|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-333 |
0e+00 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 781.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 5 AEKKVLLEIADLKVHFNIKDGRQWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLG 84
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 85 RDLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEF 164
Cdd:PRK15079 83 KDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 245 LGTYSEVYNNPQHPYTRALMSAVPIPDPDREKNKEIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGGFRHA 324
Cdd:PRK15079 243 LGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHA 322
|
....*....
gi 1799545459 325 VSCLKVDPL 333
Cdd:PRK15079 323 VSCLKVDPL 331
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-327 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 550.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 4 VAEKKVLLEIADLKVHFNIKDGrqWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWL 83
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGG--LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 84 GRDLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHE 163
Cdd:COG4608 79 GQDITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLR-IHGLASKAERRERVAELLELVGLRPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 164 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 244 ELGTYSEVYNNPQHPYTRALMSAVPIPDPDREKNKeiQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLL-EGGFR 322
Cdd:COG4608 238 EIAPRDELYARPLHPYTQALLSAVPVPDPERRRER--IVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLrEVGPG 315
|
....*
gi 1799545459 323 HAVSC 327
Cdd:COG4608 316 HQVAC 320
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-332 |
7.13e-180 |
|
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: 499.96 E-value: 7.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA---TEGRVAWLGRD 86
Cdd:COG0444 1 LLEVRNLKVYFPTRRG---------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 87 LLGQSEEEWRKAR-SDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGLLP--NLINRYPHE 163
Cdd:COG0444 72 LLKLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLR-IHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 164 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 244 ELGTYSEVYNNPQHPYTRALMSAVPIPDPDREknkEIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRP-LLEGGFR 322
Cdd:COG0444 231 EEGPVEELFENPRHPYTRALLSSIPRLDPDGR---RLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPpLREVGPG 307
|
330
....*....|
gi 1799545459 323 HAVSCLKVDP 332
Cdd:COG0444 308 HRVACHLYEE 317
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-331 |
1.11e-151 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 429.00 E-value: 1.11e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 8 KVLLEIADLKVHFNIKDGrqwFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDL 87
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRG---LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 88 LGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGG 167
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLI-NTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 248 YSEVYNNPQHPYTRALMSAVPIPDPDREKNKEiqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGGFRHAVSC 327
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPDDRRERI--KLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVAC 316
|
....
gi 1799545459 328 LKVD 331
Cdd:PRK11308 317 FAVE 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-271 |
5.10e-150 |
|
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: 432.19 E-value: 5.10e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 3 AVAEKKVLLEIADLKVHFNIKdgRQWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVAW 82
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFPIK--RGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 83 LGRDLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPH 162
Cdd:COG4172 345 DGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
250 260
....*....|....*....|....*....
gi 1799545459 243 VELGTYSEVYNNPQHPYTRALMSAVPIPD 271
Cdd:COG4172 505 VEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-273 |
6.18e-147 |
|
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: 423.93 E-value: 6.18e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 3 AVAEKKVLLEIADLKVHFNIKdgrqwfwqPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAW 82
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVR--------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 83 LGRDLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPH 162
Cdd:COG1123 325 DGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLR-LHGLLSRAERRERVAELLERVGLPPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
250 260 270
....*....|....*....|....*....|.
gi 1799545459 243 VELGTYSEVYNNPQHPYTRALMSAVPIPDPD 273
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-246 |
2.98e-122 |
|
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: 350.27 E-value: 2.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGRQwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSV---------KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-269 |
1.26e-114 |
|
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: 331.77 E-value: 1.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGRQwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlg 89
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV---------PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 qSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHpsmpRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:COG1124 70 -TRRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYS 249
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250 260
....*....|....*....|
gi 1799545459 250 EVYNNPQHPYTRALMSAVPI 269
Cdd:COG1124 225 DLLAGPKHPYTRELLAASLA 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-286 |
6.92e-106 |
|
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: 319.71 E-value: 6.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNikdgrqwfwQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL----VKATEGRVAWLGR 85
Cdd:COG4172 6 LLSVEDLSVAFG---------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 DLLGQSEEEWRKAR-SDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPSMPRQEVKDRVKTMMMKVGLlPN---LINRYP 161
Cdd:COG4172 77 DLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRL-HRGLSGAAARARALELLERVGI-PDperRLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1799545459 242 AVELGTYSEVYNNPQHPYTRALMSAVPIPDPDREKNKEIQLLEGE 286
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-324 |
2.23e-96 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 297.92 E-value: 2.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 2 NAVAEKKVLLEIADLKVHFNIKDGrqWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVA 81
Cdd:PRK10261 305 DTVVDGEPILQVRNLVTRFPLRSG--LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEII 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 82 WLGRDLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPSMPRQEVKDRVKTMMMKVGLLPNLINRYP 161
Cdd:PRK10261 383 FNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRV-HGLLPGKAAAARVAWLLERVGLLPEHAWRYP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 242 AVELGTYSEVYNNPQHPYTRALMSAVPIPDPDREKNKEIqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGGF 321
Cdd:PRK10261 542 IVEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRV-LLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAF 620
|
...
gi 1799545459 322 RHA 324
Cdd:PRK10261 621 MRR 623
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
10-266 |
5.86e-94 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 280.19 E-value: 5.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGrqWFWQpaKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:COG4167 4 LLEVRNLSKTFKYRTG--LFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSeeewRKARS-DIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQ 168
Cdd:COG4167 80 GD----YKYRCkHIRMIFQDPNTSLNPRLNIGQILEEPLR-LNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 169 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 248
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*...
gi 1799545459 249 SEVYNNPQHPYTRALMSA 266
Cdd:COG4167 235 AEVFANPQHEVTKRLIES 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-329 |
3.74e-91 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 275.45 E-value: 3.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 1 MNAVAEKKVLLEIADLKVHFNIKDGrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA---TE 77
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDG---------DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 78 GRVAWLGRDLLGQSEEEWRKARSD-IQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQE-VKDRVKtmMMKVGLLPN 155
Cdd:PRK09473 74 GSATFNGREILNLPEKELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLM-LHKGMSKAEaFEESVR--MLDAVKMPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 156 L---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 232
Cdd:PRK09473 151 ArkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 233 RVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVPIPDPDREKNKEIQlleGELPSPINPPSGCVFRTRCPIAGPECAK 312
Cdd:PRK09473 231 KVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIP---GNPPNLLRLPKGCPFQPRCPHAMEICSS 307
|
330
....*....|....*..
gi 1799545459 313 TRPLLEGGFRHAVSCLK 329
Cdd:PRK09473 308 APPLEEFGPGRLRACFK 324
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-275 |
6.64e-83 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 259.84 E-value: 6.64e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFnikdgrqwfwqPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAT---EGRVAWLGRD 86
Cdd:COG1123 4 LLEVRDLSVRY-----------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 87 LLGQSEEEWRKarsDIQMIFQDPLASLNPrMTIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSG 166
Cdd:COG1123 73 LLELSEALRGR---RIGMVFQDPMTQLNP-VTVGDQIAEALEN--LGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260
....*....|....*....|....*....
gi 1799545459 247 TYSEVYNNPQhpytraLMSAVPIPDPDRE 275
Cdd:COG1123 226 PPEEILAAPQ------ALAAVPRLGAARG 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-327 |
5.53e-80 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 246.58 E-value: 5.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNikDGRQWFwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV----KATEGRVAWLGR 85
Cdd:PRK11022 3 LLNVDKLSVHFG--DESAPF-------RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 DLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPSMPRQEVKDRVKTMMMKVGLlPNLINR---YP 161
Cdd:PRK11022 74 DLQRISEKERRNlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKV-HQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 242 AVELGTYSEVYNNPQHPYTRALMSAVPIPDPDREKnkeIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGGF 321
Cdd:PRK11022 232 VVETGKAHDIFRAPRHPYTQALLRALPEFAQDKAR---LASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA 308
|
....*.
gi 1799545459 322 RHAVSC 327
Cdd:PRK11022 309 GRQSKC 314
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-279 |
1.55e-75 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 233.04 E-value: 1.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 32 PAKTLkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDPLA 111
Cdd:PRK10419 23 QHQTV--LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRMTIGDIIAEPLRtyH-PSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK10419 101 AVNPRKTVREIIREPLR--HlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNpQHPYTRALMSAVPIP 270
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGRVLQNAVLPA 257
|
....*....
gi 1799545459 271 DPDREKNKE 279
Cdd:PRK10419 258 FPVRRRTTE 266
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-327 |
2.31e-75 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 234.80 E-value: 2.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGRqwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK----ATEGRVAWLGR 85
Cdd:COG4170 3 LLDIRNLTIEIDTPQGR---------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 DLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGDIIAEplrtyhpSMP-----------RQEVKDRVKTMMMKVGLL 153
Cdd:COG4170 74 DLLKLSPRERRKiIGREIAMIFQEPSSCLDPSAKIGDQLIE-------AIPswtfkgkwwqrFKWRKKRAIELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 154 PN--LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS 231
Cdd:COG4170 147 DHkdIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 232 DRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVPIPDPDREKNKEIQLLEGELPSPINPPSGCVFRTRCPIAGPECA 311
Cdd:COG4170 227 DTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCV 306
|
330
....*....|....*.
gi 1799545459 312 KTrPLLEGGFRHAVSC 327
Cdd:COG4170 307 ET-PRLRKIKGHEFAC 321
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-265 |
3.45e-75 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 240.38 E-value: 3.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGrqWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVAWLGRDLLG 89
Cdd:PRK15134 275 LLDVEQLQVAFPIRKG--ILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:PRK15134 352 LNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYS 249
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE 511
|
250
....*....|....*.
gi 1799545459 250 EVYNNPQHPYTRALMS 265
Cdd:PRK15134 512 RVFAAPQQEYTRQLLA 527
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-274 |
1.45e-74 |
|
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: 230.46 E-value: 1.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLkVHFNIKDGRQWFWQPAKTLkavDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:TIGR02769 2 LLEVRDV-THTYRTGGLFGAKQRAPVL---TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHpSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:TIGR02769 78 LDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLT-SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYS 249
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
|
250 260
....*....|....*....|....*
gi 1799545459 250 EVYNNpQHPYTRALMSAVPIPDPDR 274
Cdd:TIGR02769 237 QLLSF-KHPAGRNLQSAVLPEHPVR 260
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
29-286 |
7.49e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.11 E-value: 7.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQD 108
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 plASLNPRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:COG1135 91 --FNLLSSRTVAENVALPLE--IAGVPKAEIRKRVAELLELVG-LSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 189 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVP 268
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVL 245
|
250
....*....|....*...
gi 1799545459 269 IPDPDREKNKEIQLLEGE 286
Cdd:COG1135 246 NDELPEELLARLREAAGG 263
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-256 |
2.01e-68 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 213.60 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 21 NIKDGRQWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARS 100
Cdd:cd03258 3 ELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 101 DIQMIFQ--DPLASLnprmTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARAL 178
Cdd:cd03258 83 RIGMIFQhfNLLSSR----TVFENVALPLEIAG--VPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 179 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-266 |
3.53e-68 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 214.27 E-value: 3.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 8 KVLLEIADLKVHFNIKDGrqWFWQpaKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDL 87
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTG--WFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 88 lGQSEEEWRKARsdIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGG 167
Cdd:PRK15112 78 -HFGDYSYRSQR--IRMIFQDPSTSLNPRQRISQILDFPLR-LNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*....
gi 1799545459 248 YSEVYNNPQHPYTRALMSA 266
Cdd:PRK15112 234 TADVLASPLHELTKRLIAG 252
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-267 |
1.77e-67 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 212.37 E-value: 1.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 1 MNAVAEKkvLLEIADLKVHFNIKDGRQWfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV 80
Cdd:COG4107 1 MTNEEQP--LLSVRGLSKRYGPGCGTVV---------ACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 81 AWLGR-----DLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGDIIAEPL-----RTYhpsmprQEVKDRVKTMMMK 149
Cdd:COG4107 70 YYRDRdggprDLFALSEAERRRlRRTDWGMVYQNPRDGLRMDVSAGGNIAERLmaageRHY------GDIRARALEWLER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 150 VGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 229
Cdd:COG4107 144 VEIPLERIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRL 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 1799545459 230 ISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAV 267
Cdd:COG4107 224 LADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-268 |
1.84e-67 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 222.42 E-value: 1.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVA----WLGR------DLLGQSEEEWRKA 98
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmLLRRrsrqviELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 99 R-SDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGL--LPNLINRYPHEFSGGQCQRIGIA 175
Cdd:PRK10261 102 RgADMAMIFQEPMTSLNPVFTVGEQIAESIR-LHQGASREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 176 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
250
....*....|...
gi 1799545459 256 QHPYTRALMSAVP 268
Cdd:PRK10261 261 QHPYTRALLAAVP 273
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
40-262 |
7.10e-67 |
|
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: 209.84 E-value: 7.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDP--LASlnprM 117
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQGGalFDS----L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:COG1127 98 TVFENVAFPLR-EHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPqHPYTRA 262
Cdd:COG1127 176 TSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-273 |
1.49e-65 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 215.34 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNikdgrqwfwQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL-----VKATEGRVAWLG 84
Cdd:PRK15134 5 LLAIENLSVAFR---------QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 85 RDLLGQSEEEWRKARSD-IQMIFQDPLASLNPRMTIGDIIAEPLrTYHPSMPRQEVKDRVKTMMMKVGL--LPNLINRYP 161
Cdd:PRK15134 76 ESLLHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVL-SLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|..
gi 1799545459 242 AVELGTYSEVYNNPQHPYTRALMSAVPIPDPD 273
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
29-267 |
1.74e-65 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 209.66 E-value: 1.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQ- 107
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 -DPLASlnprMTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:PRK11153 91 fNLLSS----RTVFDNVALPLELAG--TPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSA 266
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
.
gi 1799545459 267 V 267
Cdd:PRK11153 244 T 244
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
40-261 |
2.93e-61 |
|
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: 195.41 E-value: 2.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDplASLNPRMTI 119
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS--GALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEPLRtYHPSMPRQEVKDRVktmMMK---VGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03261 95 FENVAFPLR-EHTRLSEEEIREIV---LEKleaVG-LRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNpQHPYTR 261
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVR 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-259 |
1.01e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.01 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 7 KKVLLEIADLKVHFNikdgrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRD 86
Cdd:COG3842 2 AMPALELENVSKRYG-------------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 87 LLGQSEEEwrkaRsDIQMIFQDPlaSLNPRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSG 166
Cdd:COG3842 69 VTGLPPEK----R-NVGMVFQDY--ALFPHLTVAENVAFGLR--MRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD----LAvvkhISDRVLVMYLGHA 242
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRI 214
|
250
....*....|....*..
gi 1799545459 243 VELGTYSEVYNNPQHPY 259
Cdd:COG3842 215 EQVGTPEEIYERPATRF 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-327 |
4.62e-59 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 193.10 E-value: 4.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDGrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK----ATEGRVAWLGR 85
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG---------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 DLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGD--IIAEPLRTYHPSMpRQEV---KDRVKTMMMKVGLL--PNLI 157
Cdd:PRK15093 74 DLLRLSPRERRKlVGHNVSMIFQEPQSCLDPSERVGRqlMQNIPGWTYKGRW-WQRFgwrKRRAIELLHRVGIKdhKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 158 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 238 YLGHAVELGTYSEVYNNPQHPYTRALMSAVP-----IPDPDReknkeIQLLEGELPSPINPPSGCVFRTRCPIAGPECAK 312
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPdfgsaMPHKSR-----LNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIE 307
|
330
....*....|....*
gi 1799545459 313 TrPLLEGGFRHAVSC 327
Cdd:PRK15093 308 T-PRLTGAKNHLYAC 321
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
35-267 |
1.22e-58 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 189.37 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGR-----DLLGQSEEEWRK-ARSDIQMIFQD 108
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRlLRTEWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 PLASLNPRMTIGDIIAEPL-----RTYhpsmprQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:PRK11701 98 PRDGLRMQVSAGGNIGERLmavgaRHY------GDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRAL 263
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
....
gi 1799545459 264 MSAV 267
Cdd:PRK11701 252 VSSV 255
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-267 |
1.89e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 183.27 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 22 IKDGRQWFwqpaKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVaWLGRDLLGQSEEEWRKARSD 101
Cdd:COG1126 4 IENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-TVDGEDLTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 102 IQMIFQdplaSLN--PRMTIGDIIAEPLRTYHpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALI 179
Cdd:COG1126 79 VGMVFQ----QFNlfPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 180 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPY 259
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHER 231
|
....*...
gi 1799545459 260 TRALMSAV 267
Cdd:COG1126 232 TRAFLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-244 |
3.26e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 179.47 E-value: 3.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 8 KVLLEIADLKVHFNIKDGRqwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDL 87
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE---------VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 88 LGQSEEEWRKARSD-IQMIFQDPlaSLNPRMTIGDIIAEPLRtYHpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSG 166
Cdd:COG1136 73 SSLSERELARLRRRhIGFVFQFF--NLLPELTALENVALPLL-LA-GVSRKERRERARELLERVGL-GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 244
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
37-256 |
4.63e-55 |
|
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: 179.45 E-value: 4.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLASL-NP 115
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPDDQLfAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 rmTIGDIIA---EPLRtyhpsMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:COG1122 92 --TVEEDVAfgpENLG-----LPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-241 |
5.81e-55 |
|
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: 178.84 E-value: 5.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFNIKDGRQWfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQ 90
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQ---------ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 91 SEEEWRKARSD-IQMIFQDPlaSLNPRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQC 169
Cdd:cd03255 72 SEKELAAFRRRhIGFVFQSF--NLLPDLTALENVELPLL--LAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGH 241
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
38-246 |
3.78e-54 |
|
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: 176.56 E-value: 3.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrkaRSDIQMIFQDPlaSLNPRM 117
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIGMVFQDY--ALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:cd03259 88 TVAENIAFGLK--LRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
35-237 |
1.05e-53 |
|
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: 175.35 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSeeewrkarSDIQMIFQDPlaSLN 114
Cdd:cd03293 16 AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG--------PDRGYVFQQD--ALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:cd03293 86 PWLTVLDNVALGLE--LQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVM 237
Cdd:cd03293 163 DALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
28-241 |
1.26e-53 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 174.96 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 28 WFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKarsDIQMIFQ 107
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR---KVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 DPLASL-NPrmTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:cd03225 83 NPDDQFfGP--TVEEEVAFGLENLG--LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-237 |
8.33e-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: 174.51 E-value: 8.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 1 MNAVAekkVLLEIADLKVHFNIKDGRqwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV 80
Cdd:COG1116 1 MSAAA---PALELRGVSKRFPTGGGG---------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 81 AWLGRDLLGqseeewrkARSDIQMIFQDPlaSLNPRMTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLLPnLINRY 160
Cdd:COG1116 69 LVDGKPVTG--------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGLAG-FEDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 161 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQaqvvNLLQQLQREMGLSLIFIAHDL--AVVkhISDRV 234
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVdeAVF--LADRV 209
|
...
gi 1799545459 235 LVM 237
Cdd:COG1116 210 VVL 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
38-256 |
2.93e-52 |
|
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: 172.04 E-value: 2.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSeeewrKARSDIQMIFQDplASLNPRM 117
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PHKRPVNTVFQN--YALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:cd03300 88 TVFENIAFGLRL--KKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
37-241 |
7.20e-52 |
|
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: 169.29 E-value: 7.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLRRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLrtyhpsmprqevkdrvktmmmkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03229 91 LTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
37-267 |
1.68e-51 |
|
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: 171.17 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRD-----LLGQSEEEWRK-ARSDIQMIFQDPL 110
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRlMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNPRMTIGDIIAEPLRTY---HPSMPRQEVKDRVKtmmmKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLMAIgarHYGNIRATAQDWLE----EVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAV 267
Cdd:TIGR02323 173 DEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
37-243 |
4.78e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 169.47 E-value: 4.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:COG3638 17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIFQQF--NLVPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MT---------IGDIiaEPLRTYHPSMPRQEvKDRVKTMMMKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:COG3638 95 LSvltnvlagrLGRT--STWRSLLGLFPPED-RERALEALERVGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG3638 171 DEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
37-260 |
1.38e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 171.48 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGqseeeWRKAR-SDIQMIFQDPLasLNP 115
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-----NLPPReRRVGFVFQHYA--LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPLRTYHPSmpRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:COG1118 89 HMTVAENIAFGLRVRPPS--KAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYT 260
Cdd:COG1118 166 AKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-268 |
1.79e-50 |
|
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: 168.59 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARS-DIQMIFQDplASLNPR 116
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03294 117 RTVLENVAFGLEVQG--VPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVP 268
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
37-259 |
3.50e-50 |
|
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: 167.13 E-value: 3.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrkarSDIQMIFQDplASLNPR 116
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHPSM--PRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:cd03296 89 MTVFDNVAFGLRVKPRSErpPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPY 259
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
37-259 |
5.05e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 164.86 E-value: 5.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwRkarsDIQMIFQDPlaSLNPR 116
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R----NIAMVFQSY--ALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:COG3839 90 MTVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHD------LAvvkhisDRVLVMYLGHAVELGTYSEVYNNPQHPY 259
Cdd:COG3839 167 KLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
37-261 |
1.22e-47 |
|
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: 160.54 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkaRSdIQMIFQDplASLNPR 116
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--RK-IGYVIQQ--IGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLLP-NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:cd03295 90 MTVEENIALVPKLLK--WPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTR 261
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-241 |
5.57e-47 |
|
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: 158.08 E-value: 5.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFnikdgrqwfwqpaKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlGQ 90
Cdd:cd03262 1 IEIKNLHKSF-------------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 91 SEEEWRKARSDIQMIFQDplASLNPRMTIGDIIAEPLRTYHpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQ 170
Cdd:cd03262 67 DKKNINELRQKVGMVFQQ--FNLFPHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-190 |
1.17e-46 |
|
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: 155.11 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKarsDIQMIFQDPlaSLNPRMT 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK---EIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 119 IGDIIAEPLRTYHPSmpRQEVKDRVKTMMMKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:pfam00005 76 VRENLRLGLLLKGLS--KREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
37-251 |
3.03e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.76 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrkARSDIQMIFQDPlaSLNPR 116
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRRIGYVPQEP--ALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:COG1131 88 LTVRENLRFFARLYG--LPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 197 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:COG1131 165 EARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-255 |
6.20e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 160.11 E-value: 6.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 1 MNAVAEKKVLLEIADLKVHFnikDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSF---DGKE----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 81 AWLGRDLLGQSEEewrkaRSDIQMIFQDplASLNPRMTIGDIIAEPLRtyhpsM---PRQEVKDRVKTMMMKVGLlPNLI 157
Cdd:PRK09452 72 MLDGQDITHVPAE-----NRHVNTVFQS--YALFPHMTVFENVAFGLR-----MqktPAAEITPRVMEALRMVQL-EEFA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 158 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
250
....*....|....*...
gi 1799545459 238 YLGHAVELGTYSEVYNNP 255
Cdd:PRK09452 219 RDGRIEQDGTPREIYEEP 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
37-246 |
3.54e-45 |
|
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: 153.18 E-value: 3.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseEEWRKARSDIQMIFQDplASLNPR 116
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKDRDIAMVFQN--YALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03301 87 MTVYDNIAFGLKLRK--VPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03301 164 KLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
37-244 |
5.15e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 153.28 E-value: 5.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDplASLNPR 116
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLR-TYhpsMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:COG2884 94 RTVYENVALPLRvTG---KSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799545459 196 VSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:COG2884 170 PETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
37-256 |
4.55e-44 |
|
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: 152.22 E-value: 4.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDPLASLNpR 116
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAeplrtYHPS---MPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:TIGR04521 98 ETVYKDIA-----FGPKnlgLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 194 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
39-251 |
6.58e-44 |
|
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: 151.35 E-value: 6.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSdiqMIFQDPLASLNprMT 118
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA---YVPQEPPAPFG--LT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAepL-RTYHPSM---PRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:COG1120 92 VRELVA--LgRYPHLGLfgrPSAEDREAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:COG1120 169 DLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
37-251 |
8.18e-44 |
|
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: 150.41 E-value: 8.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHP---SMPRQ---EVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:cd03256 93 LSVLENVLSGRLGRRStwrSLFGLfpkEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:cd03256 172 VASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-241 |
8.71e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.58 E-value: 8.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 19 HFNIKDGRQWFWQPaktlkavdgVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKa 98
Cdd:COG4619 5 GLSFRVGGKPILSP---------VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 99 rsDIQMIFQDPLAslnPRMTIGDIIAEPLRTYHPSMPRQEVKDrvktMMMKVGLLPNLINRYPHEFSGGQCQRIGIARAL 178
Cdd:COG4619 75 --QVAYVPQEPAL---WGGTVRDNLPFPFQLRERKFDRERALE----LLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 179 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
38-253 |
5.90e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.31 E-value: 5.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseeewRKARSDI----QMifqdplASL 113
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRARRRIgyvpQR------AEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPR--MTIGDIIAEPLRTYHP--SMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:COG1121 87 DWDfpITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMyLGHAVELGTYSEVYN 253
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-253 |
1.25e-42 |
|
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: 147.44 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNikDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:TIGR02315 1 MLEVENLSKVYP--NGKQ----------ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRKARSDIQMIFQDplASLNPRMTIGDIIAEPLRTYHPSM-------PRQEvKDRVKTMMMKVGLLpNLINRYPH 162
Cdd:TIGR02315 69 LRGKKLRKLRRRIGMIFQH--YNLIERLTVLENVLHGRLGYKPTWrsllgrfSEED-KERALSALERVGLA-DKAYQRAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:TIGR02315 145 QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
250
....*....|.
gi 1799545459 243 VELGTYSEVYN 253
Cdd:TIGR02315 225 VFDGAPSELDD 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
39-256 |
1.62e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 147.10 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrkaRSDIQMIFQDplASLNPRMT 118
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQN--YALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:cd03299 88 VYKNIAYGLK--KRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
37-251 |
1.79e-42 |
|
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: 146.56 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA-----TEGRVAWLGRDLLGQSEE-EWRKARsdIQMIFQDPl 110
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvLELRRR--VGMVFQKP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 aslNP-RMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKVGLLPNLINR-YPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03260 91 ---NPfPGSIYDNVAYGLR-LHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 189 EPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-256 |
6.17e-42 |
|
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: 146.34 E-value: 6.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 9 VLLEIADLKVHFnikDGrqwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLL 88
Cdd:COG0411 3 PLLEVRGLTKRF---GG----------LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 89 GQSEEE-WRK--ARSdiqmiFQdpLASLNPRMTIGD-------------IIAEPLRTYHPSMPRQEVKDRVKTMMMKVGL 152
Cdd:COG0411 70 GLPPHRiARLgiART-----FQ--NPRLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 153 LPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 232
Cdd:COG0411 143 AD-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLAD 221
|
250 260
....*....|....*....|....
gi 1799545459 233 RVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:COG0411 222 RIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
37-264 |
1.32e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 146.77 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkaRS---DIQMIfqdplaSL 113
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR--RRigyVIQQI------GL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIGDIIAeplrTYhPSM---PRQEVKDRVKTMMMKVGLLPN-LINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:COG1125 88 FPHMTVAENIA----TV-PRLlgwDKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALM 264
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
38-267 |
1.52e-41 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 144.56 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRkaRSDIQMIFQDplASLNPRM 117
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDA---TRVHAR--DRKIGFVFQH--YALFKHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYHPsmPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:TIGR00968 88 TVRDNIAFGLEIRKH--PKAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAV 267
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
39-266 |
1.66e-41 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.84 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL----VKATEGRVAWLGRDLLGQSeeewRKARSdIQMIFQDPLASLN 114
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCA----LRGRK-IATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAEPLRtyhpSMPRQEVKDRVKTMMMKVGL--LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK10418 94 PLHTMHTHARETCL----ALGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSA 266
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-251 |
2.98e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 143.84 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKdgrqwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDllg 89
Cdd:COG4555 1 MIEVENLSKKYGKV-------------PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 qSEEEWRKARSDIQMIFQDPlaSLNPRMTIGDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQC 169
Cdd:COG4555 65 -VRKEPREARRQIGVLPDER--GLYDRLTVRENIRYFAELYG--LFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYS 249
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
..
gi 1799545459 250 EV 251
Cdd:COG4555 218 EL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-256 |
3.57e-40 |
|
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: 141.04 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFnikDGrqwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQ 90
Cdd:cd03219 1 LEVRGLTKRF---GG----------LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 91 SEEewRKARSDIQMIFQDPlaSLNPRMTIGD--IIAEPLRTYHPSMP------RQEVKDRVKTMMMKVGLLPnLINRYPH 162
Cdd:cd03219 68 PPH--EIARLGIGRTFQIP--RLFPELTVLEnvMVAAQARTGSGLLLararreEREARERAEELLERVGLAD-LADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
250
....*....|....
gi 1799545459 243 VELGTYSEVYNNPQ 256
Cdd:cd03219 222 IAEGTPDEVRNNPR 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-241 |
1.27e-39 |
|
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: 137.53 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFnikdgrqwfwqpaKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgq 90
Cdd:cd03230 1 IEVRNLSKRY-------------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 91 sEEEWRKARSDIQMIFQDPlaSLNPRMTIGDIIaeplrtyhpsmprqevkdrvktmmmkvgllpnlinryphEFSGGQCQ 170
Cdd:cd03230 65 -KKEPEEVKRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-269 |
6.20e-39 |
|
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: 140.32 E-value: 6.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 54 VVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrkaRSDIQMIFQDplASLNPRMTIGDIIAEPLRTyhPS 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQS--YALFPHMTVEENVAFGLKM--RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 134 MPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREM 213
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 214 GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVPI 269
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
38-251 |
6.50e-39 |
|
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: 146.13 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDPlaslnprM 117
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ---IGVVLQDV-------F 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYHPSMPRQEVKDRVKtmmmKVGLLPnLINRYPH-----------EFSGGQCQRIGIARALILEPKLII 186
Cdd:COG2274 560 LFSGTIRENITLGDPDATDEEIIEAAR----LAGLHD-FIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEV 251
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
37-241 |
6.78e-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: 135.06 E-value: 6.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQdplaslnpr 116
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 mtigdiiaeplrtyhpsmprqevkdrvktmmmkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 197 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
38-237 |
7.31e-39 |
|
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: 136.89 E-value: 7.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseeewRKARSDIQMIFQDPLASLNPRM 117
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPlRTYHPSM---PRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:cd03235 86 SVRDVVLMG-LYGHKGLfrrLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1799545459 195 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
32-237 |
2.01e-38 |
|
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: 134.43 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 32 PAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDP-L 110
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN---IAYVPQDPfL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASlnprMTIGDiiaeplrtyhpsmprqevkdrvktmmmkvgllpNLinrypheFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:cd03228 88 FS----GTIRE---------------------------------NI-------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03228 124 TSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVL 167
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
38-254 |
2.45e-38 |
|
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: 142.97 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDP-LaslnPR 116
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ---IAWVPQNPyL----FA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTigdiIAEPLRTYHPSMPRQEVKDRVKtmmmKVGLLpNLINRYPHEF-----------SGGQCQRIGIARALILEPKLI 185
Cdd:COG4988 425 GT----IRENLRLGRPDASDEELEAALE----AAGLD-EFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 186 ICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-261 |
1.02e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.43 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFnikDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlg 89
Cdd:PRK11607 19 LLEIRNLTKSF---DGQH----------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 qseEEWRKARSDIQMIFQDplASLNPRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQC 169
Cdd:PRK11607 84 ---SHVPPYQRPINMMFQS--YALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSI----QAQVVNLLQQLqremGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 245
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250
....*....|....*.
gi 1799545459 246 GTYSEVYnnpQHPYTR 261
Cdd:PRK11607 232 GEPEEIY---EHPTTR 244
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-252 |
1.44e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.53 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQdplaslNPR- 116
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRRQVGMVFQ------NPDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 ----MTIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK13635 93 qfvgATVQDDVAFGLENI--GVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVY 252
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
39-272 |
1.71e-37 |
|
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: 137.43 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA--TEGRVAWLGRDLLGQSEEewrkaRSDIQMIFQDplASLNPR 116
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPH-----KRGLALLFQN--YALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:TIGR03258 94 LKVEDNVAFGLRAQ--KMPKADIAERVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 197 SIQAQVVNLLQQLQREM-GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVPIPDP 272
Cdd:TIGR03258 171 NIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
39-255 |
1.86e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 137.16 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrkarSDIQMIFQDplASLNPRMT 118
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDICMVFQS--YALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK11432 95 LGENVGYGLKML--GVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-266 |
8.08e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 8.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwRKarsdIQMIFQDplASLNPRMTIGDI 122
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP----VSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 IAEPLrtyHPSM-PRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:COG3840 92 IGLGL---RPGLkLTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSA 266
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-237 |
9.82e-37 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 131.79 E-value: 9.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDgrqwfwQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV------AWL 83
Cdd:COG4778 4 LLEVENLSKTFTLHL------QGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdgGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 84 grDLLGQSEEEW---RkaRSDI----QmiFqdplasLN--PRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLP 154
Cdd:COG4778 78 --DLAQASPREIlalR--RRTIgyvsQ--F------LRviPRVSALDVVAEPLL--ERGVDREEARARARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 155 NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRV 234
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
...
gi 1799545459 235 LVM 237
Cdd:COG4778 223 VDV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
40-267 |
1.34e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 131.75 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwRKARSDIQMIFQDplASLNPRMTI 119
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQEAGMVFQQ--FYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIA-EPLRTYhpSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK09493 95 LENVMfGPLRVR--GASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 199 QAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAV 267
Cdd:PRK09493 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
39-246 |
2.23e-36 |
|
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: 129.09 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSdiqmifqdplaslnprmt 118
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 igdiiaeplrtYhpsmprqevkdrVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:cd03214 77 -----------Y------------VPQALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799545459 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
41-265 |
4.39e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.86 E-value: 4.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLG------RDLLGQ----SEEEWRKARSDIQMIFQDpl 110
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvRDKDGQlkvaDKNQLRLLRTRLTMVFQH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNPRMTIGDIIAE-PLRTYhpSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK10619 101 FNLWSHMTVLENVMEaPIQVL--GLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMS 265
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
27-244 |
6.30e-36 |
|
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: 129.86 E-value: 6.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 27 QWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSD-IQMI 105
Cdd:COG4181 16 KTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARhVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 FQdplaS--LNPRMTIGDIIAEPLrtyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:COG4181 96 FQ----SfqLLPTLTALENVMLPL----ELAGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 244
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
38-256 |
6.37e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 6.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDP----LASl 113
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQNPdnqfIGA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 nprmTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK13632 100 ----TVEDDIAFGLE--NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 194 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDL-AVVKhiSDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-269 |
9.01e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 133.62 E-value: 9.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKAR-SDIQMIFQDplASLNPR 116
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK10070 121 MTVLDNTAFGMEL--AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVPI 269
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
42-256 |
2.94e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.21 E-value: 2.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGR--DLLGQ-SEEEWRKARSDIQMIFQDplASLNPRMT 118
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTpSDKAIRELRRNVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 -IGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK11124 99 vQQNLIEAPCRVL--GLSKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 198 IQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEvYNNPQ 256
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
42-256 |
5.70e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.44 E-value: 5.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDL---LGQSEEEWRKARSDIQMIFQDplASLNPRMT 118
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGD-IIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:COG4161 99 VMEnLIEAPCKVL--GLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 198 IQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTySEVYNNPQ 256
Cdd:COG4161 176 ITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-262 |
9.61e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.46 E-value: 9.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 1 MNAVAEK-KVLLEIADLKVHFNIKdgrqwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAI------IGLV 73
Cdd:COG1117 1 MTAPASTlEPKIEVRNLNVYYGDK-------------QALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 74 KaTEGRVAWLGRDLLGQSE--EEWRKarsDIQMIFQDPlaslNP-RMTIGDIIAEPLRtYHPSMPRQEVKDRVKTMMMKV 150
Cdd:COG1117 68 R-VEGEILLDGEDIYDPDVdvVELRR---RVGMVFQKP----NPfPKSIYDNVAYGLR-LHGIKSKSELDEIVEESLRKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 151 GL-------LpnliNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHD 223
Cdd:COG1117 139 ALwdevkdrL----KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 1799545459 224 LAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRA 262
Cdd:COG1117 213 MQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
41-265 |
1.27e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.79 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG--RVAWLGRDL---LGQSEEEWRKARSDIQMIFQDplASLNP 115
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtiRVGDITIDTarsLSQQKGLIRQLRQHVGFVFQN--FNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 -RMTIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK11264 99 hRTVLENIIEGPVIV--KGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 195 DVSIQAQVVNLLQQLQREMgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMS 265
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-237 |
1.60e-34 |
|
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: 125.49 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 48 EGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEE-----EWRKarsdIQMIFQDplASLNPRMTIGDI 122
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppQQRK----IGLVFQQ--YALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 IAEPLRTYHPSmprqEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 202
Cdd:cd03297 96 LAFGLKRKRNR----EDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1799545459 203 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
38-255 |
3.07e-34 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 128.42 E-value: 3.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVaWLGRDLLGQSEEEWRkarsDIQMIFQDplASLNPRM 117
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRVVNELEPADR----DIAMVFQN--YALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK11650 92 SVRENMAYGLKIR--GMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHD------LAvvkhisDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK11650 169 LRVQMRLEIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
37-243 |
4.65e-34 |
|
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: 122.54 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARsdIQMIFQdplaslnpr 116
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--IAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 mtigdiiaeplrtyhpsmprqevkdrvktmmmkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799545459 197 SIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
241-329 |
5.20e-34 |
|
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: 120.16 E-value: 5.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 241 HAVELGTYSEVYNNPQHPYTRALMSAVPIP-DPDREKNKeiqlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRP-LLE 318
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRDRKLIS----IPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPaLVE 76
|
90
....*....|.
gi 1799545459 319 GGFRHAVSCLK 329
Cdd:TIGR01727 77 IAEGHRVACHL 87
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
37-254 |
5.34e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEeWRKARSDIQMIFQDPLASLNPR 116
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGL-LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13637 100 TIEKDIAFGPINL---GLSEEEIENRVKRAMNIVGLdYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
41-266 |
5.75e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 125.30 E-value: 5.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLG------RDLLGQSEEEWRKA----RSDIQMIFQdpl 110
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkPDRDGELVPADRRQlqriRTRLGMVFQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 aSLN--PRMTI-GDIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:COG4598 103 -SFNlwSHMTVlENVIEAPVHVLG--RPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSA 266
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
42-255 |
7.97e-34 |
|
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: 127.52 E-value: 7.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKA-RSDIQMIFQDplASLNPRMTIg 120
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQE--ARLFPHLSV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 diiAEPLRtY----HPSMPRQEVKDRVKTMMmkvGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:COG4148 95 ---RGNLL-YgrkrAPRAERRISFDEVVELL---GIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-265 |
1.17e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 130.27 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 32 PAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDP-- 109
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQRPhl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 -LASlnprmtigdiIAEPLRtyhpsMPRQEVKD-RVKTMMMKVGLLPnLINRYPH-----------EFSGGQCQRIGIAR 176
Cdd:COG4987 421 fDTT----------LRENLR-----LARPDATDeELWAALERVGLGD-WLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYSEVYNnpQ 256
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA--Q 559
|
....*....
gi 1799545459 257 HPYTRALMS 265
Cdd:COG4987 560 NGRYRQLYQ 568
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
37-267 |
1.31e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.74 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkarsdIQMIFQDplASLNPR 116
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-----VGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTyhpsMPRQE------VKDRVkTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK10851 89 MTVFDNIAFGLTV----LPRRErpnaaaIKAKV-TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAV 267
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-260 |
1.06e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.87 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK-----ATEGRVAWLGRDLLGQSEEEWRkARSDIQMIFQDPlaSL 113
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYP--NP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYT 260
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
38-254 |
1.45e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 120.62 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrKARSDIQMIFQDPlaSLNPRM 117
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE--RARAGIGYVPEGR--RIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TigdiIAEPLRTYHPSMPRQEVKDRVKTMmmkVGLLPNLINRYPH---EFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:cd03224 91 T----VEENLLLGAYARRRAKRKARLERV---YELFPRLKERRKQlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 195 DVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:cd03224 164 APKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
10-237 |
2.40e-32 |
|
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: 120.19 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNIKDgrqwfwQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV------AWL 83
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQ------QGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRIlvrhegAWV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 84 grDLLGQSEEEWRKAR-SDIQMIFQdpLASLNPRMTIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPNLINRYPH 162
Cdd:TIGR02324 75 --DLAQASPREVLEVRrKTIGYVSQ--FLRVIPRVSALEVVAEPLLER--GVPREAARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-252 |
2.48e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.88 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLkvHFNIKDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlG 89
Cdd:PRK13636 5 ILKVEEL--NYNYSDGTH----------ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQC 169
Cdd:PRK13636 72 YSRKGLMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNL---KLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYS 249
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 1799545459 250 EVY 252
Cdd:PRK13636 228 EVF 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-253 |
3.64e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.43 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEW-RKARSDIQMIFQDPLASLNP 115
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPlrtYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13646 101 DTVEREIIFGP---KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYN 253
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
37-237 |
6.80e-32 |
|
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: 118.13 E-value: 6.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseEEWRKARSdIQMIFQDPLASLnpr 116
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKS-IGYVMQDVDYQL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 mtIGDIIAEPLRtyhPSMPR-QEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:cd03226 85 --FTDSVREELL---LGLKElDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799545459 196 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03226 159 YKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
37-250 |
9.75e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.89 E-value: 9.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDP-LASlnp 115
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ---IGVVPQDTfLFS--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 rMTIGDIIAeplrtY-HPSMPRQEVKDRVKtmmmKVGLLpNLINRYPH-----------EFSGGQCQRIGIARALILEPK 183
Cdd:COG1132 428 -GTIRENIR-----YgRPDATDEEVEEAAK----AAQAH-EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 184 LIICDEPVSALDVSIQAQVvnlLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:COG1132 497 ILILDEATSALDTETEALI---QEALERLMkGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
42-259 |
9.87e-32 |
|
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: 121.76 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRdLLGQSEE------EWRKarsdIQMIFQDplASLNP 115
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSRKgiflppEKRR----IGYVFQE--ARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIgdiiAEPLR-TYHPSMP--RQEVKDRVKTMMmkvGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:TIGR02142 89 HLSV----RGNLRyGMKRARPseRRISFERVIELL---GIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPY 259
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-261 |
1.27e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 119.37 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIiGLVKATEGRVAWLGR-DLLGQSEEEWR----KARSDIQMIFQDP 109
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRvEFFNQNIYERRvnlnRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 laSLNPrMTIGDIIAEPLRT--YHPSMprqEVKDRVKTMMMKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:PRK14258 98 --NLFP-MSVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLwdeIKHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 185 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY-----LGHAVELGTYSEVYNNPQHPY 259
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSR 251
|
..
gi 1799545459 260 TR 261
Cdd:PRK14258 252 TR 253
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
38-250 |
1.32e-31 |
|
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: 117.86 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLgqseEEWRKARSDIQMIFQDPlaSLNPRM 117
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDL--SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:cd03265 89 TGWENLYIHARLY--GVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSE 250
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-237 |
1.79e-31 |
|
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: 117.51 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDPLasLN 114
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFR--LL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAEPLR-TYHPsmpRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:cd03292 91 PDRNVYENVAFALEvTGVP---PREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799545459 194 LDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03292 167 LDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-256 |
1.88e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 119.35 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwLGRDLL--GQSEEEWRKARSDIQMIFQDPLASLN 114
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVItaGKKNKKLKPLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK13634 100 EETVEKDICFGPMNF---GVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
39-225 |
2.38e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.20 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA---TEGRVaWL-GRDLLGQSEEEWRkarsdIQMIFQDPLasLN 114
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV-LLnGRRLTALPAEQRR-----IGILFQDDL--LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAEPLRtyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:COG4136 89 PHLSVGENLAFALP---PTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 1799545459 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLA 225
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-260 |
2.65e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 118.23 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVK------ATEGRVAWLGRDLLgqsEEEWRKARSDIQMIFQDPlaSLNP 115
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIF---QIDAIKLRKEVGMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPLRTyHPSMPRQEVKDRVKTMMMKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK14246 104 HLSIYDNIAYPLKS-HGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYT 260
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-256 |
2.67e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLkvHFNIKDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlG 89
Cdd:PRK13639 1 ILETRDL--KYSYPDGTE----------ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQC 169
Cdd:PRK13639 68 YDKKSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNL---GLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYS 249
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
....*..
gi 1799545459 250 EVYNNPQ 256
Cdd:PRK13639 223 EVFSDIE 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-251 |
4.92e-31 |
|
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: 122.22 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV------AWLgrDLLGQSEEEWRKARSDIQMIFQDp 109
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWV--DMTKPGPDGRGRAKRYIGILHQE- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 lASLNPRMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGL----LPNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:TIGR03269 374 -YDLYPHRTVLDNLTEAIGL---ELPDELARMKAVITLKMVGFdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
39-284 |
6.05e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.91 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLASLnPRMT 118
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVFQNPDNQF-VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK13650 99 VEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYSEVYNNPQH--------PYTRALMSAVP-- 268
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFTTSLVQSLRqn 254
|
250 260
....*....|....*....|
gi 1799545459 269 -IPDPDR---EKNKEIQLLE 284
Cdd:PRK13650 255 gYDLPEGyltEKELEEQLWE 274
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-251 |
1.18e-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: 115.64 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseeewRKARSDIQMIFQDplASLNPRMT 118
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI--------TEPGPDRMVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
38-254 |
1.54e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.73 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDllgQSEEE--WrKARSDIQMIFQdplaslNP 115
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD---TSDEEnlW-DIRNKAGMVFQ------NP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPLRTYHPS---MPRQEVKDRVKTMMMKVGLLPnlINRY-PHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK13633 95 DNQIVATIVEEDVAFGPEnlgIPPEEIRERVDESLKKVGMYE--YRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 192 SALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAVVkhiSDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHymEEAVE---ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
37-256 |
2.92e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.08 E-value: 2.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQ-SEEEWRKARSDIQMIFQDPLASLNP 115
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13641 101 NTVLKDVEFGPKNF---GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 196 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-260 |
4.86e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.62 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFNikdgrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK-----ATEGRVAWLGR 85
Cdd:PRK14247 4 IEIRDLKVSFG-------------QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 DLLGQSEEEWRKArsdIQMIFQDPlaSLNPRMTIGDIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPNLINRY---PH 162
Cdd:PRK14247 71 DIFKMDVIELRRR---VQMVFQIP--NPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*...
gi 1799545459 243 VELGTYSEVYNNPQHPYT 260
Cdd:PRK14247 224 VEWGPTREVFTNPRHELT 241
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
40-223 |
6.33e-30 |
|
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: 112.96 E-value: 6.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlGQSEEEWRKarsdiQMIFQDPLASLNPRMTI 119
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRR-----RLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 gdiiAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 199
Cdd:COG4133 93 ----RENLRFWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 1799545459 200 AQVVNLLQQLQREmGLSLIFIAHD 223
Cdd:COG4133 168 ALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-247 |
2.31e-29 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 112.85 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLkvHFNIKDGrqwfwqpaKTLKavdGVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRVAWLGRDLL 88
Cdd:COG0396 1 LEIKNL--HVSVEGK--------EILK---GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 89 GQSEEEwrKARSDIQMIFQDPLASlnPRMTIGDIiaepLRT-----YHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHE 163
Cdd:COG0396 68 ELSPDE--RARAGIFLAFQYPVEI--PGVSVSNF----LRTalnarRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 164 -FSGGQCQRIGIARALILEPKLIICDEPVSALDV---SIQAQVVNLLqqlqREMGLSLIFIAHDLAVVKHIS-DRVLVMY 238
Cdd:COG0396 140 gFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYIKpDFVHVLV 215
|
....*....
gi 1799545459 239 LGHAVELGT 247
Cdd:COG0396 216 DGRIVKSGG 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
38-251 |
2.36e-29 |
|
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: 112.58 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDlLGQSEEEWrkARSDIQMIFQDPLasLNPRm 117
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD-LALADPAW--LRRQVGVVLQENV--LFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAeplrTYHPSMPRQEVKDRVK-----TMMMKvglLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03252 91 SIRDNIA----LADPGMSMERVIEAAKlagahDFISE---LPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 189 EPVSALDVSIQAqvvNLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEV 251
Cdd:cd03252 164 EATSALDYESEH---AIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
34-250 |
3.97e-29 |
|
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: 111.44 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLgqseEEWRKARSDIQMIFQDplASL 113
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQSLGYCPQF--DAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTigdiIAEPLRTYHP--SMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:cd03263 87 FDELT----VREHLRFYARlkGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 192 SALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSE 250
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-237 |
5.02e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFNIKDGRQwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQ 90
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQ---------PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 91 SEEewrkaRSdiqMIFQDplASLNPRMTIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQ 170
Cdd:COG4525 75 GAD-----RG---VVFQK--DALLPWLNVLDNVAFGLRL--RGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVVkhISDRVLVM 237
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVM 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-237 |
5.14e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARsdIQMIFQDPlaSLNPR 116
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG--IAIIHQEL--NLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIA---EPLRtyHPSMPRQEVKDRVKTMMMKVGL-LPnlinryPH----EFSGGQCQRIGIARALILEPKLIICD 188
Cdd:COG1129 94 LSVAENIFlgrEPRR--GGLIDWRAMRRRARELLARLGLdID------PDtpvgDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 189 EPVSALDvsiQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:COG1129 166 EPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-287 |
1.48e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.34 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 30 WQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgQSEEEWrKARSDIQMIFQDP 109
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL--TAENVW-NLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 LASLnPRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK13642 91 DNQF-VGATVEDDVAFGME--NQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNNPQH--------PYTR 261
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDmveigldvPFSS 245
|
250 260 270
....*....|....*....|....*....|.
gi 1799545459 262 ALM-----SAVPIPDPDREKNKEIQLLEGEL 287
Cdd:PRK13642 246 NLMkdlrkNGFDLPEKYLSEDELVELLADKL 276
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
38-256 |
1.51e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.38 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKarsDIQMIFQDPlaslnPRM 117
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK---HIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDII----AEPLRTYhpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK13648 96 FVGSIVkydvAFGLENH--AVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 194 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-241 |
2.16e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.58 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDPLASLNpr 116
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYHPSMprQEVKDRVKTMMMKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASG--DDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 197 SIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10908 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-261 |
3.81e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.58 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseeewrkARSDIQMIfqd-plaSL 113
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----------DPEDRRRIgylpeerGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIGDII---AEpLRtyhpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:COG4152 83 YPKMKVGEQLvylAR-LK----GLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 191 VSALD-VSiqaqvVNLLQQL---QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNnpQHPYTR 261
Cdd:COG4152 157 FSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QFGRNT 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-256 |
3.96e-28 |
|
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: 109.30 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFnikdGRqwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:COG0410 3 MLEVENLHAGY----GG---------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEewRKARSDI------QMIFqdplaslnPRMTIgdiiAEPLRT-YHPSMPRQEVKDRVKTMMmkvGLLPNLinrypH 162
Cdd:COG0410 70 LPPH--RIARLGIgyvpegRRIF--------PSLTV----EENLLLgAYARRDRAEVRADLERVY---ELFPRL-----K 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 163 EF--------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRV 234
Cdd:COG0410 128 ERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRA 206
|
250 260
....*....|....*....|..
gi 1799545459 235 LVMYLGHAVELGTYSEVYNNPQ 256
Cdd:COG0410 207 YVLERGRIVLEGTAAELLADPE 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
39-251 |
7.76e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.09 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSdiqMIFQDplASLNPRMT 118
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA---VLPQH--SSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIA---EPLRTyhpsmPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALI------LEPKLIICDE 189
Cdd:PRK13548 93 VEEVVAmgrAPHGL-----SRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-246 |
1.12e-27 |
|
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: 107.45 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrkARSDIQMIFQD 108
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE----ARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 plASLNPRMTIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03266 87 --TGLYDRLTARENLEYFAGLY--GLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 189 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-241 |
1.49e-27 |
|
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: 105.98 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 8 KVLLEIADLKVHfnikdgrqwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDL 87
Cdd:cd03215 2 EPVLEVRGLSVK-----------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 88 LGQSEEEWRKARsdIQMIFQDPLAS-LNPRMTIGDiiaeplrtyhpsmprqevkdrvktmmmkvgllpNLINryPHEFSG 166
Cdd:cd03215 65 TRRSPRDAIRAG--IAYVPEDRKREgLVLDLSVAE---------------------------------NIAL--SSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-283 |
1.97e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV---KATEGRVAWLGRDLlgQSEEEWrKARSDIQMI 105
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITL--TAKTVW-DIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 FQDPLASLnPRMTIGDIIAEPLRtyHPSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:PRK13640 90 FQNPDNQF-VGATVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNNPQH-------- 257
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEMlkeigldi 244
|
250 260 270
....*....|....*....|....*....|.
gi 1799545459 258 PYTRALM-----SAVPIPDPDREKNKEIQLL 283
Cdd:PRK13640 245 PFVYKLKnklkeKGISVPQEINTEEKLVQYL 275
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-255 |
2.39e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.77 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVHFNikdgrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:PRK11300 5 LLSVSGLMMRFG-------------GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEwrKARSDIQMIFQDplASLNPRMTI-------------GDIIAEPLRTyhPSMPRQEVK--DRVKTMMMKVGLLP 154
Cdd:PRK11300 72 LPGHQ--IARMGVVRTFQH--VRLFREMTVienllvaqhqqlkTGLFSGLLKT--PAFRRAESEalDRAATWLERVGLLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 155 nLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 234
Cdd:PRK11300 146 -HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 1799545459 235 LVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
36-283 |
3.11e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.17 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkategrVAWLGRDLLGQSE--------EEWRKARSDIQMIFQ 107
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIVGDYAipanlkkiKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 DPLASLNPRMTIGDIIAEPLrtyHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:PRK13645 98 FPEYQLFQETIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQhpytraLMSAV 267
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE------LLTKI 248
|
250 260
....*....|....*....|..
gi 1799545459 268 PIPDPD------REKNKEIQLL 283
Cdd:PRK13645 249 EIDPPKlyqlmyKLKNKGIDLL 270
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
37-246 |
3.27e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.12 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGeTLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEeewrKARSDIQMIFQDPlaSLNPR 116
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLRRRIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03264 87 FTVREFLDYIAWLK--GIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799545459 197 SIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03264 164 EERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
38-251 |
4.11e-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: 106.46 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrKARSDI------QMIFqdpla 111
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIayvpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 slnPRMTIgdiiAEPLRTYHPSMPR--QEVKDRVKTMMmkvGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR03410 88 ---PRLTV----EENLLTGLAALPRrsRKIPDEIYELF---PVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
36-237 |
4.62e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARsdIQMIFQDPlaSLNP 115
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG--IGMVHQHF--MLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGD-II--AEPLRtyHPSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:COG3845 94 NLTVAEnIVlgLEPTK--GGRLDRKAARARIRELSERYGLDVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799545459 193 ALDvsiQAQVVNLLQQLQR--EMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:COG3845 171 VLT---PQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
36-241 |
4.93e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 106.69 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDgvsLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwLGRDLLGQseeewrkARSDIQMIFQDplASLNP 115
Cdd:PRK11247 28 LNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPLAE-------AREDTRLMFQD--ARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPLRTyhpsmprqEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK11247 95 WKKVIDNVGLGLKG--------QWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1799545459 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
39-237 |
6.36e-27 |
|
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: 104.22 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkarsdiqmifqdplaslnprmt 118
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 igdiiaeplrtyhpsmprqevkDRVKTMMMKVGLLPNLINRypHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:cd03246 76 ----------------------DHVGYLPQDDELFSGSIAE--NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1799545459 199 QAQVVNLLQQLqREMGLSLIFIAHDLAVVKhISDRVLVM 237
Cdd:cd03246 132 ERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVL 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
42-241 |
1.38e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.90 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARS-DIQMIFQdpLASLNPRMTIG 120
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 DIIAEPLRTYHpsMPRQEVKDRVKTMMMKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:PRK11629 106 ENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1799545459 201 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISdRVLVMYLGH 241
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
34-246 |
1.83e-26 |
|
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: 103.90 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLG-------RDLLGQSEEE---WRKARSDIQ 103
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaaRNRIGYLPEErglYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 104 MIFqdpLASLNprmtigdiiaeplrtyhpSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:cd03269 91 LVY---LAQLK------------------GLKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
37-237 |
2.08e-26 |
|
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: 109.30 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKarsdiqmifQDPLASLNPR 116
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---------QIAWVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDiIAEPLRTYHPSMPRQEVKDRVktmmMKVGL----------LPNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:TIGR02857 407 LFAGT-IAENIRLARPDASDAEIREAL----ERAGLdefvaalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVkHISDRVLVM 237
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-260 |
2.46e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 6 EKKVLLEIADLKVHFNIKdgrqwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAI------IGLVKATeGR 79
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKK-------------KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlNPEVTIT-GS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 80 VAWLGRDLLGQSEE--EWRKarsDIQMIFQDPlaslNP-RMTIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLLPNL 156
Cdd:PRK14239 67 IVYNGHNIYSPRTDtvDLRK---EIGMVFQQP----NPfPMSIYENVVYGLRL--KGIKDKQVLDEAVEKSLKGASIWDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 157 INRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISD 232
Cdd:PRK14239 138 VKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISD 215
|
250 260
....*....|....*....|....*...
gi 1799545459 233 RVLVMYLGHAVELGTYSEVYNNPQHPYT 260
Cdd:PRK14239 216 RTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-224 |
2.88e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrkarsdiQMIFQDplASLNPRM 117
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTyhPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK11248 86 NVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*..
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDL 224
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-252 |
3.31e-26 |
|
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: 103.85 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 28 WFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQ 107
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 DPLaslnprmTIGDIIAEPLRTYHPSMPRQEVKDRVKTmmmkvGLLPNLINRYPHEF-----------SGGQCQRIGIAR 176
Cdd:cd03251 84 DVF-------LFNDTVAENIAYGRPGATREEVEEAARA-----ANAHEFIMELPEGYdtvigergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVY 252
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-250 |
4.83e-26 |
|
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: 103.77 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTlaraIIGLVK----ATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDP-LA 111
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDI---RDLNLRWLRSQIGLVSQEPvLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SlnprMTIGDIIAEPLRtyhpsmprqevkDRVKTMMMKVGLLPNL---INRYPHEF-----------SGGQCQRIGIARA 177
Cdd:cd03249 90 D----GTIAENIRYGKP------------DATDEEVEEAAKKANIhdfIMSLPDGYdtlvgergsqlSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-251 |
1.12e-25 |
|
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: 102.30 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDPLaslnprm 117
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---IGVVLQDTF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYHPSMPRQEVKDRVKT-----MMMKvglLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03254 88 LFSGTIMENIRLGRPNATDEEVIEAAKEagahdFIMK---LPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 189 EPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEV 251
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-241 |
1.37e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.35 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVaWLGrdllGQSEEEWRKARSDIQMIFQDplASLNPRMTIGDI 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLN----GQDHTTTPPSRRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 IAEPLrtyHPSMP-RQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK10771 92 IGLGL---NPGLKlNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799545459 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
39-251 |
1.38e-25 |
|
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: 107.52 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlGQSEEEWrkARSDIQMIFQDPLasLNPRMt 118
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL-AIADPAW--LRRQMGVVLQENV--LFSRS- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 igdiIAEPLRTYHPSMPRQEVKDRVKTmmmkVGLLpNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIIC 187
Cdd:TIGR01846 547 ----IRDNIALCNPGAPFEHVIHAAKL----AGAH-DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-250 |
1.82e-25 |
|
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: 101.92 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 18 VHFNIKDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRK 97
Cdd:cd03253 6 VTFAYDPGRP----------VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 98 ArsdIQMIFQD-PLaslnprmtIGDIIAEPLRTYHPSMPRQEVKDRVKtmmmkVGLLPNLINRYPHEF-----------S 165
Cdd:cd03253 76 A---IGVVPQDtVL--------FNDTIGYNIRYGRPDATDEEVIEAAK-----AAQIHDKIMRFPDGYdtivgerglklS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 166 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 245
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
....*
gi 1799545459 246 GTYSE 250
Cdd:cd03253 217 GTHEE 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-243 |
2.06e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEeeWRKARsDIQMIFQDPLASLNPR 116
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE--YKRAK-YIGRVFQDPMMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTigdiIAEPL---------RTYHPSMP---RQEVKDRVKTMMM--------KVGLLpnlinryphefSGGQCQRIGIAR 176
Cdd:COG1101 97 MT----IEENLalayrrgkrRGLRRGLTkkrRELFRELLATLGLglenrldtKVGLL-----------SGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVMYLGHAV 243
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-246 |
2.61e-25 |
|
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: 101.03 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlGQSEeewrKARSDIQMIFQDplASLNPRMTIGDI 122
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAP----PADRPVSMLFQE--NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 IAEPLrtyHPSMP-RQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:cd03298 91 VGLGL---SPGLKlTAEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-255 |
2.70e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.39 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 7 KKVLLEIADLKVHFNIKDGRQwfwqpaktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVaWLGRD 86
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENE--------LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 87 LLGQSEEEWR--------------KARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGL 152
Cdd:PRK13631 89 YIGDKKNNHElitnpyskkiknfkELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAL---GVKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 153 LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISD 232
Cdd:PRK13631 166 DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVAD 244
|
250 260
....*....|....*....|...
gi 1799545459 233 RVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
42-256 |
5.14e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.57 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrvawlgrDLL--GQSEEEWRKARSDIQMIFQDplASLNPRMTI 119
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-------DLFigEKRMNDVPPAERGVGMVFQS--YALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEPLRTyhPSMPRQEVKDRVKTMMmKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 199
Cdd:PRK11000 93 AENMSFGLKL--AGAKKEEINQRVNQVA-EVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 200 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK11000 170 VQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-256 |
6.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLkvHFNIKDGRqwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlGQ 90
Cdd:PRK13647 5 IEVEDL--HFRYKDGT----------KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 91 SEEEWrkARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQ 170
Cdd:PRK13647 72 ENEKW--VRSKVGLVFQDPDDQVFSSTVWDDVAFGPVNM---GLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTySE 250
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KS 223
|
....*.
gi 1799545459 251 VYNNPQ 256
Cdd:PRK13647 224 LLTDED 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-270 |
6.24e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.38 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSDIQMIFQDplASLNPRMTI 119
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEPLRTyHPSMPRQEVKdrvKTMMMK---VGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK11831 102 FDNVAYPLRE-HTQLPAPLLH---STVMMKleaVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQhPYTRALMSAV---PIP 270
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFLDGIadgPVP 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
37-270 |
1.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLASLNPR 116
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEPLRTyhpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK13652 95 TVEQDIAFGPINL---GLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHpYTRALMSAVPIP 270
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL-LARVHLDLPSLP 243
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-250 |
1.34e-24 |
|
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: 104.03 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 32 PAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPla 111
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL---ADYTLASLRRQVALVSQDV-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 slnprMTIGDIIAEPLRtYhpSMPRQEVKDRVKTMMMKVGLLpNLINRYPHEF-----------SGGQCQRIGIARALIL 180
Cdd:TIGR02203 416 -----VLFNDTIANNIA-Y--GRTEQADRAEIERALAAAYAQ-DFVDKLPLGLdtpigengvllSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 181 EPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-237 |
1.35e-24 |
|
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: 99.20 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQD 108
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI---RQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 P-LASlnprMTIGDIIAeplrtyhpsMPRQEVKDRVKTMMMKVGLLPNLINRYPHEF-----------SGGQCQRIGIAR 176
Cdd:cd03245 87 VtLFY----GTLRDNIT---------LGAPLADDERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVM 237
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVM 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
39-251 |
6.76e-24 |
|
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: 102.13 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV--------AWlGRDLLGQSeeewrkarsdIQMIFQDPl 110
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQW-DREELGRH----------IGYLPQDV- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 aSLNPRmTIGDIIAeplRtyHPSMPRQEVKD-----RVKTMMMKvglLPN----LINRYPHEFSGGQCQRIGIARALILE 181
Cdd:COG4618 416 -ELFDG-TIAENIA---R--FGDADPEKVVAaaklaGVHEMILR---LPDgydtRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 182 PKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEV 251
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEV 553
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-252 |
7.12e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.54 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 28 WF-WQPAKTLKavdGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDlLGQSEEEWRKARSDIQMIF 106
Cdd:PRK13638 8 WFrYQDEPVLK---GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-LDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 107 QDPlaslNPRMTIGDI---IAEPLRTYhpSMPRQEVKDRVKTMMMKVGllpnlINRYPHE----FSGGQCQRIGIARALI 179
Cdd:PRK13638 84 QDP----EQQIFYTDIdsdIAFSLRNL--GVPEAEITRRVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 180 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVY 252
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
38-255 |
9.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSeeEWRKARSDIQMIFQDPLASLnprm 117
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKLVGIVFQNPETQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 tIGDIIAEPLrTYHPS---MPRQEVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK13644 91 -VGRTVEEDL-AFGPEnlcLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 195 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVkHISDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-246 |
1.33e-23 |
|
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: 96.06 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVhfNIKDGRqwfwqpakTLKavdGVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRVAWLGRDLL 88
Cdd:cd03217 1 LEIKDLHV--SVGGKE--------ILK---GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 89 GQSEEEwrKARSDIQMIFQDPLASlnPRMTIGDIIaeplrtyhpsmprqevkdrvktmmmkvgllpnlinRYPHE-FSGG 167
Cdd:cd03217 68 DLPPEE--RARLGIFLAFQYPPEI--PGVKNADFL-----------------------------------RYVNEgFSGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHI-SDRVLVMYLGHAVELG 246
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
54-259 |
1.40e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.18 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 54 VVGESGCGKSTLARAIIGLVKATEGRVAwLGRDLLGQSEE------EWRKarsdIQMIFQDplASLNPRMTI-GDIiaep 126
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIV-LNGRVLFDAEKgiclppEKRR----IGYVFQD--ARLFPHYKVrGNL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 127 lrTY--HPSMPRQevKDRVktmmmkVGLL--PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 202
Cdd:PRK11144 98 --RYgmAKSMVAQ--FDKI------VALLgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 203 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ-HPY 259
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
243-310 |
1.58e-23 |
|
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: 91.69 E-value: 1.58e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 243 VELGTYSEVYNNPQHPYTRALMSAVPIPDPdreKNKEIQLLEGELPSPINPPSGCVFRTRCPIAGPEC 310
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP---PKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-252 |
1.59e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.27 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 28 WFWQPAKTL--KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwLGRDLLGQS--EEEWRKARSDIQ 103
Cdd:PRK13643 9 YTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTskQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 104 MIFQDPLASLNPRMTIGDIIAEPlrtYHPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVY 252
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
29-250 |
2.00e-23 |
|
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: 100.93 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKT-LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkarSDIQMIFQ 107
Cdd:TIGR02204 345 FAYPARPdQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELR---ARMALVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 DPLASLNPRMtigdiiaEPLRTYHPSMPRQEVKDRVKTMMMK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILE 181
Cdd:TIGR02204 422 DPVLFAASVM-------ENIRYGRPDATDEEVEAAARAAHAHefISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 182 PKLIICDEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:TIGR02204 495 APILLLDEATSALD----AESEQLVQQaLETLMkGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAE 560
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-243 |
6.29e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.95 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 3 AVAEKKVLLEIADLKVHfnikdgrqwfwqPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAW 82
Cdd:COG3845 250 PAEPGEVVLEVENLSVR------------DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 83 LGRDLLGQSEEEWRKARsdIQMIFQDPLAS-LNPRMTIGDIIAepLRTYH-------PSMPRQEVKDRVKTMM--MKVgl 152
Cdd:COG3845 318 DGEDITGLSPRERRRLG--VAYIPEDRLGRgLVPDMSVAENLI--LGRYRrppfsrgGFLDRKAIRAFAEELIeeFDV-- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 153 lpnlinRYPHE------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAV 226
Cdd:COG3845 392 ------RTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDE 464
|
250
....*....|....*..
gi 1799545459 227 VKHISDRVLVMYLGHAV 243
Cdd:COG3845 465 ILALSDRIAVMYEGRIV 481
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
36-254 |
8.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.31 E-value: 8.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQ---SEEEW------------RKA-- 98
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktKEKEKvleklviqktrfKKIkk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 99 ----RSDIQMIFQDPLASLNPRMTIGDIIAEPLrtyhpSM--PRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRI 172
Cdd:PRK13651 100 ikeiRRRVGVVFQFAEYQLFEQTIEKDIIFGPV-----SMgvSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 173 GIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG-TYSEV 251
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGdTYDIL 253
|
...
gi 1799545459 252 YNN 254
Cdd:PRK13651 254 SDN 256
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
37-253 |
8.77e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 99.04 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDP------- 109
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQEPyifsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 ----LASLNPRMTIGDIIAeplrtyhpSMPRQEVKDRVKTMMMKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:TIGR01193 565 lenlLLGAKENVSQDEIWA--------ACEIAEIKDDIENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 186 ICDEPVSALDVSIQAQVVNLLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYN 253
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
37-254 |
1.39e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV---KATEGRVAWLGRDLL--GQSEEEWRKARSDIQMIFQDplA 111
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQreGRLARDIRKSRANTGYIFQQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRMT------IGDIIAEPL-RTYHPSMPRQEvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:PRK09984 96 NLVNRLSvlenvlIGALGSTPFwRTCFSWFTREQ-KQRALQALTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 185 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTySEVYNN 254
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS-SQQFDN 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
41-223 |
2.60e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.30 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARS-DIQMIFQDPLasLNPRMTI 119
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkHVGFVFQSFM--LIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEP--LRtyhpSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK10584 106 LENVELPalLR----GESSRQSRNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHD 223
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
39-237 |
2.70e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwlgrdllgqseeewRKARSDIQMIFQDPlaslnpRMT 118
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RPAGARVLFLPQRP------YLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDiiaepLR---TYhPSMPRQEVKDRVKTMMMKVGLlPNLINRY------PHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:COG4178 439 LGT-----LRealLY-PATAEAFSDAELREALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799545459 190 PVSALDVSIQAQvvnLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:COG4178 512 ATSALDEENEAA---LYQLLREELpGTTVISVGHRSTLAAF-HDRVLEL 556
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
38-250 |
3.93e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.95 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLaraiIGLVK----ATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDPLasL 113
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQrvfdPQSGRILIDGTDIRTVTRASLRRN---IAVVFQDAG--L 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMtigdiIAEPLRTYHPSMPRQEVKDRVKT------MMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:PRK13657 421 FNRS-----IEDNIRVGRPDATDEEMRAAAERaqahdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-246 |
4.51e-22 |
|
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: 92.23 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSeeewrKARSDIQMIFQDplASLNPRMTIGDI 122
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 IAEPLrtyHPSMPRQEV-KDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:TIGR01277 91 IGLGL---HPGLKLNAEqQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
37-251 |
6.12e-22 |
|
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: 96.47 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDL--LGQSEeewrkARSDIQMIFQDP---LA 111
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqIDPAD-----LRRNIGYVPQDPrlfYG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRMTIGDIIAEplrtyhpsmprqevkdrvKTMMMKV----GLLpNLINRYPHEF-----------SGGQCQRIGIAR 176
Cdd:TIGR03375 554 TLRDNIALGAPYAD------------------DEEILRAaelaGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQvvnLLQQLQREM-GLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEER---FKDRLKRWLaGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQV 686
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
41-255 |
6.38e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.71 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLASlnpRMTIG 120
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEPVLF---SGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 DIIAEPLRTYhpsmPRQEVKDRVKTMMMK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:TIGR00958 573 ENIAYGLTDT----PDEEIMAAAKAANAHdfIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 195 DVSIQAqvvnLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:TIGR00958 649 DAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
34-255 |
6.80e-22 |
|
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: 92.22 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgQSEEEWRKARSDIQMIFQDplASL 113
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLPMHKRARLGIGYLPQE--ASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIGDIIAEPLRTYHPsmPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:cd03218 87 FRKLTVEENILAVLEIRGL--SKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 194 LD-VSIQaQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:cd03218 164 VDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
38-265 |
7.68e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.92 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARA------IIGLVKAtEGRVAWLGRDLLGqSEEEWRKARSDIQMIFQDPla 111
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRV-EGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 slNP-RMTIGDIIAEPLRT--YHPSMP-------RQ-----EVKDRVKTMmmkvGLlpnlinryphEFSGGQCQRIGIAR 176
Cdd:PRK14243 101 --NPfPKSIYDNIAYGARIngYKGDMDelverslRQaalwdEVKDKLKQS----GL----------SLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVM---------YLGHAVELGT 247
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDR 242
|
250
....*....|....*...
gi 1799545459 248 YSEVYNNPQHPYTRALMS 265
Cdd:PRK14243 243 TEKIFNSPQQQATRDYVS 260
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-260 |
9.81e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 9.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrVAWLGRDLLG-QSEEEWRKA---RSDIQMIFQDPlaslN 114
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGgRSIFNYRDVlefRRRVGMLFQRP----N 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 P-RMTIGDIIAEPLRTyHPSMPRQEVKDRVKTMMMKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK14271 112 PfPMSIMDNVLAGVRA-HKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYT 260
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-252 |
1.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSE-EEWRKARSDIQMIFQDPLASLNP 115
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGDIIAEPlRTYHPSMPRQEVKDRVKTMMmkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13649 101 ETVLKDVAFGP-QNFGVSQEEAEALAREKLAL--VGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 196 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVY 252
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-253 |
1.59e-21 |
|
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: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFNIKDG-----RQWFWQPAKTLK----AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG--- 78
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslKELLLRRRRTRReefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrve 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 79 ---RVAWL------------GRD-------LLGQSEEEWRKARSDIqmI-FQDplaslnprmtIGDIIAEPLRTYhpsmp 135
Cdd:COG1134 85 vngRVSALlelgagfhpeltGREniylngrLLGLSRKEIDEKFDEI--VeFAE----------LGDFIDQPVKTY----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 136 rqevkdrvktmmmkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGL 215
Cdd:COG1134 148 -----------------------------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GR 197
|
250 260 270
....*....|....*....|....*....|....*...
gi 1799545459 216 SLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYN 253
Cdd:COG1134 198 TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-236 |
2.27e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK--ATEGRVAWLGRDLLGQS--EEEwrkaRSDIQMIFQDpLAs 112
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNirDTE----RAGIAIIHQE-LA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 113 LNPRMTIGDII---AEPlrTYHPSMPRQEVKDRVKTMMMKVGLLPNlINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK13549 93 LVKELSVLENIflgNEI--TPGGIMDYDAMYLRAQKLLAQLKLDIN-PATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799545459 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICV 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
34-237 |
4.29e-21 |
|
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: 89.58 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwlgrdLLGQSEEEWRKARSDIQMIFQDPlaSL 113
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGKSYQKNIEALRRIGALIEAP--GF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIgdiiAEPLRTYH--PSMPRQEVkDRVKTMmmkVGLlpnliNRYPHE----FSGGQCQRIGIARALILEPKLIIC 187
Cdd:cd03268 84 YPNLTA----RENLRLLArlLGIRKKRI-DEVLDV---VGL-----KDSAKKkvkgFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGII 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
35-268 |
7.76e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 7.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG--RVAwlGRDLLG-QSEEEWRKARSDIQMIFQDplA 111
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVA--GQDVATlDADALAQLRREHFGFIFQR--Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRMTIGDIIAEPlrTYHPSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK10535 96 HLLSHLTAAQNVEVP--AVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 192 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVelgtySEVYNNPQHPYTRALMSAVP 268
Cdd:PRK10535 173 GALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV-----RNPPAQEKVNVAGGTEPVVN 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-243 |
8.94e-21 |
|
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: 92.58 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK--ATEGRVAWLGRDLLGQSEEEwrKARSDIQMIFQDplASL 113
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRD--TERAGIVIIHQE--LTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTI------GDIIAEP-LRTYHPSMPRqevkdRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:TIGR02633 90 VPELSVaeniflGNEITLPgGRMAYNAMYL-----RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
33-237 |
9.39e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 9.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 33 AKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARS---DIQMIFQDp 109
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSycaQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 laslnprmTIGDIIAEP--LRTYHPSMprqevkDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:PRK10247 96 --------TVYDNLIFPwqIRNQQPDP------AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
38-247 |
1.36e-20 |
|
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: 88.32 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPL------- 110
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNPRMTIGDI-IAEPLRTYHpsmprqeVKDRVKTMmmkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:cd03244 96 SNLDPFGEYSDEeLWQALERVG-------LKEFVESL---PGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 190 PVSALDVsiqaQVVNLLQQLQREM--GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT 247
Cdd:cd03244 166 ATASVDP----ETDALIQKTIREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-241 |
2.04e-20 |
|
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: 88.16 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 11 LEIADLKVHFNIKDGRQWFWQPAKTL--------KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAW 82
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKSLfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 83 LGRD--------------LLGQSEEEWRkarsDIQmifqdPLASLNPRMTIGDIiaeplrtyhpsmPRQEVKDRVK--TM 146
Cdd:cd03267 81 AGLVpwkrrkkflrrigvVFGQKTQLWW----DLP-----VIDSFYLLAAIYDL------------PPARFKKRLDelSE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 147 MMKVGLLPNLINRyphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAV 226
Cdd:cd03267 140 LLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKD 216
|
250
....*....|....*
gi 1799545459 227 VKHISDRVLVMYLGH 241
Cdd:cd03267 217 IEALARRVLVIDKGR 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-246 |
3.06e-20 |
|
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: 87.59 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 23 KDGRQWFWqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG------RVAWL------------G 84
Cdd:cd03220 29 KGEVGEFW-------ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtvtvrgRVSSLlglgggfnpeltG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 85 RD-------LLGQSEEEWRKARSDIQMiFQDplaslnprmtIGDIIAEPLRTYhpsmprqevkdrvktmmmkvgllpnli 157
Cdd:cd03220 102 REniylngrLLGLSRKEIDEKIDEIIE-FSE----------LGDFIDLPVKTY--------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 158 nryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03220 144 -------SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVL 215
|
....*....
gi 1799545459 238 YLGHAVELG 246
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
37-247 |
6.54e-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: 86.31 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLaslnpr 116
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPT------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 mtigdIIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLpNLinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03369 93 -----LFSGTIRSNLDPFDEYSDEEIYGALRVSEGGL-NL--------SQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 197 SIQAqvvnLLQQLQREM--GLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGT 247
Cdd:cd03369 159 ATDA----LIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
39-251 |
1.75e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEeewRKARSDIQMIFQDPLASLNPRmt 118
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRVASVPQDTSLSFEFD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 iGDIIAEPLRTYHPSM--PRQEVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK09536 94 -VRQVVEMGRTPHRSRfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 197 SIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:PRK09536 173 NHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
39-251 |
1.89e-19 |
|
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: 85.91 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG-RVAWLGRDLLGQSEEEWRK----ARSDIQMIFQdplasl 113
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKriglVSPALQLRFP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 nPRMTIGDIIAeplrT-YHPSM-----PRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:COG1119 93 -RDETVLDVVL----SgFFDSIglyrePTDEQRERARELLELLGLAH-LADRPFGTLSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHdlavvkHISD------RVLVMYLGHAVELGTYSEV 251
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVEEippgitHVLLLKDGRVVAAGPKEEV 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-224 |
2.17e-19 |
|
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: 88.57 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 3 AVAEKKVLLEIADLKVHfnikdgrqwfWQPAKtlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAW 82
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAG----------YPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 83 LGRDLLGQSEEEWRKArsdIQMIFQDPlaslnprMTIGDIIAEPLRTYHPSMPRQEVKDrvktMMMKVGLLpNLINRYPH 162
Cdd:TIGR02868 395 DGVPVSSLDQDEVRRR---VSVCAQDA-------HLFDTTVRENLRLARPDATDEELWA----ALERVGLA-DWLRALPD 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 163 -----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDL 224
Cdd:TIGR02868 460 gldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-243 |
2.22e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARsdIQMIFQDPLAS-LNP 115
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAG--IAYVPEDRKGEgLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGD-IIAEPLRTYHPSM---PRQEVKD--------RVKT--MMMKVGLLpnlinryphefSGGQCQRIGIARALILE 181
Cdd:COG1129 344 DLSIREnITLASLDRLSRGGlldRRRERALaeeyikrlRIKTpsPEQPVGNL-----------SGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-255 |
2.73e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwlgrdLLGQSEEEWRK---ARSDIQMI 105
Cdd:PRK10575 19 FRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-----LDAQPLESWSSkafARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 FQDPLASlnpRMTIGDIIAEPLRTYHPSMPRQEVKDR--VKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:PRK10575 92 QQLPAAE---GMTVRELVAIGRYPWHGALGRFGAADRekVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
39-251 |
3.59e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.17 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKA----RSDIQMiFQDPLASLN 114
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHigylPQDVEL-FPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMtigDIIAEPLRTYHPSmprqevkdrvktmmmKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPK 183
Cdd:TIGR01842 413 ARF---GENADPEKIIEAA---------------KLAGVHELILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
42-251 |
4.23e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVaWLGRDLLGQ--SEEEWRKarsdIQMIFQDPlaslnprMTI 119
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHyaSKEVARR----IGLLAQNA-------TTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEPL--RTYHPSMP-----RQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK10253 94 GDITVQELvaRGRYPHQPlftrwRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
34-246 |
5.14e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 84.24 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV---KATEGRVAWLGRDLlgqSEEEWRKARSdiqmiFQDPL 110
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR---KPDQFQKCVA-----YVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNPRMTIgdiiAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLPNL-INRYPHEF----SGGQCQRIGIARALILEPKLI 185
Cdd:cd03234 90 DILLPGLTV----RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLaLTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-280 |
1.06e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.78 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRV----------AWLGR------------------ 85
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcGYVERpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 --DLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAeplrtyhpSMPRQEVKDRvKTMMMKVGLLP--NLINRYP 161
Cdd:TIGR03269 93 evDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLE--------ALEEIGYEGK-EAVGRAVDLIEmvQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 162 H---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:TIGR03269 164 HiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1799545459 239 LGHAVELGTYSEVYNnpqhpytrALMSAVpiPDPDREKNKEI 280
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA--------VFMEGV--SEVEKECEVEV 275
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-241 |
1.08e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsDIQMIFQDPLA------- 111
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN--GIVYISEDRKRdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRMTI---GDIIAEPLRTYHpSMPRQEVKD-----RVKT--MMMKVGLLpnlinryphefSGGQCQRIGIARALILE 181
Cdd:PRK10762 346 SVKENMSLtalRYFSRAGGSLKH-ADEQQAVSDfirlfNIKTpsMEQAIGLL-----------SGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
37-256 |
1.29e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVaWL-GRDLLGQSEeeWRKARSDIQMIFQDPlaSLNP 115
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLdGEDITHLPM--HKRARLGIGYLPQEA--SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 116 RMTIGD---IIAEPLRtyhpsMPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:COG1137 92 KLTVEDnilAVLELRK-----LSKKEREERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 193 ALD---VS-IQAQVVNLlqqlqREMGLSlIFIA-HD----LAVVkhisDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:COG1137 166 GVDpiaVAdIQKIIRHL-----KERGIG-VLITdHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
36-254 |
1.36e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrKARSDIQMIFQ-----DPL 110
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL--AAQLGIGIIYQelsviDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNP----RMTIGDIIAEPLRTYhpsmprQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:PRK09700 96 TVLENlyigRHLTKKVCGVNIIDW------REMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
36-243 |
1.70e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseEEWRKARsdiqmIFQDPLA---- 111
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-----TDWQTAK-----IMREAVAivpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 --SLNPRMTI------GDIIAEplrtyhpsmpRQEVKDRVKTMMmkvGLLPNLINRYPHE---FSGGQCQRIGIARALIL 180
Cdd:PRK11614 88 grRVFSRMTVeenlamGGFFAE----------RDQFQERIKWVY---ELFPRLHERRIQRagtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799545459 181 EPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
34-256 |
1.86e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRD--LLGQSEeewrKARSDIQMIFQDplA 111
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHA----RARRGIGYLPQE--A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRMTIGDIIAEPLRTYHpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 192 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
39-251 |
2.30e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWrkARSdIQMIFQDPLAslnPR-M 117
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--ARR-LALLPQHHLT---PEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYHPSMPRQEVKDR--VKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK11231 92 TVRELVAYGRSPWLSLWGRLSAEDNarVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 196 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:PRK11231 171 INHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-246 |
2.76e-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: 81.21 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwLGRDLLGQSEEEWRKARSDIQmifqd 108
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDLEKALSSLISVLN----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 plaslnprmtigdiiaeplrtyhpsmprQEVKDRVKTMMMKVGLlpnlinryphEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03247 82 ----------------------------QRPYLFDTTLRNNLGR----------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 189 EPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELG 246
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-247 |
2.92e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.77 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 6 EKKVLLEIADLKVHFNikdgrqwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIG--LVKATEGRVAWL 83
Cdd:CHL00131 3 KNKPILEIKNLHASVN-------------ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 84 GRDLLGQSEEEwrKARSDIQMIFQDP-------------LASLNPRMTIGDIIAEPLRTYHPSMPRQEVkdrvktmmmkV 150
Cdd:CHL00131 70 GESILDLEPEE--RAHLGIFLAFQYPieipgvsnadflrLAYNSKRKFQGLPELDPLEFLEIINEKLKL----------V 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 151 GLLPNLINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDVS---IQAQVVNLLQQLQRemglSLIFIAHDLAV 226
Cdd:CHL00131 138 GMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRL 213
|
250 260
....*....|....*....|..
gi 1799545459 227 VKHIS-DRVLVMYLGHAVELGT 247
Cdd:CHL00131 214 LDYIKpDYVHVMQNGKIIKTGD 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-235 |
8.75e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.97 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG----QSEEEWR---KARSDIQMIFQDPL 110
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAyvpqRSEVPDSlplTVRDLVAMGRWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNPrmtigdiiaeplrtyhpsmPRQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:NF040873 87 GLWRR-------------------LTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL 235
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
40-250 |
9.61e-18 |
|
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: 84.10 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDPLasL-Nprmt 118
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---IGIVPQDTV--LfN---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 igDIIAEPLRTYHPSMPRQEVKDRVKtmmmkvglLPNLinrypHEF-------------------SGGQCQRIGIARALI 179
Cdd:COG5265 446 --DTIAYNIAYGRPDASEEEVEAAAR--------AAQI-----HDFieslpdgydtrvgerglklSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 180 LEPKLIICDEPVSALDV----SIQAQvvnlLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:COG5265 511 KNPPILIFDEATSALDSrterAIQAA----LREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAE 578
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-240 |
1.01e-17 |
|
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: 83.72 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 30 WQPAKT-LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGlvkATEGRvaWLGRDLLGQSEEEWRKA----RSDIQM 104
Cdd:TIGR02633 266 WDVINPhRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG---AYPGK--FEGNVFINGKPVDIRNPaqaiRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 105 IFQD----------------PLASLNPRMTIGDIIAEP-LRTYHPSMPRQEVKdrvktmmmkvGLLPNL-INRypheFSG 166
Cdd:TIGR02633 341 VPEDrkrhgivpilgvgkniTLSVLKSFCFKMRIDAAAeLQIIGSAIQRLKVK----------TASPFLpIGR----LSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 240
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
41-237 |
1.45e-17 |
|
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: 80.21 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLasLNPRmTIG 120
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEPV--LFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 DIIAEPLrtyhPSMPRQEVKDRVKTMMMKvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:cd03248 106 DNIAYGL----QSCSFECVKEAAQKAHAH-SFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799545459 194 LDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03248 181 LDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-240 |
2.66e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 78.75 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 26 RQWFWQPAKTLkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK--ATEGRVAWLGRDLlgqSEEEWRKArsdIQ 103
Cdd:cd03213 14 KSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPL---DKRSFRKI---IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 104 MIFQDplaslnprmtigDIIaeplrtyHPSMPRQEvkdrvkTMMMKVGLlpnlinrypHEFSGGQCQRIGIARALILEPK 183
Cdd:cd03213 86 YVPQD------------DIL-------HPTLTVRE------TLMFAAKL---------RGLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDL-AVVKHISDRVLVMYLG 240
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-240 |
2.68e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 30 WQPAKT-LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK-ATEGRVAWLGRDLLGQSEEEwrKARSDIQMIFQ 107
Cdd:PRK13549 268 WDPVNPhIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 D----------------PLASLNpRMTIGDII--AEPLRTYHPSMPRQEVKdrVKTMMMKVGLLpnlinryphefSGGQC 169
Cdd:PRK13549 346 DrkrdgivpvmgvgkniTLAALD-RFTGGSRIddAAELKTILESIQRLKVK--TASPELAIARL-----------SGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 240
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-237 |
4.98e-17 |
|
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: 78.53 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 30 WQPAktLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWR-KARSDIQMIFQD 108
Cdd:cd03290 10 WGSG--LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 PLAsLNPRMTIGDIIAEPLRtyhpsmprqevKDRVKTMMMKVGLLPNlINRYPH-----------EFSGGQCQRIGIARA 177
Cdd:cd03290 88 PWL-LNATVEENITFGSPFN-----------KQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 178 LILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAM 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
43-222 |
9.10e-17 |
|
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: 76.42 E-value: 9.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwlgrdllgqseeewRKARSDIQMIfqdplaslnprmtigdi 122
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------MPEGEDLLFL----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 iaePLRTYhpsmprqevkdrvktmmMKVGLLPNLINrYP--HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:cd03223 70 ---PQRPY-----------------LPLGTLREQLI-YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 1799545459 201 QVVNLLqqlqREMGLSLIFIAH 222
Cdd:cd03223 129 RLYQLL----KELGITVISVGH 146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
42-235 |
1.24e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrKARSDIQMifqdPLA-----SLNPR 116
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ---KLYLDTTL----PLTvnrflRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIaeplrtyhPSMPRQEVKDRVKTMMMKVgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK09544 96 TKKEDIL--------PALKRVQAGHLIDAPMQKL--------------SGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1799545459 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 235
Cdd:PRK09544 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-236 |
1.25e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.62 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLR-----LYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWlgrDLlgqseeewrkarsDI----QMIFQ 107
Cdd:PRK13409 348 KKLGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---EL-------------KIsykpQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 DPlaslnpRMTIGDIIAEPLRTYHPSMPRQEVKDRVKtmmmkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:PRK13409 412 DY------DGTVEDLLRSITDDLGSSYYKSEIIKPLQ--------LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-240 |
1.53e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 32 PAKTLkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWlgrdllgqseeewrkaRSDIQMIF--QDP 109
Cdd:COG0488 9 GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------------PKGLRIGYlpQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 laSLNPRMTIGD-----------IIAEPLRTYH-PSMPRQEVKD------------------RVKTMMMKVGLLPNLINR 159
Cdd:COG0488 71 --PLDDDLTVLDtvldgdaelraLEAELEELEAkLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 160 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQaqvvnLLQQ-LQREMGlSLIFIAHD---L-AVVKHI--- 230
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEfLKNYPG-TVLVVSHDryfLdRVATRIlel 222
|
250
....*....|
gi 1799545459 231 SDRVLVMYLG 240
Cdd:COG0488 223 DRGKLTLYPG 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-255 |
1.78e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.14 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkarSDIQMIFQD 108
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR---SRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 PLaslnprmTIGDIIAEPLRTYHPSMPRQEVKdrvktmmmKVGLLPNL---INRYPHEF-----------SGGQCQRIGI 174
Cdd:PRK10789 398 PF-------LFSDTVANNIALGRPDATQQEIE--------HVARLASVhddILRLPQGYdtevgergvmlSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 175 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQ 539
|
.
gi 1799545459 255 P 255
Cdd:PRK10789 540 S 540
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-236 |
3.00e-16 |
|
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: 79.44 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLR-----LYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdllgqsEEEWRKA------RSDIQMI 105
Cdd:COG1245 349 KSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKISykpqyiSPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 FQDPLASLNPRMTIGDI----IAEPLRtyhpsmprqevkdrvktmmmkvglLPNLINRYPHEFSGGQCQRIGIARALILE 181
Cdd:COG1245 418 VEEFLRSANTDDFGSSYykteIIKPLG------------------------LEKLLDKNVKDLSGGELQRVAIAACLSRD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
41-227 |
3.55e-16 |
|
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: 75.86 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkarsdiQMIFQDPLASLNPRMTIg 120
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLGHLPGLKPELSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 diiAEPLRTYHPSMprQEVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:TIGR01189 91 ---LENLHFWAAIH--GGAQRTIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....*...
gi 1799545459 201 QVVNLL-QQLQREmGLSLIFIAHDLAVV 227
Cdd:TIGR01189 165 LLAGLLrAHLARG-GIVLLTTHQDLGLV 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
41-227 |
3.64e-16 |
|
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: 75.61 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDlLGQSEEEWRKArsdiqMIFQDPLASLNPRMTig 120
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-LDFQRDSIARG-----LLYLGHAPGIKTTLS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 diIAEPLRTYHPSMPRQEVKDRVKTMMmkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:cd03231 90 --VLENLRFWHADHSDEQVEEALARVG-----LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|....*..
gi 1799545459 201 QVVNLLQQLQREMGLSLIFIAHDLAVV 227
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
39-246 |
3.90e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSeeewRKARSDIQMIFQdpLASLNPRMT 118
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA----RLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 igdiIAEPLRTY--HPSMPRQEVkDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK13536 131 ----VRENLLVFgrYFGMSTREI-EAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1799545459 197 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:PRK13536 206 HARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-236 |
7.02e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRD--------------LLGQseeewrkaR 99
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkefarrigvVFGQ--------R 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 100 SdiQMIFQDPLA-SLNprmTIGDIiaeplrtYhpSMPRQEVKDRVKTM--MMKVGllpNLINRYPHEFSGGQCQRIGIAR 176
Cdd:COG4586 105 S--QLWWDLPAIdSFR---LLKAI-------Y--RIPDAEYKKRLDELveLLDLG---ELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-250 |
8.03e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.14 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMI--- 105
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQVALVsqn 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 ---FQDplaslnprmTIGDIIAEPlRTYHPSMPRQEVKDRVKTMMmkvgllpNLINRYPHEF-----------SGGQCQR 171
Cdd:PRK11176 426 vhlFND---------TIANNIAYA-RTEQYSREQIEEAARMAYAM-------DFINKMDNGLdtvigengvllSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 172 IGIARALILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQREMgLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGT 247
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQKNR-TSLV-IAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
...
gi 1799545459 248 YSE 250
Cdd:PRK11176 562 HAE 564
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
42-241 |
2.33e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEeewrKARSDIQMIF--QDPLASlnprmti 119
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST----AQRLARGLVYlpEDRQSS------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEPLR------TYH-PSMPRQEVKDR--VKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK15439 351 GLYLDAPLAwnvcalTHNrRGFWIKPARENavLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-250 |
4.55e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 8 KVLLEIADLKVHFnikDGRQWFwqpaktlkavDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWlGRDL 87
Cdd:COG0488 313 KKVLELEGLSKSY---GDKTLL----------DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 88 -LG---QSEEEwrkarsdiqmifqdplasLNPRMTIGDIIAEplrtYHPSMPRQEVK----------DRVKTmmmKVGLL 153
Cdd:COG0488 379 kIGyfdQHQEE------------------LDPDKTVLDELRD----GAPGGTEQEVRgylgrflfsgDDAFK---PVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 154 pnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQAqVVNLLQQLQremGlSLIFIAHDLAVVKHISD 232
Cdd:COG0488 434 -----------SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP---G-TVLLVSHDRYFLDRVAT 497
|
250
....*....|....*....
gi 1799545459 233 RVLVMYLGHAVE-LGTYSE 250
Cdd:COG0488 498 RILEFEDGGVREyPGGYDD 516
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-237 |
4.68e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKArsDIQMIFQDplasLN-- 114
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA--GIGIIHQE----LNli 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDII---AEPLRTY----HPSMPRQEVKdrvktmmmkvgLLPNL-INRYPH----EFSGGQCQRIGIARALILEP 182
Cdd:PRK10762 92 PQLTIAENIflgREFVNRFgridWKKMYAEADK-----------LLARLnLRFSSDklvgELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 183 KLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
41-251 |
5.19e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 73.67 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRVAWLGRDLLGQSEEEwrKARSDIQMIFQDP--LASLNPR 116
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQYPveIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGDIIAEpLRTY--HPSMPRQEVKDRVKTMMMKVGLLPNLINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK09580 97 FFLQTALNA-VRSYrgQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 194 LDV---SIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHIS-DRVLVMYLGHAVELGTYSEV 251
Cdd:PRK09580 176 LDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDFTLV 233
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
39-251 |
6.55e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.19 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWrkARSdIQMIFQDPlaSLNPRMT 118
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--AKR-LAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIA---EPlrtYHPSMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:COG4604 92 VRELVAfgrFP---YSKGRLTAEDREIIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:COG4604 168 MKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-236 |
7.76e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 72.83 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 46 LYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEeewrKARSDIQMIFQDPLASLNPRMTIgdiiae 125
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ----YIKADYEGTVRDLLSSITKDFYT------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 126 plrtyHPSMprqevkdrvKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 205
Cdd:cd03237 92 -----HPYF---------KTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|.
gi 1799545459 206 LQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
42-229 |
9.53e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWrkARSDIQMIFQDPL----------- 110
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKW--WRSKIGVVSQDPLlfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ------------------------ASLNPRMTIGDIIAEPL---------------RTYHPSMPRQEVKDRVKTMMMK-- 149
Cdd:PTZ00265 482 yslyslkdlealsnyynedgndsqENKNKRNSCRAKCAGDLndmsnttdsneliemRKNYQTIKDSEVVDVSKKVLIHdf 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 150 VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLA 225
Cdd:PTZ00265 562 VSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
....
gi 1799545459 226 VVKH 229
Cdd:PTZ00265 642 TIRY 645
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-255 |
9.54e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKaTEGRVAWLGRDLLGQSEEEWRKArsdIQMIFQDPL---ASLNPRMT 118
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKH---LSWVGQNPQlphGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRTYHpSMPRQEVKDRVKtmmmkvgLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK11174 445 LGNPDASDEQLQQ-ALENAWVSEFLP-------LLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799545459 195 DVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYSEVYNNP 255
Cdd:PRK11174 517 DAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-268 |
2.34e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSdiqMIFQDP-LASLNPRMTI 119
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS---IIPQSPvLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 gdiiaEPLRTYH-----PSMPRQEVKDRVKTMMMKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PLN03232 1331 -----DPFSEHNdadlwEALERAHIKDVIDRNPFG---LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 195 DVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSAVP 268
Cdd:PLN03232 1403 DVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
40-237 |
2.47e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.01 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWlgrdllgqseeewrkarsdiqmifqdplaslNPRMTI 119
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------------------------GSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GdiiaeplrtyhpsmprqevkdrvktmmmkvgllpnlinrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 199
Cdd:cd03221 66 G---------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190
....*....|....*....|....*....|....*...
gi 1799545459 200 AQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03221 107 EALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
39-251 |
3.28e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVAWLGRDLLGQSEEEWRKARSdiqMIFQDPLASLNprMT 118
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRA---YLSQQQSPPFA--MP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAeplRTYHPSMPRQEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALI-------LEPKLIICDEPV 191
Cdd:COG4138 86 VFQYLA---LHQPAGASSEAVEQLLAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 192 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:COG4138 162 NSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
49-232 |
4.72e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 49 GETLGVVGESGCGKSTLARAIIGLVKATEGRVAwlgrdLLGQSEEEWRKaRSDIQMIFQDPLASLNPRMTIGDIIAEPLR 128
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKIS-----ILGQPTRQALQ-KNLVAYVPQSEEVDWSFPVLVEDVVMMGRY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 129 TYHPSMPRQEVKDR--VKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 206
Cdd:PRK15056 107 GHMGWLRRAKKRDRqiVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170 180
....*....|....*....|....*.
gi 1799545459 207 QQLqREMGLSLIFIAHDLAVVKHISD 232
Cdd:PRK15056 186 REL-RDEGKTMLVSTHNLGSVTEFCD 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-250 |
5.83e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.55 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 2 NAVAEKKVLLEIADlkVHFNIKDGRQwfwqpaktlKAVDGVSLRLYEGETLGVVGESGCGKSTLaraiIGLV----KATE 77
Cdd:PRK11160 330 STAAADQVSLTLNN--VSFTYPDQPQ---------PVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLtrawDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 78 GRVAWLGRDLLGQSEEEWRKARSDIQM---IFQDplaslnprmTIGD--IIAEPLRTyhpsmprqevKDRVKTMMMKVGL 152
Cdd:PRK11160 395 GEILLNGQPIADYSEAALRQAISVVSQrvhLFSA---------TLRDnlLLAAPNAS----------DEALIEVLQQVGL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 153 lPNLINRYP----------HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAH 222
Cdd:PRK11160 456 -EKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
250 260
....*....|....*....|....*...
gi 1799545459 223 DLAVVKHIsDRVLVMYLGHAVELGTYSE 250
Cdd:PRK11160 533 RLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-244 |
7.93e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 12 EIADLKVHFNIKDGRQwfwqpakTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrvawlgrdllgqs 91
Cdd:COG2401 26 RVAIVLEAFGVELRVV-------ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 92 eeewrKARSDIqmifqdPLASLNPRMTIGDIIAeplrtyhpsmPRQEVKDRVKTMMMkVGLL-PNLINRYPHEFSGGQCQ 170
Cdd:COG2401 86 -----AGCVDV------PDNQFGREASLIDAIG----------RKGDFKDAVELLNA-VGLSdAVLWLRRFKELSTGQKF 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 171 RIGIARALILEPKLIICDEPVSALDVSiQAQVVNL-LQQLQREMGLSLIFIAHDLAVVKHIS-DRVLVMYLGHAVE 244
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-208 |
8.61e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 10 LLEIADLKVhfnIKDGRQWFwqpaktlkavDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG 89
Cdd:PRK13538 1 MLEARNLAC---ERDERILF----------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QSEEEWRkarsdiQMIFQDPLASLNPRMTigdiIAEPLRTYHPsMPRQEVKDRVKTMMMKVGL-----LPnlinryPHEF 164
Cdd:PRK13538 68 QRDEYHQ------DLLYLGHQPGIKTELT----ALENLRFYQR-LHGPGDDEALWEALAQVGLagfedVP------VRQL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799545459 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ 208
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
55-250 |
2.98e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 55 VGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEeewRKARSDIQMIFQDPL---ASLNPRMTIGDIIAEplrtyh 131
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDPVvlaDTFLANVTLGRDISE------ 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 132 psmprqevkDRVKTMMMKVGL------LPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK10790 444 ---------EQVWQALETVQLaelarsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799545459 202 VVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSE 250
Cdd:PRK10790 515 IQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-244 |
3.27e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.20 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAT--EGRVAWLG-----RDLlGQSEEEwrkarsDIQMIFQDp 109
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGevcrfKDI-RDSEAL------GIVIIHQE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 110 LAsLNPRMTIGDII---AEPLRtyHPSMPRQEVKDRVKTMMMKVGLLPNlinryPHEFSG----GQCQRIGIARALILEP 182
Cdd:NF040905 87 LA-LIPYLSIAENIflgNERAK--RGVIDWNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 183 KLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
30-237 |
4.70e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 67.11 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 30 WQPAKTL--KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLG----------------RD--LLG 89
Cdd:cd03250 10 WDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvsqepwiqngtiREniLFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 90 QS-EEEWRKA-------RSDIQMifqdplaslnprMTIGDiiaeplRTyhpsmprqEVKDRvktmmmkvGLlpNLinryp 161
Cdd:cd03250 90 KPfDEERYEKvikacalEPDLEI------------LPDGD------LT--------EIGEK--------GI--NL----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 162 hefSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVN-LLQQLQREMGLSL---IFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03250 129 ---SGGQKQRISLARAVYSDADIYLLDDPLSAVD----AHVGRhIFENCILGLLLNNktrILVTHQLQLLPH-ADQIVVL 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-238 |
6.71e-13 |
|
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: 67.39 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 48 EGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdllgQSEEEWRK-----ARSDIQMIFQdplaslnpRMTIGDI 122
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---------DDPPDWDEildefRGSELQNYFT--------KLLEGDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 123 IAEPLRTYHPSMPRQeVKDRV------------KTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:cd03236 88 KVIVKPQYVDLIPKA-VKGKVgellkkkdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799545459 191 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
41-207 |
8.28e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDllgqseEEWRKARSDIQMIfqDPLASLNPRMTIG 120
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYL--GHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 DII---AEPLRTyHPSMPRQEVKDrvktmmmkVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK13539 92 ENLefwAAFLGG-EELDIAAALEA--------VG-LAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170
....*....|
gi 1799545459 198 IQAQVVNLLQ 207
Cdd:PRK13539 162 AVALFAELIR 171
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-250 |
1.19e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 29 FWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAII-----GLVKAteGRVAWLGRDLlgqsEEEWRKARSDIQ 103
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKGS--GSVLLNGMPI----DAKEMRAISAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 104 MifQDPLasLNPRMTIGD--IIAEPLRtyhpsMPRQEVKD----RVKTMMMKVGLLP--NLINRYPHE---FSGGQCQRI 172
Cdd:TIGR00955 105 Q--QDDL--FIPTLTVREhlMFQAHLR-----MPRRVTKKekreRVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 173 GIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL-QRemGLSLIFIAHD-LAVVKHISDRVLVMYLGHAVELGTYSE 250
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-220 |
2.22e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRvAWlgrdLLGQSEEewrkARsDIQMifqdplaslnpRM 117
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-AW----LFGQPVD----AG-DIAT-----------RR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIG------------------DIIAeplRTYHpsMPRQEVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALI 179
Cdd:NF033858 340 RVGymsqafslygeltvrqnlELHA---RLFH--LPAAEIAARVAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1799545459 180 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSlIFI 220
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFI 453
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-236 |
2.26e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdLLGQSEEEWRKAR----SDIQMIFQDplAS 112
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI------LIDGQEMRFASTTaalaAGVAIIYQE--LH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 113 LNPRMTigdiIAEPLrtYHPSMP-----------RQEVKDRVKTMMMKVGllPNLINRYpheFSGGQCQRIGIARALILE 181
Cdd:PRK11288 90 LVPEMT----VAENL--YLGQLPhkggivnrrllNYEAREQLEHLGVDID--PDTPLKY---LSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-284 |
3.65e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.84 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrDLLGQSeeewrkarSDIQMIfqdplASLNPRM 117
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA--------ALIAIS-----SGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 T-IGDIiaePLRTYHPSMPRQEVKDrVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK13545 101 TgIENI---ELKGLMMGLTKEKIKE-IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 197 SIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNpqhpYTRALMSAVPIPDPDREK 276
Cdd:PRK13545 177 TFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH----YDEFLKKYNQMSVEERKD 251
|
....*...
gi 1799545459 277 NKEIQLLE 284
Cdd:PRK13545 252 FREEQISQ 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-250 |
5.01e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSE-EEWRKARSDIQMIFQD---- 108
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRRDngff 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 109 PLASLNPRMTIGDIIAE-----PLRTYHPSMPRQEVKDRVKTMMMKVGLLPNLINryphEFSGGQCQRIGIARALILEPK 183
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSE 250
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
39-195 |
5.33e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.60 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSeeewRKARSDIQMIFQdpLASLNPRMT 118
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHARQRVGVVPQ--FDNLDPDFT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 119 IgdiiAEPLRTY--HPSMPRQEVKDRVKTMMmKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13537 97 V----RENLLVFgrYFGLSAAAARALVPPLL-EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-256 |
1.05e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAtEGRVAWLGRDLLGQSEEEWRKARSdiQMIFQDPLASLNPrmtigd 121
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRA--YLSQQQTPPFAMP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 122 iIAEPLRTYHPSMPR-QEVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIA-------RALILEPKLIICDEPVSA 193
Cdd:PRK03695 86 -VFQYLTLHQPDKTRtEAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 194 LDVsiqAQvVNLLQQLQREM---GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PRK03695 164 LDV---AQ-QAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-238 |
1.69e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.81 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLY------EGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdllgQSEEEWRK-----ARSDIQMIFQDpla 111
Cdd:COG1245 87 GFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---------DEEPSWDEvlkrfRGTELQDYFKK--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 slnprmtigdIIAEPLRTYH-PSM----PRQeVKDRVKTMMMKV---GL---------LPNLINRYPHEFSGGQCQRIGI 174
Cdd:COG1245 155 ----------LANGEIKVAHkPQYvdliPKV-FKGTVRELLEKVderGKldelaeklgLENILDRDISELSGGELQRVAI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 175 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
49-241 |
2.72e-11 |
|
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: 60.85 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 49 GETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGrdllgqseeewrkarsdiqmifqdplaslnprmtiGDIIAEPLR 128
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------------------------------GEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 129 tyhpsmprqevkdrvktmmmkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV-----V 203
Cdd:smart00382 47 ---------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1799545459 204 NLLQQLQREMGLSLIFIAHDL-----AVVKHISDRVLVMYLGH 241
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
39-251 |
2.74e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGrDLLGQSEEEWrkarsdIQMifqdplASLNPRMT 118
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAW------IQN------DSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPlrtyhpsmprqevkdRVKTMMMKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:TIGR00957 721 FGKALNEK---------------YYQQVLEACALLPDLeilpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 189 EPVSALDVSIQAQVvnlLQQLQREMGL----SLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR00957 786 DPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-235 |
4.23e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdllgQSEEEWRKARsdIQmifQDPlaslnPRMTI 119
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI---------IYEQDLIVAR--LQ---QDP-----PRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDI----------IAEPLRTYH---------PS------MPR-QEVKD---------RVKTMMMKVGLLPN-LINryphE 163
Cdd:PRK11147 81 GTVydfvaegieeQAEYLKRYHdishlvetdPSeknlneLAKlQEQLDhhnlwqlenRINEVLAQLGLDPDaALS----S 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 164 FSGGQCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 235
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
36-243 |
7.72e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDgvsLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEewrKARS-DIQMIFQDPLasLN 114
Cdd:PRK15439 27 LKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA---KAHQlGIYLVPQEPL--LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAepLRtyhpsMPR-QEVKDRVKTMMMKVGLLPNLinryphEFSGGQC-----QRIGIARALILEPKLIICD 188
Cdd:PRK15439 99 PNLSVKENIL--FG-----LPKrQASMQKMKQLLAALGCQLDL------DSSAGSLevadrQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 189 EPVSALdvsIQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:PRK15439 166 EPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-286 |
9.65e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSdiqMIFQDP-LASLNPRMTI 119
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG---IIPQAPvLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 gdiiaEPLRTYH-----PSMPRQEVKDRVKTMMMKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PLN03130 1334 -----DPFNEHNdadlwESLERAHLKDVIRRNSLG---LDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 195 DVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYNNPQHPYTRA---------- 262
Cdd:PLN03130 1406 DVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSKMvqstgaanaq 1480
|
250 260
....*....|....*....|....*
gi 1799545459 263 -LMSAVPIPDPDREKNKEIQLLEGE 286
Cdd:PLN03130 1481 yLRSLVFGGDEDRLAREESKALDGQ 1505
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-237 |
1.36e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEE-----------EWRKARSDIqmifqdPL 110
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagimlcpEDRKAEGII------PV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 111 ASLNPRMTI---------GDII-----AEPLRTYHPSMprqevkdRVKTmmmkvgllPN---LINryphEFSGGQCQRIG 173
Cdd:PRK11288 346 HSVADNINIsarrhhlraGCLInnrweAENADRFIRSL-------NIKT--------PSreqLIM----NLSGGNQQKAI 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 174 IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
49-265 |
2.23e-10 |
|
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: 60.31 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 49 GETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDPLA-------SLNPRMTIGD 121
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI---SKLPLHTLRSRLSIILQDPILfsgsirfNLDPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 122 iiaeplRTYHPSMPRQEVKDRVKTMmmkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaq 201
Cdd:cd03288 124 ------DRLWEALEIAQLKNMVKSL---PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-- 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 202 vvNLLQQ--LQREMGLSLIFIAHdlaVVKHI--SDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMS 265
Cdd:cd03288 193 --NILQKvvMTAFADRTVVTIAH---RVSTIldADLVLVLSRGILVECDTPENLLAQEDGVFASLVRT 255
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
42-251 |
2.63e-10 |
|
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: 61.89 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWlgrDLLGQSEEEWRKARSDIQMIFQDP-LASLNPRMTIg 120
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII---DGLNIAKIGLHDLRFKITIIPQDPvLFSGSLRMNL- 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 diiaEPLRTYhpsmPRQEVKDRVKTMMMK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:TIGR00957 1381 ----DPFSQY----SDEEVWWALELAHLKtfVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 195 DVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYSEV 251
Cdd:TIGR00957 1453 DLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-236 |
2.98e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 153 LPNL----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 228
Cdd:PTZ00265 1344 LPNKydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
....*...
gi 1799545459 229 HiSDRVLV 236
Cdd:PTZ00265 1424 R-SDKIVV 1430
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-220 |
3.57e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG-------RVAWLGRDLLGQ-SEEEWRKARSDIQMIFQDPLAsln 114
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITRLSFEQLQKlVSDEWQRNNTDMLSPGEDDTG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 prMTIGDIIAEplrtyhpsmprqEVKD--RVKTMMMKVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK10938 100 --RTTAEIIQD------------EVKDpaRCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*...
gi 1799545459 193 ALDVSIQAQVVNLLQQLQREmGLSLIFI 220
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
48-238 |
3.59e-10 |
|
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: 58.35 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 48 EGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWlgrdllgqseeewrkarsdiqmifqdplaslnPRMTIgdiiaepl 127
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--------------------------------DGITP-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 128 rTYHPsmprQEVKdrvktmmmkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 207
Cdd:cd03222 64 -VYKP----QYID-----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|.
gi 1799545459 208 QLQREMGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-247 |
4.39e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqsEEEWRKARSDIQMIFQDPLasLNPRM 117
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNI--LFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TigdiIAEPLRTYHPSMPR--QEVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:TIGR01257 1019 T----VAEHILFYAQLKGRswEEAQLEMEAMLEDTG-LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 196 VSIQAQVVNLLqqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:TIGR01257 1094 PYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
39-250 |
6.98e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAT--EGRVAWLGRDLLGQSEEEwrkarsdIQMIFQDPLasLNPR 116
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR-------TGFVTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 117 MTIGD-IIAEPLRTYHPSMPRQEVKDRVKTMMMKVGLLP--NLI--NRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PLN03211 155 LTVREtLVFCSLLRLPKSLTKQEKILVAESVISELGLTKceNTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 192 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSE 250
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-238 |
7.54e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 45 RLY------EGETLGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdllgQSEEEW-----RKARSDIQMIFQDpLASl 113
Cdd:PRK13409 89 KLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---------EEEPSWdevlkRFRGTELQNYFKK-LYN- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 nprmtiGDIiaeplRTYH-PSM----PRQeVKDRVKTMMMKV---GL---------LPNLINRYPHEFSGGQCQRIGIAR 176
Cdd:PRK13409 158 ------GEI-----KVVHkPQYvdliPKV-FKGKVRELLKKVderGKldevverlgLENILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799545459 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
39-229 |
9.06e-10 |
|
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: 59.76 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwlgrdllgqseeewRKARSDIQMIFQDPLASLNprmT 118
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT--------------KPAKGKLFYVPQRPYMTLG---T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRTYhpSMPRQEVKDRVKTMMMKVGLLPNLINR---------YPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR00954 531 LRDQIIYPDSSE--DMKRRGLSDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799545459 190 PVSALDVSIQAQVVNLLqqlqREMGLSLIFIAHDLAVVKH 229
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-243 |
9.17e-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: 57.66 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 35 TLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK---ATEGRVAWLGRDllgqSEEEWRKARSDIQMIFQDPLA 111
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIP----YKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 slNPRMTIGDIIAEPLRtyhpsmprqevkdrvktmmMKvGllpnliNRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:cd03233 95 --FPTLTVRETLDFALR-------------------CK-G------NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 192 SALDVSIQAQVVNLLQQLQREMGLSLIFI---AHDLAVvkHISDRVLVMYLGHAV 243
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIY--DLFDKVLVLYEGRQI 199
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
34-251 |
2.43e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGrdllgqseeewrkarsDIQMIFQDplASL 113
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIGDIIAepLRTYHPSMPRQEVKdRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK13546 97 SGQLTGIENIE--FKMLCMGFKRKEIK-AMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 194 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEV 251
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-291 |
5.18e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 32 PAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLgqseeewrkarSDIQMIFQDplA 111
Cdd:TIGR01257 1948 SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-----------TNISDVHQN--M 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 112 SLNPRM-TIGDIIA--EPLRTYHP--SMPRQEVkDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:TIGR01257 2015 GYCPQFdAIDDLLTgrEHLYLYARlrGVPAEEI-EKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYSEVYNNPQHPYTRALMSA 266
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIK 2172
|
250 260
....*....|....*....|....*
gi 1799545459 267 VPIPDPDREKNKEIQLLEGELPSPI 291
Cdd:TIGR01257 2173 SPKDDLLPDLNPVEQFFQGNFPGSV 2197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-253 |
6.39e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRdLLGQSEEEW---RKARSDIqmIFQDPLASLNPRMT 118
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSWimpGTIKDNI--IFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 IGDIIAEPLRTYHPSmprqevKDrvKTMMMKVGLlpnlinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:TIGR01271 522 IKACQLEEDIALFPE------KD--KTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 199 QAQ-----VVNLLQQLQRemglslIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYSEVYN 253
Cdd:TIGR01271 584 EKEifescLCKLMSNKTR------ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQA 636
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
41-256 |
3.81e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRKARSdiqMIFQDPL-------ASL 113
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS---MIPQDPVlfdgtvrQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 114 NPRMTIGDiiAEPLRTYHPSMPRQEVKDRVKTMMMKVglLPNLINrypheFSGGQCQRIGIARALILE-PKLIICDEPVS 192
Cdd:PTZ00243 1405 DPFLEASS--AEVWAALELVGLRERVASESEGIDSRV--LEGGSN-----YSVGQRQLMCMARALLKKgSGFILMDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799545459 193 ----ALDVSIQAQVVNLLQqlqremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYSEVYNNPQ 256
Cdd:PTZ00243 1476 nidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
39-257 |
4.14e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGlvkategrvawlgrDLLGQSEEEWRKARSDIQmIFQDPLASLNPRMT 118
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--------------DLTGGGAPRGARVTGDVT-LNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 119 igdiiaEPLRTYHPSMPRQEVKDRVKTMMmkvgllpnLINRYPH---------------------------------EFS 165
Cdd:PRK13547 82 ------ARLRAVLPQAAQPAFAFSAREIV--------LLGRYPHarragalthrdgeiawqalalagatalvgrdvtTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 166 GGQCQRIGIARAL---------ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
250 260
....*....|....*....|.
gi 1799545459 237 MYLGHAVELGTYSEVYnNPQH 257
Cdd:PRK13547 228 LADGAIVAHGAPADVL-TPAH 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-237 |
4.66e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEwrKARSDIQMIFQDplasLN- 114
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQE----LNl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 -------PRMTIGDIIAEPLRTYHPSMPRQevkdrVKTMMMKVGllpnlINRYPHE----FSGGQCQRIGIARALILEPK 183
Cdd:PRK10982 85 vlqrsvmDNMWLGRYPTKGMFVDQDKMYRD-----TKAIFDELD-----IDIDPRAkvatLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 184 LIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
53-237 |
6.82e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 53 GVVGESGCGKSTLARAIIglvkATEGRVAWlgrdllgqseEEWRKARSDIQMIFQDPLASLnprmtigdiiaeplrtyhp 132
Cdd:cd03238 25 VVTGVSGSGKSTLVNEGL----YASGKARL----------ISFLPKFSRNKLIFIDQLQFL------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 133 smprqevkdrvktmmMKVGL--LPnlINRYPHEFSGGQCQRIGIARALILEPK--LIICDEPVSALDVSIQAQVVNLLQQ 208
Cdd:cd03238 72 ---------------IDVGLgyLT--LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180
....*....|....*....|....*....
gi 1799545459 209 LqREMGLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03238 135 L-IDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-254 |
9.39e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 5 AEKKVLLEIADLKVHF---NIKDGrQWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATE---- 77
Cdd:PLN03130 597 AEERVLLPNPPLEPGLpaiSIKNG-YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasv 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 78 ---GRVAWLgrdllgqseeewrkarSDIQMIFQdplASLNPRMTIGDiiaeplrTYHPSmpRQEVKDRVKTMMMKVGLLP 154
Cdd:PLN03130 676 virGTVAYV----------------PQVSWIFN---ATVRDNILFGS-------PFDPE--RYERAIDVTALQHDLDLLP 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 155 ----NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKH 229
Cdd:PLN03130 728 ggdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQ 805
|
250 260
....*....|....*....|....*
gi 1799545459 230 IsDRVLVMYLGHAVELGTYSEVYNN 254
Cdd:PLN03130 806 V-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
38-245 |
2.53e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqSEEEWRKARSDIQMIFQDplASLNPRM 117
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLFSAVFTD--FHLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 118 TIGDIIAEPLRTYHPSMPRQEVKDRVKtmmMKVGLLPNLinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLE---LEDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1799545459 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 245
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-250 |
3.66e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLG---QSEEE--------------WRKARSDI 102
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyaQDHAYdfendltlfdwmsqWRQEGDDE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 103 QMIfqdplaslnpRMTIGDIIaeplrtyhpsMPRQEVKDRVKTMmmkvgllpnlinryphefSGGQCQRIGIARALILEP 182
Cdd:PRK15064 416 QAV----------RGTLGRLL----------FSQDDIKKSVKVL------------------SGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 183 KLIICDEPVSALDV-SIQAqvvnLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVE-LGTYSE 250
Cdd:PRK15064 458 NVLVMDEPTNHMDMeSIES----LNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-235 |
3.90e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV--------AWLGRDL--LGQSEEEW-----RKARSdiq 103
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlAWVNQETpaLPQPALEYvidgdREYRQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 104 miFQDPLASLNPRMTiGDIIAeplrTYHPSMPRQE---VKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALIL 180
Cdd:PRK10636 94 --LEAQLHDANERND-GHAIA----TIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 181 EPKLIICDEPVSALDVSiqaQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVL 235
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKII 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
42-253 |
9.56e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRD------------------LLGQSEEEWRkARSDIQ 103
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfssqfswimpgtikeniIFGVSYDEYR-YKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 104 MIFQDPlaslnprmtigDIIAEPlrtyhpsmprqevkDRVKTMMMKVGLLpnlinrypheFSGGQCQRIGIARALILEPK 183
Cdd:cd03291 135 ACQLEE-----------DITKFP--------------EKDNTVLGEGGIT----------LSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799545459 184 LIICDEPVSALDVSIQAQ-----VVNLLQQLQRemglslIFIAHDLAVVKhISDRVLVMYLGHAVELGTYSEVYN 253
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEifescVCKLMANKTR------ILVTSKMEHLK-KADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-227 |
2.23e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 8 KVLLEIADlkVHFNIKDgrqwfwqpaKTLkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwLGRDL 87
Cdd:PRK11147 317 KIVFEMEN--VNYQIDG---------KQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 88 lgqseeewrkarsDIQMiFQDPLASLNPRMTIGDIIAEplrtyhpsmPRQEV----KDR------------VKTMMMKVG 151
Cdd:PRK11147 383 -------------EVAY-FDQHRAELDPEKTVMDNLAE---------GKQEVmvngRPRhvlgylqdflfhPKRAMTPVK 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 152 LLpnlinryphefSGGQCQRIGIARaLILEP-KLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVV 227
Cdd:PRK11147 440 AL-----------SGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
42-228 |
2.89e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.25 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLlgqseeEWRKARSDIQMIFQDPLASLNPRMTIGD 121
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 122 iiaEPLRTYHPSMPRQEVkdrvkTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK13540 94 ---NCLYDIHFSPGAVGI-----TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*..
gi 1799545459 202 VVNLLQQLQREMGLSLIFIAHDLAVVK 228
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
42-237 |
3.62e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIglvkATEGRVAWL------GRDLLGQSEE---EWRKARSDIQMIFQDpLAS 112
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLAFDTI----YAEGQRRYVeslsayARQFLGQMDKpdvDSIEGLSPAIAIDQK-TTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 113 LNPRMTIGDI--IAEPLRTYHPSMPrqeVKDRVKtMMMKVGLLPNLINRYPHEFSGGQCQRIGIARAL--ILEPKLIICD 188
Cdd:cd03270 89 RNPRSTVGTVteIYDYLRLLFARVG---IRERLG-FLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799545459 189 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03270 165 EPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDI 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-254 |
4.67e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 21 NIKDGrQWFWQPAKTLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATE-------GRVAWLgrdllgqsee 93
Cdd:PLN03232 616 SIKNG-YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAYV---------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 94 ewrkarSDIQMIFQdplASLNPRMTIGDiiaeplrTYHPSMPRQEVKdrVKTMMMKVGLLPNL----INRYPHEFSGGQC 169
Cdd:PLN03232 685 ------PQVSWIFN---ATVRENILFGS-------DFESERYWRAID--VTALQHDLDLLPGRdlteIGERGVNISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGT 247
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
....*..
gi 1799545459 248 YSEVYNN 254
Cdd:PLN03232 823 FAELSKS 829
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-223 |
4.96e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrvawlgrdllgqseEEWRKARSDIQMIFQDPlaSLNPRMTI 119
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIKVGYLPQEP--QLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 120 GDIIAEPLRTYHPSMPR--------QEVKDRVKTMMMKVGLLPNLIN------------------RYP------HEFSGG 167
Cdd:TIGR03719 86 RENVEEGVAEIKDALDRfneisakyAEPDADFDKLAAEQAELQEIIDaadawdldsqleiamdalRCPpwdadvTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799545459 168 QCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHD 223
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
42-237 |
5.18e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQS------------EEEWRK----ARSDIQmi 105
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalvTEERRStgiyAYLDIG-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 FQDPLASLNPRMT-IGDIIAEPLRTyhpsmPRQEVKD--RVKTMMMK--VGLLpnlinryphefSGGQCQRIGIARALIL 180
Cdd:PRK10982 345 FNSLISNIRNYKNkVGLLDNSRMKS-----DTQWVIDsmRVKTPGHRtqIGSL-----------SGGNQQKVIIGRWLLT 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 181 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM 464
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
36-247 |
5.19e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 36 LKAVDGVSLRLYEGETLGVVGESGCG--KSTLARAIIGlvkATEGRVAW------LGRDLLGQSEEEWRKARSDIQMIFQ 107
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWrf*twcANRRALRRTIG*HRPVR*GRRESFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 dplASLNPRMtIGDIIaeplrtyhpSMPRQEVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:NF000106 103 ---GRENLYM-IGR*L---------DLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799545459 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIF---------IAHDLAVVkhisDRVLVMYLGHAVELGT 247
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTtqymeeaeqLAHELTVI----DRGRVIADGKVDELKT 233
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-108 |
1.05e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 1.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAWLGRDLLGQSEEEWRkarsdiQM---IFQD 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLfsaVFSD 414
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
52-223 |
1.23e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 52 LGVVGESGCGKSTLARAIIGLVKATEGRVawlgrdllgqseeeWRKARSDIQMIFQDPLASLnprmtigDIIAEPL---- 127
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHHVDGL-------DLSSNPLlymm 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 128 RTYhPSMPRQevkdRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaQVVNLLQ 207
Cdd:PLN03073 597 RCF-PGVPEQ----KLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQ 668
|
170
....*....|....*.
gi 1799545459 208 QLQREMGlSLIFIAHD 223
Cdd:PLN03073 669 GLVLFQG-GVLMVSHD 683
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-196 |
2.58e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGvSLRLYEGETLGVVGESGCGKSTLAR-----AIIGLVKATEgrVAWLGRDLLGQS------------------EEEW 95
Cdd:PLN03073 194 VDA-SVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNCQ--ILHVEQEVVGDDttalqcvlntdiertqllEEEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 96 R----KARSDIQMIFQDPLASLNPRMTiGDIIAEPLRTYHPsmpRQEVKD------RVKTMMMKVGLLPNLINRYPHEFS 165
Cdd:PLN03073 271 QlvaqQRELEFETETGKGKGANKDGVD-KDAVSQRLEEIYK---RLELIDaytaeaRAASILAGLSFTPEMQVKATKTFS 346
|
170 180 190
....*....|....*....|....*....|.
gi 1799545459 166 GGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-199 |
1.14e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.13 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVAWLGRDLLGQSEEEWRKARSDI-QMIFqdpLASLNPRMTIg 120
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIpQKVF---IFSGTFRKNL- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 121 diiaEPlrtyHPSMPRQEVKdRVKTmmmKVGlLPNLINRYPHE-----------FSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR01271 1313 ----DP----YEQWSDEEIW-KVAE---EVG-LKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170
....*....|.
gi 1799545459 190 PVSALD-VSIQ 199
Cdd:TIGR01271 1380 PSAHLDpVTLQ 1390
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
26-222 |
1.23e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 43.35 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 26 RQWFWQPaktlkavdgvslRLYEGETLGVVGESGCGKSTLARAIiglvkATegRVAwLGRDLLGqseeeWRKARSDIQMI 105
Cdd:COG3598 2 RRWLVPG------------LLPEGGVTLLAGPPGTGKSFLALQL-----AA--AVA-AGGPWLG-----RRVPPGKVLYL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 106 -FQDPLASLNPRMTigDIIAeplrtyHPSMPRQEVKDRVktmmmkvgLLPNLINRYPHEFSGGQcqrigIARALILE-PK 183
Cdd:COG3598 57 aAEDDRGELRRRLK--ALGA------DLGLPFADLDGRL--------RLLSLAGDLDDTDDLEA-----LERAIEEEgPD 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799545459 184 LIICDePVSAL------DVSIQAQVVNLLQQLQREMGLSLIFIAH 222
Cdd:COG3598 116 LVVID-PLARVfggdenDAEEMRAFLNPLDRLAERTGAAVLLVHH 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-196 |
2.98e-04 |
|
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: 42.61 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVAwLGRDL----LGQSeeewRKARSDIQMIFQDpLASLN 114
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVklayVDQS----RDALDPNKTVWEE-ISGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 115 PRMTIGDIIAePLRTYhpsMPRQEVK--DRVKtmmmKVGLLpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:TIGR03719 412 DIIKLGKREI-PSRAY---VGRFNFKgsDQQK----KVGQL-----------SGGERNRVHLAKTLKSGGNVLLLDEPTN 472
|
....
gi 1799545459 193 ALDV 196
Cdd:TIGR03719 473 DLDV 476
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
165-228 |
3.07e-04 |
|
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: 41.83 E-value: 3.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799545459 165 SGGQCQRIGIARALILE---PKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK 228
Cdd:cd03271 171 SGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 236
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
165-235 |
3.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 165 SGGQCQRIGIARALIL---EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKhISDRVL 235
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVK-VADYVL 882
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-190 |
3.59e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 34 KTLkAVDGVSLRLYEGETLGVVGESGCGKSTL------ARAIiglvkaTEGRVAWLGRDLlgqseeewRKARSdiqmifq 107
Cdd:NF033858 13 KTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSLlsliagARKI------QQGRVEVLGGDM--------ADARH------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 108 dpLASLNPRmtigdiIAeplrtYhpsMP---------------------------RQEVKDRVKTMMMKVGLLPNLiNRY 160
Cdd:NF033858 71 --RRAVCPR------IA-----Y---MPqglgknlyptlsvfenldffgrlfgqdAAERRRRIDELLRATGLAPFA-DRP 133
|
170 180 190
....*....|....*....|....*....|
gi 1799545459 161 PHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-222 |
5.71e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 137 QEVKDRVKTMMMK----VGLLPNLINRYPHEFSGGQcQRIG-IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQR 211
Cdd:PRK10938 371 QAVSDRQQKLAQQwldiLGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIS 449
|
90
....*....|.
gi 1799545459 212 EMGLSLIFIAH 222
Cdd:PRK10938 450 EGETQLLFVSH 460
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
165-232 |
7.41e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 7.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799545459 165 SGGQCQRIGIARALILE---PKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK---HISD 232
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIKtadYIID 903
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-243 |
8.02e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 9 VLLEIADLKVHFNIKDGRQwfwqpaktlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV--KATEGRVAWLGR- 85
Cdd:NF040905 256 VVFEVKNWTVYHPLHPERK----------VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKe 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 86 -DLLGQSE---------EEWRKAR-----SDIQmiFQDPLASLN---PRMTIGDI----IAEPLRTyhpSMprqevkdRV 143
Cdd:NF040905 326 vDVSTVSDaidaglayvTEDRKGYglnliDDIK--RNITLANLGkvsRRGVIDENeeikVAEEYRK---KM-------NI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 144 KT--MMMKVGllpNLinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIA 221
Cdd:NF040905 394 KTpsVFQKVG---NL--------SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVIS 461
|
250 260
....*....|....*....|..
gi 1799545459 222 HDLAVVKHISDRVLVMYLGHAV 243
Cdd:NF040905 462 SELPELLGMCDRIYVMNEGRIT 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-285 |
1.79e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 137 QEVKDRVKtMMMKVGLLPNLINRYPHEFSGGQCQRIGIARAL--ILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMG 214
Cdd:TIGR00630 463 KEIRERLG-FLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 215 LSLIFIAHDLAVVKHiSDRVLVM------YLGHAVELGTYSEVYNNPqHPYTRALMSA---VPIPDPDREKNKEIQLLEG 285
Cdd:TIGR00630 541 NTLIVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANP-DSLTGQYLSGrkkIEVPAERRPGNGKFLTLKG 618
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
54-128 |
4.64e-03 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 38.82 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 54 VVGESGCGKSTLARAII-GLVKATEGRVAWLG-----RDLLGQSEEEWRKA----RSDIQMIFQDPLASLNPRMTIGDII 123
Cdd:TIGR03925 368 IFGDSESGKTTLLRTIArGIVRRYSPDQARLVvvdyrRTLLGAVPEDYLAGyaatSAALTELIAALAALLERRLPGPDVT 447
|
....*
gi 1799545459 124 AEPLR 128
Cdd:TIGR03925 448 PQQLR 452
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
52-129 |
5.32e-03 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 38.07 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799545459 52 LGVVGESGCGKSTLARAIIGLvkategrvawLGRDL-----LGQSEEEWRKARSDIqmifqdPLASLNPRMTIGDIIAEP 126
Cdd:PRK07429 11 LGVAGDSGCGKTTFLRGLADL----------LGEELvtvicTDDYHSYDRKQRKEL------GITALDPRANNLDIMYEH 74
|
...
gi 1799545459 127 LRT 129
Cdd:PRK07429 75 LKA 77
|
|
| |
