFIAHDLSmvkYI--SDRIGVMHYGRMLEI 228
Cdd:PRK10522 475 E--WAADQDPHFRREfyqVLLPLL-QEMGKTIFAISHDDH---YFihADRLLEMRNGQLSEL 530
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
4.97e-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: 54.30 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 30 QGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFkgedvsklrskaqkqrfrrdmqmifqdpyaslnprmkvkdivaeg 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 110 IDINHLAKNDADRtkqvedlletvgLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQV---- 185
Cdd:smart00382 36 IDGEDILEEVLDQ------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllle 103
|
170 180
....*....|....*....|..
gi 2784741926 186 -VNLLKRLQRERDLTYLFIAHD 206
Cdd:smart00382 104 eLRLLLLLKSEKNLTVILTTND 125
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-179 |
5.39e-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: 56.87 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkaDEVrAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFkGEDVsKLRSKAQKqr 80
Cdd:TIGR03719 323 IEAENLTKAFG----DKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-KLAYVDQS-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 frRDmqmifqdpyaSLNPRMKVKDIVAEGIDINHLAKND--------------ADRTKQVEDLletvglnkdhssryphe 146
Cdd:TIGR03719 394 --RD----------ALDPNKTVWEEISGGLDIIKLGKREipsrayvgrfnfkgSDQQKKVGQL----------------- 444
|
170 180 190
....*....|....*....|....*....|...
gi 2784741926 147 fSGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:TIGR03719 445 -SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-234 |
7.15e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 1 MEVEHLKQYFNvgkadEVRAVDDITFDVYQGETFGLVGESGSGKTTtGRAIIHLYEPTSGKIIFKGEDVSklrskAQKQR 80
Cdd:NF000106 14 VEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWC-----ANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 81 FRRDM---QMIFQDPYASLNPRMKVKdIVAEGIDinhLAKNDAdrTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGI 157
Cdd:NF000106 83 LRRTIg*hRPVR*GRRESFSGRENLY-MIGR*LD---LSRKDA--RARADELLERFSLT-EAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 158 ARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEI 234
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-226 |
1.03e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 19 RAVDDITFDVYQGETFGLVGESGSGKTTTGRAII-HLYEPT-------SGKIIFKGEDVSKLRSKaQKQRFRRDMQMIFQ 90
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAP-RLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 DPYAslnprMKVKDIVAEGI--------DINHLAKNDADRTKQVEDLLETVGlnkdhssRYPHEFSGGQRQRIGIARALA 162
Cdd:PRK13547 94 PAFA-----FSAREIVLLGRypharragALTHRDGEIAWQALALAGATALVG-------RDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784741926 163 ---------VQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:PRK13547 162 qlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-270 |
1.24e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 26 FDVYQGETFGLVGESGSGKTTTGRAIihlyeptSGKII-FKGEDVSklrskaqkqRFRR-------DMQMIFQDPYASLN 97
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARAL-------AGELPlLSGERQS---------QFSHitrlsfeQLQKLVSDEWQRNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKD------IVAEGIDINHlakNDADRTKQvedLLETVGLNKDHSSRYPHeFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PRK10938 88 TDMLSPGeddtgrTTAEIIQDEV---KDPARCEQ---LAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVM------HYGRMLEIAsSDEIYAHPLHdytAS 245
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLadctlaETGEREEIL-QQALVAQLAH---SE 235
|
250 260
....*....|....*....|....*
gi 2784741926 246 LLSAVPVPDPEYERARQQIPYDPSR 270
Cdd:PRK10938 236 QLEGVQLPEPDEPSARHALPANEPR 260
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
120-223 |
1.31e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 120 ADRTKQVEDLLETVGLNK--DHSSRyphEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERd 197
Cdd:PRK13409 187 VDERGKLDEVVERLGLENilDRDIS---ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK- 262
|
90 100
....*....|....*....|....*.
gi 2784741926 198 lTYLFIAHDLSMVKYISDRIGVMhYG 223
Cdd:PRK13409 263 -YVLVVEHDLAVLDYLADNVHIA-YG 286
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-223 |
1.40e-08 |
|
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: 55.56 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 30 QGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIifkGEDVSKlrsKAQKQRFRR-DMQMIFQDPY-----ASLNPRM--- 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSW---DEVLKRFRGtELQDYFKKLAngeikVAHKPQYvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 -------KVKDIvaegidinhLAKndADRTKQVEDLLETVGLNK--DHSSRyphEFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:COG1245 172 ipkvfkgTVREL---------LEK--VDERGKLDELAEKLGLENilDRDIS---ELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 172 EPISALDVSIQAQVVNLLKRLQRErDLTYLFIAHDLSMVKYISDRIGVMhYG 223
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL-YG 287
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-250 |
2.77e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYePTSGKIIFKGEDVSKLrSKAQKQRFR---RDMQM------IFQdpYA 94
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRaylSQQQSppfampVFQ--YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 95 SLnprmkvkdivaegidinHLAKN--DADRTKQVEDLLETVGLNkDHSSRYPHEFSGGQRQRIGIARAL-----AVQPE- 166
Cdd:COG4138 91 AL-----------------HQPAGasSEAVEQLLAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 167 -FIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIAHDLSMVKYISDRIGVMHYGRMLEIASSDEIyahplhdYTAS 245
Cdd:COG4138 153 qLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV-------MTPE 224
|
....*
gi 2784741926 246 LLSAV 250
Cdd:COG4138 225 NLSEV 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-236 |
4.53e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 16 DEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEdVSKLRSKAQKQRFRRDMQMIFQDPyas 95
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAWIQNDSLRENILFGKA--- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 96 LNPRMKVKDIVAEGI--DINHLAknDADRTKQVEDlletvGLNkdhssrypheFSGGQRQRIGIARALAVQPEFIIADEP 173
Cdd:TIGR00957 725 LNEKYYQQVLEACALlpDLEILP--SGDRTEIGEK-----GVN----------LSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784741926 174 ISALDVSIQAQVV-NLLKRLQRERDLTYLFIAHDLSMVKYIsDRIGVMHYGRMLEIASSDEIYA 236
Cdd:TIGR00957 788 LSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-225 |
5.15e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSkLRSKaqKQRFRRDMQMIFQD-------PYASl 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSP--RDAIRAGIMLCPEDrkaegiiPVHS- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 97 nprmkvkdiVAEGIDI----NHL-AKNDADRTKQVEDLLETVG-LN-KDHSSRYPHEF-SGGQRQRIGIARALAVQPEFI 168
Cdd:PRK11288 348 ---------VADNINIsarrHHLrAGCLINNRWEAENADRFIRsLNiKTPSREQLIMNlSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2784741926 169 IADEPISALDVSIQAQVVNLLKRLQrERDLTYLFIAHDLSMVKYISDRIGVMHYGRM 225
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-226 |
6.92e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 31 GETFGLVGESGSGKTTTGRAI---IHLYEPTsGKIIFKGEdvsklrsKAQKQRFRRdMQMIFQDPYasLNPRMKVKD--I 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALagrIQGNNFT-GTILANNR-------KPTKQILKR-TGFVTQDDI--LYPHLTVREtlV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 106 VAEGIDI-NHLAKNDadRTKQVEDLLETVGLNKDHSSRYPHEF----SGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:PLN03211 163 FCSLLRLpKSLTKQE--KILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2784741926 181 IQAQVVNLLKRLQRERDLTYLFIAHDLSMVKYISDRIGVMHYGRML 226
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
224-289 |
9.03e-08 |
|
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: 48.90 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 224 RMLEIASSDEIYAHPLHDYTASLLSAVPVP-DPEYERAR--QQIPyDPSREFDG----------------KPRQLVEIVP 284
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRDRKLISipGEVP-SLINLPSGcrfyprcpyaqdecrkEPPALVEIAE 79
|
....*
gi 2784741926 285 HHWVR 289
Cdd:TIGR01727 80 GHRVA 84
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
148-234 |
4.13e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 148 SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNllKRLQRE-RDLTYLFIAHDLSMVKYIsDRIGVMHYGRML 226
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
....*...
gi 2784741926 227 EIASSDEI 234
Cdd:PLN03130 819 EEGTYEEL 826
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-212 |
6.66e-07 |
|
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: 50.52 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYePTSGKiifkgedvskLRSKAQKQRfrrdMQMIFQDPYASLN--- 97
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGG----------RLTKPAKGK----LFYVPQRPYMTLGtlr 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 -----PrMKVKDIVAEGIdinhlakNDADRTK-----QVEDLLE-TVGLnkDHSSRYPHEFSGGQRQRIGIARALAVQPE 166
Cdd:TIGR00954 533 dqiiyP-DSSEDMKRRGL-------SDKDLEQildnvQLTHILErEGGW--SAVQDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2784741926 167 FIIADEPISALDVSIQAQVVNLLKRLqrerDLTYLFIAHDLSMVKY 212
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSHRKSLWKY 644
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-217 |
9.25e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAI---IHLYEptsGKIIFKGE-DVSKLRskaqkqrfrrdmqmifQDPyasln 97
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILngeVLLDD---GRIIYEQDlIVARLQ----------------QDP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRM---KVKDIVAEGI-----------DINHLAKND-ADRT--------------------KQVEDLLETVGLNKDHSSR 142
Cdd:PRK11147 76 PRNvegTVYDFVAEGIeeqaeylkryhDISHLVETDpSEKNlnelaklqeqldhhnlwqleNRINEVLAQLGLDPDAALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2784741926 143 yphEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRerdlTYLFIAHDLSMVKYISDRI 217
Cdd:PRK11147 156 ---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-179 |
1.08e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 21 VDDITFDVYQGETFGLVGESGSGKTTTGRAI-IHLYE--PTSGKII-----FKGEDVSKL---------RSKAQKQRFR- 82
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMaMHAIDgiPKNCQILhveqeVVGDDTTALqcvlntdieRTQLLEEEAQl 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 83 RDMQMIFQDPYASLNPRMKVKDivaeGIDINHLAKNDADRTKQVE------------DLLETVGLNKDHSSRYPHEFSGG 150
Cdd:PLN03073 273 VAQQRELEFETETGKGKGANKD----GVDKDAVSQRLEEIYKRLElidaytaearaaSILAGLSFTPEMQVKATKTFSGG 348
|
170 180
....*....|....*....|....*....
gi 2784741926 151 QRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-217 |
1.13e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 11 NVGKAdEVRAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIhlyeptsgkiifkgEDVSKLRSKAQKQRFRRDmQMIFQ 90
Cdd:cd03238 2 TVSGA-NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL--------------YASGKARLISFLPKFSRN-KLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 91 DPYASLnprmkvkdivaegIDINhlakndadrtkqvedlLETVGLNKDHSSrypheFSGGQRQRIGIARALAVQPE---F 167
Cdd:cd03238 66 DQLQFL-------------IDVG----------------LGYLTLGQKLST-----LSGGELQRVKLASELFSEPPgtlF 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 168 IIaDEPISALDVSIQAQVVNLLKRLqreRDL--TYLFIAHDLSMVKYiSDRI 217
Cdd:cd03238 112 IL-DEPSTGLHQQDINQLLEVIKGL---IDLgnTVILIEHNLDVLSS-ADWI 158
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-259 |
1.22e-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: 49.91 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGedvsklrskaqkqrfrrdmQMIFQDPYASLNPRMkV 102
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------------RISFSPQTSWIMPGT-I 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDINHLAKNDADRTKQVEDLLeTVGLNKDHSSRYPH--EFSGGQRQRIGIARALAVQPEFIIADEPISALDVS 180
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQLEEDI-ALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 181 IQAQVVN--LLKRLQRErdlTYLFIAHDLSMVKYiSDRIGVMHYGRMLEIASSDEIYA-HPlhDYTASLLSAVPVPDPEY 257
Cdd:TIGR01271 583 TEKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAkRP--DFSSLLLGLEAFDNFSA 656
|
..
gi 2784741926 258 ER 259
Cdd:TIGR01271 657 ER 658
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-223 |
2.85e-06 |
|
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: 47.93 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGE-----DVSKLRSKAQKQrfrrdmQMIFQDPYASLN 97
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssQFSWIMPGTIKE------NIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 98 PRMKVKDIVAEGiDINHLAKNDadrtkqvEDLLETVGLNkdhssrypheFSGGQRQRIGIARALAVQPEFIIADEPISAL 177
Cdd:cd03291 129 YKSVVKACQLEE-DITKFPEKD-------NTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2784741926 178 DVSIQAQVV-NLLKRLQRERdlTYLFIAHDLSMVKyISDRIGVMHYG 223
Cdd:cd03291 191 DVFTEKEIFeSCVCKLMANK--TRILVTSKMEHLK-KADKILILHEG 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-172 |
4.63e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.87 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 24 ITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKGEDVSKLRSKAQKQRFrrdmQMIFQDPYasLNPRMkvk 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLF----SAVFSDFH--LFDRL--- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 104 divaegidinhLAKNDADRTKQVEDLLETVGLnkDH---------SSRyphEFSGGQRQRIGIARALAVQPEFIIADE 172
Cdd:COG4615 422 -----------LGLDGEADPARARELLERLEL--DHkvsvedgrfSTT---DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-179 |
5.42e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYFNvgkaDEVrAVDDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFkGEDVsKLRSKAQKqrf 81
Cdd:PRK11819 326 EAENLSKSFG----DRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-KLAYVDQS--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 82 rRDmqmifqdpyaSLNPRMKVKDIVAEGIDINHLAKND--------------ADRTKQVEDLletvglnkdhssryphef 147
Cdd:PRK11819 396 -RD----------ALDPNKTVWEEISGGLDIIKVGNREipsrayvgrfnfkgGDQQKKVGVL------------------ 446
|
170 180 190
....*....|....*....|....*....|..
gi 2784741926 148 SGGQRQRIGIARALAVQPEFIIADEPISALDV 179
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-206 |
6.36e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.62 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 22 DDITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIF-KGEDVSKLRskaqkqrfrrdmqmifQDPYasLNPRM 100
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYLP----------------QEPQ--LDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 101 KVKDIVAEGI-DINHL-----------AKNDADRTK------QVEDLLETVGL-NKD-------HSSRYP------HEFS 148
Cdd:TIGR03719 84 TVRENVEEGVaEIKDAldrfneisakyAEPDADFDKlaaeqaELQEIIDAADAwDLDsqleiamDALRCPpwdadvTKLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 149 GGQRQRIGIARALAVQPEFIIADEPISALDvsiqAQVVNLLKRLQRERDLTYLFIAHD 206
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
227-276 |
8.01e-06 |
|
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: 42.77 E-value: 8.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2784741926 227 EIASSDEIYAHPLHDYTASLLSAVPVPDPEYER--ARQQIPYDPSREFDGKP 276
Cdd:pfam08352 2 EEGPTDDILENPLHPYTRALLNSVPRLDPPKRPlyTIPGNVPSLLELPEGCP 53
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
148-187 |
3.71e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 3.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2784741926 148 SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVN 187
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
148-310 |
1.16e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 148 SGGQRQRIGIARALAVQPEFIIADEPISALDVSIQAQVVNLLKRLQRERDLTYLFIAHDLSMVKY-ISDRIGVMHYGRML 226
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 227 EIASSDEI--------YAHPLHDYTASLLSAVPVPD-----PEYERARQQIPYDPSREFDGKP--RQLVEIVPHHWVRAS 291
Cdd:TIGR00956 291 YFGPADKAkqyfekmgFKCPDRQTTADFLTSLTSPAerqikPGYEKKVPRTPQEFETYWRNSPeyAQLMKEIDEYLDRCS 370
|
170 180
....*....|....*....|.
gi 2784741926 292 E-DEIPMYKK-RAQEHSRLVK 310
Cdd:TIGR00956 371 EsDTKEAYREsHVAKQSKRTR 391
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-237 |
2.90e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 23 DITFDVYQGETFGLVGESGSGKTTTGRAIIHLYEPTSGKIIFKgedvsklrskaqkqrfrRDMQMIFQDPYAsLNPRMKV 102
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------------RSIAYVPQQAWI-MNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 103 KDIVAEGIDINHLAknDADRTKQVE-DL------LET----VGLNkdhssrypheFSGGQRQRIGIARALAVQPEFIIAD 171
Cdd:PTZ00243 740 NILFFDEEDAARLA--DAVRVSQLEaDLaqlgggLETeigeKGVN----------LSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 172 EPISALDVSIQAQVVN--LLKRLqreRDLTYLFIAHDLSMVKYiSDRIGVMHYGRmLEIASSDEIYAH 237
Cdd:PTZ00243 808 DPLSALDAHVGERVVEecFLGAL---AGKTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSADFMR 870
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-193 |
3.17e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 2 EVEHLKQYfnvgkadevRAVDDITFDvyqGETFGLVGESGSGKTTTGRAIIH-LYEPTSGK------IIFKGEDVSK--- 71
Cdd:COG0419 6 RLENFRSY---------RDTETIDFD---DGLNLIVGPNGAGKSTILEAIRYaLYGKARSRsklrsdLINVGSEEASvel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 72 -LRSKAQKQRFRR---DMQMIFQDPYASLnprmkvKDIVAE--GIDI-----NHLAKNDADRTKQVEDLLETVGLNKDHS 140
Cdd:COG0419 74 eFEHGGKRYRIERrqgEFAEFLEAKPSER------KEALKRllGLEIyeelkERLKELEEALESALEELAELQKLKQEIL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784741926 141 SRY-----PHEFSGGQRQRIGIARALAvqpefIIADepISALDVSIQAQVVNLLKRLQ 193
Cdd:COG0419 148 AQLsgldpIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
129-217 |
4.10e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 129 LLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQPEFIIADEPISALDVSiqaqVVNLLKRLQRERDLTYLFIAHDLS 208
Cdd:PRK10636 132 LLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD----AVIWLEKWLKSYQGTLILISHDRD 207
|
....*....
gi 2784741926 209 MVKYISDRI 217
Cdd:PRK10636 208 FLDPIVDKI 216
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
148-223 |
4.81e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.95 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 148 SGGQRQRIGIARALA---VQPE-FIIADEPISALDVSIQAQVVNLLKRlQRERDLTYLFIAHDLSMVKyISD---RIGVM 220
Cdd:cd03227 79 SGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAE-LADkliHIKKV 156
|
...
gi 2784741926 221 HYG 223
Cdd:cd03227 157 ITG 159
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
128-215 |
9.88e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 36.82 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784741926 128 DLLETVGLNKDHSSRYPHEFSGGQRQRIGIARALAVQ---PEFIIADEPISALDVSIQAQVVNLLKRLqRERDLTYLFIA 204
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIE 229
|
90
....*....|....
gi 2784741926 205 HDLSMVK---YISD 215
Cdd:cd03271 230 HNLDVIKcadWIID 243
|
|
| |
