|
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: 786.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 5 AEKKVLLEIADLKVHFDIRDGKQWFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG 84
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 85 RNLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEF 164
Cdd:PRK15079 83 KDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 245 LGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGSFRHA 324
Cdd:PRK15079 243 LGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHA 322
|
....*....
gi 502790984 325 VSCLKVDPL 333
Cdd:PRK15079 323 VSCLKVDPL 331
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-327 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 549.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 5 AEKKVLLEIADLKVHFDIRDGkqWFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG 84
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGG--LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 85 RNLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEF 164
Cdd:COG4608 80 QDITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLR-IHGLASKAERRERVAELLELVGLRPEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 245 LGTYDEVYTNPQHPYTKALMSAVPIPDPdlEKNKQIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLL-EGSFRH 323
Cdd:COG4608 239 IAPRDELYARPLHPYTQALLSAVPVPDP--ERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLrEVGPGH 316
|
....
gi 502790984 324 AVSC 327
Cdd:COG4608 317 QVAC 320
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-332 |
3.03e-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: 500.74 E-value: 3.03e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGKqwfwqppksLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA---TEGRVSWLGRN 86
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV---------VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 87 LLGQSEEEWRKAR-SDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGLLP--NLINRYPHE 163
Cdd:COG0444 72 LLKLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLR-IHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 164 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 244 ELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTRP-LLEGSFR 322
Cdd:COG0444 231 EEGPVEELFENPRHPYTRALLSSIPRLDPDGRRLIPI---PGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPpLREVGPG 307
|
330
....*....|
gi 502790984 323 HAVSCLKVDP 332
Cdd:COG0444 308 HRVACHLYEE 317
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-331 |
1.26e-152 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 431.31 E-value: 1.26e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADLKVHFDIRDGkqwFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL 87
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRG---LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 LGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGG 167
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLI-NTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 248 YDEVYTNPQHPYTKALMSAVPIPDPDLEKnKQIQlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGSFRHAVSC 327
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPDDRR-ERIK-LTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVAC 316
|
....
gi 502790984 328 LKVD 331
Cdd:PRK11308 317 FAVE 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-271 |
3.46e-151 |
|
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: 435.27 E-value: 3.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 5 AEKKVLLEIADLKVHFDIRDGkqWFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVSWLG 84
Cdd:COG4172 270 PDAPPLLEARDLKVWFPIKRG--LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 85 RNLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEF 164
Cdd:COG4172 347 QDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*..
gi 502790984 245 LGTYDEVYTNPQHPYTKALMSAVPIPD 271
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-273 |
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 502790984 5 AEKKVLLEIADLKVHFDIRdgkqwfwqPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG 84
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPVR--------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 85 RNLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEF 164
Cdd:COG1123 327 KDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLR-LHGLLSRAERRERVAELLERVGLPPDLADRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
250 260
....*....|....*....|....*....
gi 502790984 245 LGTYDEVYTNPQHPYTKALMSAVPIPDPD 273
Cdd:COG1123 486 DGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-246 |
7.63e-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: 349.50 E-value: 7.63e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGKQwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG 89
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSV---------KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-269 |
3.40e-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: 330.61 E-value: 3.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGKQwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlg 89
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV---------PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 qSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHpelsRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:COG1124 70 -TRRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 249
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250 260
....*....|....*....|
gi 502790984 250 EVYTNPQHPYTKALMSAVPI 269
Cdd:COG1124 225 DLLAGPKHPYTRELLAASLA 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-286 |
1.59e-104 |
|
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: 316.24 E-value: 1.59e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirdgkqwfwQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL----VKATEGRVSWLGR 85
Cdd:COG4172 6 LLSVEDLSVAFG---------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 86 NLLGQSEEEWRKAR-SDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPELSRQDVKDRVKTMMMKVGLlPN---LINRYP 161
Cdd:COG4172 77 DLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRL-HRGLSGAAARARALELLERVGI-PDperRLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502790984 242 AVELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIQLLEGE 286
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-324 |
1.32e-94 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 293.30 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 3 SLAEKKVLLEIADLKVHFDIRDGkqWFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSW 82
Cdd:PRK10261 306 TVVDGEPILQVRNLVTRFPLRSG--LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 83 LGRNLLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPELSRQDVKDRVKTMMMKVGLLPNLINRYPH 162
Cdd:PRK10261 384 NGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRV-HGLLPGKAAAARVAWLLERVGLLPEHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 243 VELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGSFR 322
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRV-LLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFM 621
|
..
gi 502790984 323 HA 324
Cdd:PRK10261 622 RR 623
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
10-266 |
1.69e-94 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 281.34 E-value: 1.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGkqWFWQppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG 89
Cdd:COG4167 4 LLEVRNLSKTFKYRTG--LFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSeeewRKARS-DIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQ 168
Cdd:COG4167 80 GD----YKYRCkHIRMIFQDPNTSLNPRLNIGQILEEPLR-LNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 169 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 248
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*...
gi 502790984 249 DEVYTNPQHPYTKALMSA 266
Cdd:COG4167 235 AEVFANPQHEVTKRLIES 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-318 |
1.11e-90 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 273.91 E-value: 1.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 1 MSSLAEKKVLLEIADLKVHFDIRDGkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRV 80
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDG---------DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 81 S----WLGRNLLGQSEEEWRKARSD-IQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQD-VKDRVKtmMMKVGLLP 154
Cdd:PRK09473 73 GgsatFNGREILNLPEKELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLM-LHKGMSKAEaFEESVR--MLDAVKMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 155 NL---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS 231
Cdd:PRK09473 150 EArkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 232 DRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIQlleGELPSPINPPSGCVFRTRCPIAGPECA 311
Cdd:PRK09473 230 DKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIP---GNPPNLLRLPKGCPFQPRCPHAMEICS 306
|
....*..
gi 502790984 312 KTRPLLE 318
Cdd:PRK09473 307 SAPPLEE 313
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-272 |
5.37e-82 |
|
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: 257.52 E-value: 5.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFdirdgkqwfwqPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAT---EGRVSWLGRN 86
Cdd:COG1123 4 LLEVRDLSVRY-----------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 87 LLGQSEEEWRKarsDIQMIFQDPLASLNPrMTIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSG 166
Cdd:COG1123 73 LLELSEALRGR---RIGMVFQDPMTQLNP-VTVGDQIAEALEN--LGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260
....*....|....*....|....*.
gi 502790984 247 TYDEVYTNPQhpytkaLMSAVPIPDP 272
Cdd:COG1123 226 PPEEILAAPQ------ALAAVPRLGA 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-327 |
3.84e-79 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 244.27 E-value: 3.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirDGKQWFwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV----KATEGRVSWLGR 85
Cdd:PRK11022 3 LLNVDKLSVHFG--DESAPF-------RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 86 NLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyHPELSRQDVKDRVKTMMMKVGLlPNLINR---YP 161
Cdd:PRK11022 74 DLQRISEKERRNlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKV-HQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 242 AVELGTYDEVYTNPQHPYTKALMSAVPipdPDLEKNKQIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPLLEGSF 321
Cdd:PRK11022 232 VVETGKAHDIFRAPRHPYTQALLRALP---EFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA 308
|
....*.
gi 502790984 322 RHAVSC 327
Cdd:PRK11022 309 GRQSKC 314
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-327 |
6.78e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 241.35 E-value: 6.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGKqwfwqppksLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK----ATEGRVSWLGR 85
Cdd:COG4170 3 LLDIRNLTIEIDTPQGR---------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 86 NLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGDIIAE--PLRTYHPEL--SRQDVKDRVKTMMMKVGLLPN--LIN 158
Cdd:COG4170 74 DLLKLSPRERRKiIGREIAMIFQEPSSCLDPSAKIGDQLIEaiPSWTFKGKWwqRFKWRKKRAIELLHRVGIKDHkdIMN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 159 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:COG4170 154 SYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 239 LGHAVELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTrPLLE 318
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PRLR 312
|
....*....
gi 502790984 319 GSFRHAVSC 327
Cdd:COG4170 313 KIKGHEFAC 321
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-265 |
2.82e-75 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 240.76 E-value: 2.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGKQWFWQPPKSlkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVSWLGRNLLG 89
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKRTVDHNV--VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEWRKARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC 169
Cdd:PRK15134 352 LNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 249
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE 511
|
250
....*....|....*.
gi 502790984 250 EVYTNPQHPYTKALMS 265
Cdd:PRK15134 512 RVFAAPQQEYTRQLLA 527
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
35-279 |
2.26e-73 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 227.65 E-value: 2.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPLASLN 114
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRtyH-PELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK10419 104 PRKTVREIIREPLR--HlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 194 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNpQHPYTKALMSAVPIPDPD 273
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGRVLQNAVLPAFPV 260
|
....*.
gi 502790984 274 LEKNKQ 279
Cdd:PRK10419 261 RRRTTE 266
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
39-272 |
1.41e-72 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 225.45 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPLASLNPRMT 118
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRTYHpELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:TIGR02769 107 VRQIIGEPLRHLT-SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNpQHPYTKALMSAVPIPDP 272
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVLPEHP 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
29-286 |
1.32e-70 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 223.03 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQD 108
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 plASLNPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:COG1135 91 --FNLLSSRTVAENVALPLE--IAGVPKAEIRKRVAELLELVG-LSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVP 268
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVL 245
|
250
....*....|....*...
gi 502790984 269 IPDPDLEKNKQIQLLEGE 286
Cdd:COG1135 246 NDELPEELLARLREAAGG 263
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-267 |
7.81e-70 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 218.14 E-value: 7.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 1 MSSLAEKkvLLEIADLKVHFDIRDGKQWfwqppkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV 80
Cdd:COG4107 1 MTNEEQP--LLSVRGLSKRYGPGCGTVV---------ACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 81 SWLGR-----NLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGDIIAEPL-----RTYhpelsrQDVKDRVKTMMMK 149
Cdd:COG4107 70 YYRDRdggprDLFALSEAERRRlRRTDWGMVYQNPRDGLRMDVSAGGNIAERLmaageRHY------GDIRARALEWLER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 150 VGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 229
Cdd:COG4107 144 VEIPLERIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRL 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 502790984 230 ISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAV 267
Cdd:COG4107 224 LADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-266 |
2.99e-69 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 216.96 E-value: 2.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADLKVHFDIRDGkqWFWQppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL 87
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTG--WFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 lGQSEEEWRKARsdIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGG 167
Cdd:PRK15112 78 -HFGDYSYRSQR--IRMIFQDPSTSLNPRQRISQILDFPLR-LNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*....
gi 502790984 248 YDEVYTNPQHPYTKALMSA 266
Cdd:PRK15112 234 TADVLASPLHELTKRLIAG 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-268 |
3.01e-67 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 222.04 E-value: 3.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVS----WLGR------NLLGQSEEEWRKA 98
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmLLRRrsrqviELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 99 R-SDIQMIFQDPLASLNPRMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGL--LPNLINRYPHEFSGGQCQRIGIA 175
Cdd:PRK10261 102 RgADMAMIFQEPMTSLNPVFTVGEQIAESIR-LHQGASREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 176 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
250
....*....|...
gi 502790984 256 QHPYTKALMSAVP 268
Cdd:PRK10261 261 QHPYTRALLAAVP 273
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-262 |
4.98e-66 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 207.91 E-value: 4.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 9 VLLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLL 88
Cdd:COG1127 4 PMIEVRNLTKSFG-------------DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 89 GQSEEEWRKARSDIQMIFQDP--LASlnprMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGlLPNLINRYPHEFSG 166
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGalFDS----LTVFENVAFPLR-EHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|....*.
gi 502790984 247 TYDEVYTNPqHPYTKA 262
Cdd:COG1127 225 TPEELLASD-DPWVRQ 239
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-256 |
1.16e-65 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 206.66 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQ- 107
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 -DPLASLnprmTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:cd03258 91 fNLLSSR----TVFENVALPLEIAG--VPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 187 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-273 |
1.81e-63 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 209.95 E-value: 1.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFdiRDGKQwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL-----VKATEGRVSWLG 84
Cdd:PRK15134 5 LLAIENLSVAF--RQQQT-------VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 85 RNLLGQSEEEWRKARSD-IQMIFQDPLASLNPRMTIGDIIAEPLrTYHPELSRQDVKDRVKTMMMKVGL--LPNLINRYP 161
Cdd:PRK15134 76 ESLLHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVL-SLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|..
gi 502790984 242 AVELGTYDEVYTNPQHPYTKALMSAVPIPDPD 273
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
29-276 |
6.63e-63 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 203.11 E-value: 6.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQ- 107
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 -DPLASlnprMTIGDIIAEPLrtyhpEL---SRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:PRK11153 91 fNLLSS----RTVFDNVALPL-----ELagtPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 184 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKAL 263
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250
....*....|....*.
gi 502790984 264 MSAV---PIPDPDLEK 276
Cdd:PRK11153 241 IQSTlhlDLPEDYLAR 256
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
40-261 |
3.15e-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: 3.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDplASLNPRMTI 119
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS--GALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 199
Cdd:cd03261 95 FENVAFPLR-EHTRLSEEEIREIVLEKLEAVG-LRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 200 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNpQHPYTK 261
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVR 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-327 |
3.03e-60 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 196.18 E-value: 3.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDGkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK----ATEGRVSWLGR 85
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG---------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 86 NLLGQSEEEWRK-ARSDIQMIFQDPLASLNPRMTIGD--IIAEPLRTYHPELsRQDV---KDRVKTMMMKVGLL--PNLI 157
Cdd:PRK15093 74 DLLRLSPRERRKlVGHNVSMIFQEPQSCLDPSERVGRqlMQNIPGWTYKGRW-WQRFgwrKRRAIELLHRVGIKdhKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 158 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 238 YLGHAVELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNKQIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTrPLL 317
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRL 311
|
330
....*....|
gi 502790984 318 EGSFRHAVSC 327
Cdd:PRK15093 312 TGAKNHLYAC 321
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
36-267 |
1.75e-59 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 191.68 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGR-----NLLGQSEEEWRK-ARSDIQMIFQDP 109
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRlLRTEWGFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 LASLNPRMTIGDIIAEPL-----RTYhpelsrQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:PRK11701 99 RDGLRMQVSAGGNIGERLmavgaRHY------GDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 185 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALM 264
Cdd:PRK11701 173 VFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLV 252
|
...
gi 502790984 265 SAV 267
Cdd:PRK11701 253 SSV 255
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-259 |
3.41e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 193.78 E-value: 3.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 7 KKVLLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRN 86
Cdd:COG3842 2 AMPALELENVSKRYG-------------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 87 LLGQSEEEwrkaRsDIQMIFQDPlaSLNPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSG 166
Cdd:COG3842 69 VTGLPPEK----R-NVGMVFQDY--ALFPHLTVAENVAFGLR--MRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD----LAvvkhISDRVLVMYLGHA 242
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRI 214
|
250
....*....|....*..
gi 502790984 243 VELGTYDEVYTNPQHPY 259
Cdd:COG3842 215 EQVGTPEEIYERPATRF 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-267 |
2.59e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 180.19 E-value: 2.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRNLLG 89
Cdd:COG1126 1 MIEIENLHKSFG-------------DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-TVDGEDLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEWRKARSDIQMIFQdplaSLN--PRMTIGDIIAEPLRTYHpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGG 167
Cdd:COG1126 67 DSKKDINKLRRKVGMVFQ----QFNlfPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGLA-DKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250 260
....*....|....*....|
gi 502790984 248 YDEVYTNPQHPYTKALMSAV 267
Cdd:COG1126 220 PEEFFENPQHERTRAFLSKV 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
33-256 |
3.39e-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: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPLAS 112
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 L-NPrmTIGDIIAeplrtYHPE---LSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:COG1122 88 LfAP--TVEEDVA-----FGPEnlgLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-244 |
3.26e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 177.16 E-value: 3.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADLKVHFdiRDGKQwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL 87
Cdd:COG1136 2 SPLLELRNLTKSY--GTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 LGQSEEEWRKARSD-IQMIFQDPlaSLNPRMTIGDIIAEPLRtYHpELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSG 166
Cdd:COG1136 73 SSLSERELARLRRRhIGFVFQFF--NLLPELTALENVALPLL-LA-GVSRKERRERARELLERVGL-GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 244
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
34-241 |
4.90e-54 |
|
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: 176.14 E-value: 4.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSD-IQMIFQDPlaS 112
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSF--N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03255 93 LLPDLTALENVELPLL--LAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGH 241
Cdd:cd03255 170 NLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-246 |
1.15e-53 |
|
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: 175.02 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:cd03259 1 LELKGLSKTYG-------------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEewrkaRSDIQMIFQDPlaSLNPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQ 170
Cdd:cd03259 68 PPE-----RRNIGMVFQDY--ALFPHLTVAENIAFGLK--LRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-237 |
6.82e-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: 173.43 E-value: 6.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDIRDGKqwfwqppksLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:cd03293 1 LEVRNVSKTYGGGGGA---------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SeeewrkarSDIQMIFQDPlaSLNPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQ 170
Cdd:cd03293 72 G--------PDRGYVFQQD--ALLPWLTVLDNVALGLE--LQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVM 237
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--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 |
1.22e-52 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 172.27 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 28 WFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKarsDIQMIFQ 107
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR---KVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 DPLASL-NPrmTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:cd03225 83 NPDDQFfGP--TVEEEVAFGLENLG--LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-237 |
4.49e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.58 E-value: 4.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 1 MSSlaeKKVLLEIADLKVHFDIRDGkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV 80
Cdd:COG1116 1 MSA---AAPALELRGVSKRFPTGGG---------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 81 SWLGRNLLGqseeewrkARSDIQMIFQDPlaSLNPRMTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLPnLINRY 160
Cdd:COG1116 69 LVDGKPVTG--------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGLAG-FEDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 161 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQaqvvNLLQQLQREMGLSLIFIAHDL--AVVkhISDRV 234
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVdeAVF--LADRV 209
|
...
gi 502790984 235 LVM 237
Cdd:COG1116 210 VVL 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
37-241 |
6.20e-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: 169.68 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLRRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLrtyhpelsrqdvkdrvktmmmkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03229 91 LTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502790984 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 |
1.65e-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: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRN-----LLGQSEEEWRK-ARSDIQMIFQDPL 110
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRlMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 ASLNPRMTIGDIIAEPL-----RTYhpelsrQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLmaigaRHY------GNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMS 265
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVS 250
|
..
gi 502790984 266 AV 267
Cdd:TIGR02323 251 SI 252
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
37-243 |
8.44e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 169.08 E-value: 8.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:COG3638 17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIFQQF--NLVPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MT---------IGDIiaEPLRTYHPELSRQDvKDRVKTMMMKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:COG3638 95 LSvltnvlagrLGRT--STWRSLLGLFPPED-RERALEALERVGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG3638 171 DEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-260 |
1.23e-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: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGq 90
Cdd:COG1118 3 IEVRNISKRFG-------------SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 seeeWRKAR-SDIQMIFQDPLasLNPRMTIGDIIAEPLRTYHPelSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQC 169
Cdd:COG1118 69 ----NLPPReRRVGFVFQHYA--LFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQL-EGLADRYPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 249
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
250
....*....|.
gi 502790984 250 EVYTNPQHPYT 260
Cdd:COG1118 220 EVYDRPATPFV 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
38-256 |
2.02e-50 |
|
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: 167.41 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSeeewrKARSDIQMIFQDplASLNPRM 117
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PHKRPVNTVFQN--YALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:cd03300 88 TVFENIAFGLRL--KKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-268 |
1.87e-48 |
|
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: 163.58 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARS-DIQMIFQDplASLNPR 116
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03294 117 RTVLENVAFGLEVQG--VPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVP 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 ... |
35-259 |
4.79e-48 |
|
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: 161.74 E-value: 4.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwrkarSDIQMIFQDplASLN 114
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFVFQH--YALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRTYH--PELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03296 87 RHMTVFDNVAFGLRVKPrsERPPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPY 259
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
37-259 |
1.81e-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: 160.16 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkaRSdIQMIFQDplASLNPR 116
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--RK-IGYVIQQ--IGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAeplrtYHPEL---SRQDVKDRVKTMMMKVGLLP-NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03295 90 MTVEENIA-----LVPKLlkwPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPY 259
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-190 |
3.02e-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: 153.96 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKarsDIQMIFQDPlaSLNPRMT 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK---EIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 119 IGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:pfam00005 76 VRENLRLGLLLKG--LSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
34-251 |
6.84e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEewrkARSDIQMIFQDPlaSL 113
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRRIGYVPQEP--AL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPRMTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:COG1131 85 YPDLTVRENLRFFARLYG--LPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 194 LDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:COG1131 162 LDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
37-257 |
1.21e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 158.70 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwRkarsDIQMIFQDPlaSLNPR 116
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R----NIAMVFQSY--ALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:COG3839 90 MTVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHD------LAvvkhisDRVLVMYLGHAVELGTYDEVYTNPQH 257
Cdd:COG3839 167 KLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-241 |
1.37e-45 |
|
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: 154.22 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFdirdgkqwfwqppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQ 90
Cdd:cd03262 1 IEIKNLHKSF-------------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEEWRKARSDIQMIFQDplASLNPRMTIGDIIAEPLRTYHpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQ 170
Cdd:cd03262 67 DKKNINELRQKVGMVFQQ--FNLFPHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
33-244 |
3.51e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 153.67 E-value: 3.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDplAS 112
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:COG2884 90 LLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502790984 193 ALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:COG2884 167 NLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
39-253 |
6.05e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 154.05 E-value: 6.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDPLASLNprMT 118
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA---YVPQEPPAPFG--LT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIA---EPLRTYHPELSRQDvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:COG1120 92 VRELVAlgrYPHLGLFGRPSAED-REAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:COG1120 170 LAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-255 |
1.80e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 156.26 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 1 MSSLAEKKVLLEIADLKVHFDirdGKQwfwqppkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFD---GKE----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 81 SWLGRNLLGQSEEewrkaRSDIQMIFQDplASLNPRMTIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLlPNLINRY 160
Cdd:PRK09452 72 MLDGQDITHVPAE-----NRHVNTVFQS--YALFPHMTVFENVAFGLRM--QKTPAAEITPRVMEALRMVQL-EEFAQRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 161 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 240
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
250
....*....|....*
gi 502790984 241 HAVELGTYDEVYTNP 255
Cdd:PRK09452 222 RIEQDGTPREIYEEP 236
|
|
| 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 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHPEL-------SRQDvKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:cd03256 93 LSVLENVLSGRLGRRSTWrslfglfPKEE-KQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
38-253 |
1.42e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseeewRKARSDI----QMifqdplASL 113
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRARRRIgyvpQR------AEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPR--MTIGDIIAEPLRTYHPELSR--QDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:COG1121 87 DWDfpITVRDVVLMGRYGRRGLFRRpsRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMyLGHAVELGTYDEVYT 253
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-241 |
2.30e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.43 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVhfdiRDGKQWFWQPpkslkavdgVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:COG4619 1 LELEGLSF----RVGGKPILSP---------VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEEWRKarsDIQMIFQDPLAslnPRMTIGDIIAEPLRTYHPELSRQDVKDrvktMMMKVGLLPNLINRYPHEFSGGQCQ 170
Cdd:COG4619 68 PPPEWRR---QVAYVPQEPAL---WGGTVRDNLPFPFQLRERKFDRERALE----LLERLGLPPDILDKPVERLSGGERQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:COG4619 138 RLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-251 |
2.74e-43 |
|
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: 148.87 E-value: 2.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 20 FDIRDGKQWFwqppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA-----TEGRVSWLGRNLLGQSEE- 93
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 94 EWRKARsdIQMIFQDPlaslNP-RMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKVGLLPNLINR-YPHEFSGGQCQR 171
Cdd:cd03260 77 LELRRR--VGMVFQKP----NPfPGSIYDNVAYGLR-LHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 172 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
33-256 |
5.46e-43 |
|
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: 149.52 E-value: 5.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPLAS 112
Cdd:TIGR04521 15 PFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNpRMTIGDIIAeplrtYHPE---LSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR04521 95 LF-EETVYKDIA-----FGPKnlgLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
37-246 |
7.55e-43 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 147.40 E-value: 7.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseEEWRKARSDIQMIFQDplASLNPR 116
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKDRDIAMVFQN--YALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03301 87 MTVYDNIAFGLKLRK--VPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03301 164 KLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
33-255 |
1.31e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 149.47 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkaRS---DIQMIfqdp 109
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR--RRigyVIQQI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 laSLNPRMTIGDIIAeplrTYhPEL---SRQDVKDRVKTMMMKVGLLPN-LINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:COG1125 86 --GLFPHMTVAENIA----TV-PRLlgwDKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-256 |
4.12e-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: 146.72 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 9 VLLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLL 88
Cdd:COG0411 3 PLLEVRGLTKRFG-------------GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 89 GQSEEE-WRK--ARSdiqmiFQdpLASLNPRMTIGD-------------IIAEPLRTYHPELSRQDVKDRVKTMMMKVGL 152
Cdd:COG0411 70 GLPPHRiARLgiART-----FQ--NPRLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 153 LPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 232
Cdd:COG0411 143 AD-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLAD 221
|
250 260
....*....|....*....|....
gi 502790984 233 RVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:COG0411 222 RIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-253 |
2.06e-41 |
|
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: 144.36 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirDGKQwfwqppkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG 89
Cdd:TIGR02315 1 MLEVENLSKVYP--NGKQ----------ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEWRKARSDIQMIFQDplASLNPRMTIGDIIAEPLRTYHPEL-------SRQDvKDRVKTMMMKVGLLpNLINRYPH 162
Cdd:TIGR02315 69 LRGKKLRKLRRRIGMIFQH--YNLIERLTVLENVLHGRLGYKPTWrsllgrfSEED-KERALSALERVGLA-DKAYQRAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:TIGR02315 145 QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
250
....*....|.
gi 502790984 243 VELGTYDEVYT 253
Cdd:TIGR02315 225 VFDGAPSELDD 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
39-266 |
3.46e-41 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.07 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL----VKATEGRVSWLGRNLLGQSeeewRKARSdIQMIFQDPLASLN 114
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCA----LRGRK-IATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRTyhpeLSRQDVKDRVKTMMMKVGL--LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK10418 94 PLHTMHTHARETCLA----LGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSA 266
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-251 |
1.28e-40 |
|
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: 142.30 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFdirdgkqwfwqppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNllg 89
Cdd:COG4555 1 MIEVENLSKKY-------------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 qSEEEWRKARSDIQMIFQDPlaSLNPRMTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQC 169
Cdd:COG4555 65 -VRKEPREARRQIGVLPDER--GLYDRLTVRENIRYFAELYG--LFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 249
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
..
gi 502790984 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 |
2.79e-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: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:cd03219 1 LEVRGLTKRFG-------------GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEewRKARSDIQMIFQDPlaSLNPRMTIGD--IIAEPLRTYHPEL------SRQDVKDRVKTMMMKVGLLPnLINRYPH 162
Cdd:cd03219 68 PPH--EIARLGIGRTFQIP--RLFPELTVLEnvMVAAQARTGSGLLlararrEEREARERAEELLERVGLAD-LADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
250
....*....|....
gi 502790984 243 VELGTYDEVYTNPQ 256
Cdd:cd03219 222 IAEGTPDEVRNNPR 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-251 |
3.17e-40 |
|
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: 149.60 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDPla 111
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ---IGVVLQDV-- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 slnprMTIGDIIAEPLRTYHPELSRQDVKDRVKtmmmKVGLLPnLINRYPH-----------EFSGGQCQRIGIARALIL 180
Cdd:COG2274 559 -----FLFSGTIRENITLGDPDATDEEIIEAAR----LAGLHD-FIEALPMgydtvvgeggsNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 181 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 251
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
39-256 |
3.34e-40 |
|
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: 140.93 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEewrkaRSDIQMIFQDplASLNPRMT 118
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQN--YALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:cd03299 88 VYKNIAYGLK--KRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
35-267 |
8.14e-40 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 139.93 E-value: 8.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRkaRSDIQMIFQDplASLN 114
Cdd:TIGR00968 12 SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDA---TRVHAR--DRKIGFVFQH--YALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRTYHPelSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKH--PKAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAV 267
Cdd:TIGR00968 162 DAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-241 |
3.00e-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: 136.37 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFdirdgkqwfwqppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgq 90
Cdd:cd03230 1 IEVRNLSKRY-------------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 sEEEWRKARSDIQMIFQDPlaSLNPRMTIGDIIaeplrtyhpelsrqdvkdrvktmmmkvgllpnlinryphEFSGGQCQ 170
Cdd:cd03230 65 -KKEPEEVKRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
38-250 |
5.83e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 144.90 E-value: 5.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDP-LaslnPR 116
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ---IAWVPQNPyL----FA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTigdiIAEPLRTYHPELSRQDVKDRVKtmmmKVGLLpNLINRYPHEF-----------SGGQCQRIGIARALILEPKLI 185
Cdd:COG4988 425 GT----IRENLRLGRPDASDEELEAALE----AAGLD-EFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
38-237 |
7.23e-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: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseeewRKARSDIQMIFQDPLASLNPRM 117
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTY---HPELSRQDvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:cd03235 86 SVRDVVLMGLYGHkglFRRLSKAD-KAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502790984 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 |
1.05e-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: 135.20 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDP-L 110
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN---IAYVPQDPfL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 ASlnprMTIGDiiaeplrtyhpelsrqdvkdrvktmmmkvgllpNLinrypheFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:cd03228 88 FS----GTIRE---------------------------------NI-------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502790984 191 VSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03228 124 TSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVL 167
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
37-241 |
3.58e-38 |
|
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: 133.14 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQdplaslnpr 116
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 mtigdiiaeplrtyhpelsrqdvkdrvktmmmkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502790984 197 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-262 |
3.30e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.62 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 1 MSSLAEK-KVLLEIADLKVHFDirdGKQwfwqppkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAI------IGLV 73
Cdd:COG1117 1 MTAPASTlEPKIEVRNLNVYYG---DKQ----------ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 74 KaTEGRVSWLGRNLLGQSE--EEWRKarsDIQMIFQDPlaslNP-RMTIGDIIAEPLRtYHPELSRQDVKDRVKTMMMKV 150
Cdd:COG1117 68 R-VEGEILLDGEDIYDPDVdvVELRR---RVGMVFQKP----NPfPKSIYDNVAYGLR-LHGIKSKSELDEIVEESLRKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 151 GL-------LpnliNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHD 223
Cdd:COG1117 139 ALwdevkdrL----KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 502790984 224 LAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKA 262
Cdd:COG1117 213 MQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-269 |
6.47e-37 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 134.93 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 54 VVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEewrkaRSDIQMIFQDplASLNPRMTIGDIIAEPLRTyhPE 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQS--YALFPHMTVEENVAFGLKM--RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 134 LSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREM 213
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 214 GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVPI 269
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
40-258 |
6.73e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.52 E-value: 6.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwRKARSDIQMIFQDplASLNPRMTI 119
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQEAGMVFQQ--FYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDIIA-EPLRTYhpELSRQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK09493 95 LENVMfGPLRVR--GASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 199 QAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHP 258
Cdd:PRK09493 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
41-265 |
1.00e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.79 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLL------GQ----SEEEWRKARSDIQMIFQDpl 110
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdGQlkvaDKNQLRLLRTRLTMVFQH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 ASLNPRMTIGDIIAE-PLRTYHpeLSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK10619 101 FNLWSHMTVLENVMEaPIQVLG--LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMS 265
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
42-256 |
1.37e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 131.67 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL-LGQ--SEEEWRKARSDIQMIFQDplASLNPRMT 118
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKtpSDKAIRELRRNVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 -IGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK11124 99 vQQNLIEAPCRVL--GLSKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 198 IQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEvYTNPQ 256
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
39-246 |
1.77e-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: 129.48 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqmifqdplaslnprmt 118
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 igdiiaeplrtYhpelsrqdvkdrVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:cd03214 77 -----------Y------------VPQALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-267 |
2.42e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 134.58 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnLLG 89
Cdd:PRK11607 19 LLEIRNLTKSFD-------------GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM-----LDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEWRKARSDIQMIFQDplASLNPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQC 169
Cdd:PRK11607 81 VDLSHVPPYQRPINMMFQS--YALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSI----QAQVVNLLQQLqremGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 245
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|..
gi 502790984 246 GTYDEVYTNPQHPYTKALMSAV 267
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGSV 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-266 |
3.82e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 130.26 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwRKarsdIQMIFQDplASLNPRMTIGDI 122
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP----VSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 123 IAEPLrtyHP--ELSRQDvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:COG3840 92 IGLGL---RPglKLTAEQ-RAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 201 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSA 266
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
27-244 |
3.92e-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: 130.25 E-value: 3.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 27 QWFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSD-IQMI 105
Cdd:COG4181 16 KTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARhVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 106 FQdplaS--LNPRMTIGDIIAEPLrtyhpEL-SRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEP 182
Cdd:COG4181 96 FQ----SfqLLPTLTALENVMLPL-----ELaGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 183 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 244
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
39-272 |
7.90e-36 |
|
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: 132.81 E-value: 7.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA--TEGRVSWLGRNLLGQSEEewrkaRSDIQMIFQDplASLNPR 116
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPH-----KRGLALLFQN--YALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:TIGR03258 94 LKVEDNVAFGLRAQ--KMPKADIAERVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 197 SIQAQVVNLLQQLQREM-GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVPIPDP 272
Cdd:TIGR03258 171 NIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-237 |
8.84e-36 |
|
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: 129.09 E-value: 8.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDI--RDGKQwfwqppksLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLgrnl 87
Cdd:COG4778 4 LLEVENLSKTFTLhlQGGKR--------LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 lgqseeewrkaRSDIQMIfqDpLASLNPRM-------TIG---------------DIIAEPLRtyHPELSRQDVKDRVKT 145
Cdd:COG4778 71 -----------RHDGGWV--D-LAQASPREilalrrrTIGyvsqflrviprvsalDVVAEPLL--ERGVDREEARARARE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 146 MMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLA 225
Cdd:COG4778 135 LLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEE 213
|
250
....*....|..
gi 502790984 226 VVKHISDRVLVM 237
Cdd:COG4778 214 VREAVADRVVDV 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
39-290 |
1.16e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 132.15 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwrkarSDIQMIFQDplASLNPRMT 118
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDICMVFQS--YALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK11432 95 LGENVGYGLKML--GVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVPIPDPDLEKNk 278
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPATLSGD- 250
|
250
....*....|..
gi 502790984 279 QIQLLEGELPSP 290
Cdd:PRK11432 251 YVDIYGYRLPRP 262
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-252 |
4.28e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.98 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQdplaslNPR- 116
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRRQVGMVFQ------NPDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 ----MTIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK13635 93 qfvgATVQDDVAFGLENI--GVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY 252
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
29-256 |
6.35e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 6.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQD 108
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 P----LASlnprmTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:PRK13632 92 PdnqfIGA-----TVEDDIAFGLE--NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 185 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL-AVVKhiSDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
241-329 |
7.20e-35 |
|
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: 122.47 E-value: 7.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 241 HAVELGTYDEVYTNPQHPYTKALMSAVPIP-DPDLEKNKqiqlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRP-LLE 318
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRDRKLIS----IPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPaLVE 76
|
90
....*....|.
gi 502790984 319 GSFRHAVSCLK 329
Cdd:TIGR01727 77 IAEGHRVACHL 87
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
35-256 |
1.24e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.67 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL---LGQSEEEWRKARSDIQMIFQDplA 111
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGD-IIAEPLRTYhpELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:COG4161 92 NLWPHLTVMEnLIEAPCKVL--GLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 191 VSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYdEVYTNPQ 256
Cdd:COG4161 169 TAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-259 |
1.90e-34 |
|
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: 132.20 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDP-- 109
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQRPhl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 -LASlnprmtigdiIAEPLRtyhpeLSRQDVKD-RVKTMMMKVGLLPnLINRYPH-----------EFSGGQCQRIGIAR 176
Cdd:COG4987 421 fDTT----------LRENLR-----LARPDATDeELWAALERVGLGD-WLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNG 561
|
...
gi 502790984 257 HPY 259
Cdd:COG4987 562 RYR 564
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-237 |
2.74e-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: 124.71 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 48 EGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEE-----EWRKarsdIQMIFQDplASLNPRMTIGDI 122
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppQQRK----IGLVFQQ--YALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 123 IAEPLRtyhpELSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 202
Cdd:cd03297 96 LAFGLK----RKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 502790984 203 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
37-243 |
3.72e-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: 122.92 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARsdIQMIFQdplaslnpr 116
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--IAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 mtigdiiaeplrtyhpelsrqdvkdrvktmmmkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502790984 197 SIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
33-254 |
1.08e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEeWRKARSDIQMIFQDPLAS 112
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGL-LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK13637 96 LFEETIEKDIAFGPINL---GLSEEEIENRVKRAMNIVGLdYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 192 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTN 254
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
42-255 |
1.48e-33 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 126.75 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKA-RSDIQMIFQDplASLNPRMTIg 120
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQE--ARLFPHLSV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 diiAEPLRtY----HPELSRQDVKDRVKTMMmkvGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:COG4148 95 ---RGNLL-YgrkrAPRAERRISFDEVVELL---GIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
33-237 |
1.51e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.75 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseEEWRKARSdIQMIFQDPLAS 112
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKS-IGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LnprmtIGDIIAEPLRTYHPELSrqDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03226 84 L-----FTDSVREELLLGLKELD--AGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502790984 193 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
33-250 |
2.76e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.13 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDP-LA 111
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ---IGVVPQDTfLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SlnprMTIGDIIAeplrtY-HPELSRQDVKDRVKtmmmKVGLLpNLINRYPH-----------EFSGGQCQRIGIARALI 179
Cdd:COG1132 427 S----GTIRENIR-----YgRPDATDEEVEEAAK----AAQAH-EFIEALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 180 LEPKLIICDEPVSALDVSIQAQVvnlLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:COG1132 493 KDPPILILDEATSALDTETEALI---QEALERLMkGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
37-255 |
2.96e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.97 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkarsdIQMIFQDplASLNPR 116
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-----VGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTY--HPELSRQDVKDRVkTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK10851 89 MTVFDNIAFGLTVLprRERPNAAAIKAKV-TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-269 |
5.97e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 125.92 E-value: 5.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKAR-SDIQMIFQDplASLNPR 116
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK10070 121 MTVLDNTAFGMEL--AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAVPI 269
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
42-259 |
6.15e-33 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 124.84 E-value: 6.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEE-----EWRKarsdIQMIFQDplASLNPR 116
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppEKRR----IGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHPElSRQDVKDRVKTMMmkvGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPS-ERRISFERVIELL---GIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPY 259
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
41-265 |
6.83e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.17 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV-----SWLGRNLLGQSEEEWRKARSDIQMIFQDplASLNP 115
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQLRQHVGFVFQN--FNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 116 -RMTIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK11264 99 hRTVLENIIEGPVIV--KGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 195 DVSIQAQVVNLLQQLQREMgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMS 265
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
41-266 |
1.06e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 121.83 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG------RNLLGQSEEEWRKA----RSDIQMIFQdpl 110
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkPDRDGELVPADRRQlqriRTRLGMVFQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 aSLN--PRMTI-GDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:COG4598 103 -SFNlwSHMTVlENVIEAPVHVLG--RPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSA 266
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
38-255 |
1.06e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 124.19 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRNLLGQSEEEWRkarsDIQMIFQDplASLNPRM 117
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRVVNELEPADR----DIAMVFQN--YALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK11650 92 SVRENMAYGLKIR--GMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHD------LAvvkhisDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:PRK11650 169 LRVQMRLEIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
38-251 |
1.33e-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: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwrKARSDIQMIFQDPlaSLNPRM 117
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE--RARAGIGYVPEGR--RIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TigdiIAEPLRTYHPELSRQDVKDRVKTMmmkVGLLPNLINRYPH---EFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:cd03224 91 T----VEENLLLGAYARRRAKRKARLERV---YELFPRLKERRKQlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 195 DVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:cd03224 164 APKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-261 |
1.64e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.49 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK-----ATEGRVSWLGRNLLGQSEEEWRkARSDIQMIFQDPlaSL 113
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYP--NP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 191 VSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTK 261
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
36-251 |
4.97e-32 |
|
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: 125.30 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV------SWLGRNLLGQSEEEwrKARSDIQMIFQDp 109
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKPGPDGRG--RAKRYIGILHQE- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 lASLNPRMTIGDIIAEPLRTYHP-ELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:TIGR03269 374 -YDLYPHRTVLDNLTEAIGLELPdELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
33-237 |
7.66e-32 |
|
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: 118.66 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPLas 112
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFR-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIAEPLR-TYHPelsRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:cd03292 89 LLPDRNVYENVAFALEvTGVP---PREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502790984 192 SALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-256 |
3.76e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.78 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ-SEEEWRKARSDIQMIFQDPLA 111
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK13641 97 QLFENTVLKDVEFGPKNF---GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 192 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
33-256 |
1.03e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.10 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQSEEEWRKARSDIQMIFQDPLAS 112
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK13639 91 LFAPTVEEDVAFGPLNL---GLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 193 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-256 |
1.18e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.43 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwLGRNLL--GQSEEEWRKARSDIQMIFQDPLASLN 114
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVItaGKKNKKLKPLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK13634 100 EETVEKDICFGPMNF---GVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-261 |
1.71e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 116.30 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVK------ATEGRVSWLGRNLLgqsEEEWRKARSDIQMIFQDPlaSLNP 115
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIF---QIDAIKLRKEVGMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 116 RMTIGDIIAEPLRTyHPELSRQDVKDRVKTMMMKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK14246 104 HLSIYDNIAYPLKS-HGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTK 261
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-282 |
2.06e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEW-RKARSDIQMIFQDPLA 111
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGDIIAEPlRTYHPELsrQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK13646 97 QLFEDTVEREIIFGP-KNFKMNL--DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 192 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPqhpyTKALMSAVPIPD 271
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK----KKLADWHIGLPE 249
|
250
....*....|....*.
gi 502790984 272 -----PDLEKNKQIQL 282
Cdd:PRK13646 250 ivqlqYDFEQKYQTKL 265
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-261 |
3.07e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.52 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAI------IGLVKaTEGRVSWLGRNLLgQSEEEWRKARSDIQMIFQDPl 110
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVR-VEGRVEFFNQNIY-ERRVNLNRLRRQVSMVHPKP- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 aSLNPrMTIGDIIAEPLRT--YHPELsrqDVKDRVKTMMMKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:PRK14258 98 -NLFP-MSVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLwdeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY-----LGHAVELGTYDEVYTNPQHPYT 260
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSRT 252
|
.
gi 502790984 261 K 261
Cdd:PRK14258 253 R 253
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
33-252 |
3.51e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQSEEEWRKARSDIQMIFQDPLAS 112
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIAEPLRTYHPElsrQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK13636 95 LFSASVYQDVSFGAVNLKLPE---DEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 252
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-261 |
3.70e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.01 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK-----ATEGRVSWLGR 85
Cdd:PRK14247 4 IEIRDLKVSFG-------------QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 86 NLLGQSEEEWRKArsdIQMIFQDPlaSLNPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINRY---PH 162
Cdd:PRK14247 71 DIFKMDVIELRRR---VQMVFQIP--NPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHA 242
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*....
gi 502790984 243 VELGTYDEVYTNPQHPYTK 261
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTE 242
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
38-250 |
4.27e-30 |
|
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: 114.00 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLgqseEEWRKARSDIQMIFQDPlaSLNPRM 117
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDL--SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:cd03265 89 TGWENLYIHARLYG--VPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 250
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-251 |
7.59e-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: 113.71 E-value: 7.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRnllgqseeEWRKARSDIQMIFQDplASLNPRMT 118
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK--------QITEPGPDRMVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-254 |
1.07e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.41 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGrnlLGQSEEE--WrKARSDIQMIFQdpla 111
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG---LDTSDEEnlW-DIRNKAGMVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 slNPRMTIGDIIAEPLRTYHPE---LSRQDVKDRVKTMMMKVGLLPnlINRY-PHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:PRK13633 93 --NPDNQIVATIVEEDVAFGPEnlgIPPEEIRERVDESLKKVGMYE--YRRHaPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAVVkhiSDRVLVMYLGHAVELGTYDEVYTN 254
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHymEEAVE---ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
39-225 |
1.36e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.19 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKA---TEGRVsWL-GRNLLGQSEEEWRkarsdIQMIFQDPLasLN 114
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV-LLnGRRLTALPAEQRR-----IGILFQDDL--LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRtyhPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:COG4136 89 PHLSVGENLAFALP---PTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLA 225
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
39-284 |
1.68e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.06 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPLASLnPRMT 118
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVFQNPDNQF-VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK13650 99 VEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEVYTNPQH--------PYTKALMSAV--- 267
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFTTSLVQSLrqn 254
|
250 260
....*....|....*....|
gi 502790984 268 --PIPDPDL-EKNKQIQLLE 284
Cdd:PRK13650 255 gyDLPEGYLtEKELEEQLWE 274
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-251 |
1.81e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.44 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseeewrkARSDIQMIfqd-plaSL 113
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----------DPEDRRRIgylpeerGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPRMTIGDIIaeplrTYHPEL---SRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:COG4152 83 YPKMKVGEQL-----VYLARLkglSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 191 VSALD-VSiqaqvVNLLQQL---QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:COG4152 157 FSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
40-223 |
1.90e-29 |
|
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: 111.80 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQSEEEWRKarsdiQMIFQDPLASLNPRMTI 119
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRR-----RLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 gdiiAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 199
Cdd:COG4133 93 ----RENLRFWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 502790984 200 AQVVNLLQQLQREmGLSLIFIAHD 223
Cdd:COG4133 168 ALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-247 |
2.06e-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: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLkvHFDIrDGKQwfwqppkSLKavdGVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRVSWLGRNLL 88
Cdd:COG0396 1 LEIKNL--HVSV-EGKE-------ILK---GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 89 GQSEEEwrKARSDIQMIFQDPLASlnPRMTIGDIiaepLRT-----YHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHE 163
Cdd:COG0396 68 ELSPDE--RARAGIFLAFQYPVEI--PGVSVSNF----LRTalnarRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 164 -FSGGQCQRIGIARALILEPKLIICDEPVSALDV---SIQAQVVNLLqqlqREMGLSLIFIAHDLAVVKHIS-DRVLVMY 238
Cdd:COG0396 140 gFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYIKpDFVHVLV 215
|
....*....
gi 502790984 239 LGHAVELGT 247
Cdd:COG0396 216 DGRIVKSGG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-237 |
6.26e-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: 6.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARsdIQMIFQDPlaSLNPR 116
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG--IAIIHQEL--NLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIA---EPLRtyHPELSRQDVKDRVKTMMMKVGL-LPnlinryPH----EFSGGQCQRIGIARALILEPKLIICD 188
Cdd:COG1129 94 LSVAENIFlgrEPRR--GGLIDWRAMRRRARELLARLGLdID------PDtpvgDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502790984 189 EPVSALDvsiQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:COG1129 166 EPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
33-251 |
7.24e-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: 111.42 E-value: 7.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQSEEEWrkARSDIQMIFQ----- 107
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAW--LRRQVGVVLQenvlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 -----DPLASLNPRMTIGDII-AEPLRTYH------PELSRQDVKDRvktmmmKVGLlpnlinryphefSGGQCQRIGIA 175
Cdd:cd03252 89 nrsirDNIALADPGMSMERVIeAAKLAGAHdfiselPEGYDTIVGEQ------GAGL------------SGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 176 RALILEPKLIICDEPVSALDVSIQAqvvNLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 251
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEH---AIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
10-237 |
7.52e-29 |
|
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: 110.94 E-value: 7.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDIRDgkqwfwQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV------SWL 83
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQ------QGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRIlvrhegAWV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 84 grNLLGQSEEEWRKAR-SDIQMIFQdpLASLNPRMTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLPNLINRYPH 162
Cdd:TIGR02324 75 --DLAQASPREVLEVRrKTIGYVSQ--FLRVIPRVSALEVVAEPLLERG--VPREAARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-250 |
9.14e-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: 110.29 E-value: 9.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLgqseEEWRKARSDIQMIFQDplA 111
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQSLGYCPQF--D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTigdiIAEPLRTYHP--ELSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:cd03263 85 ALFDELT----VREHLRFYARlkGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 250
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-241 |
9.32e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.73 E-value: 9.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDPLASLNpr 116
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK10908 94 RTVYDNVAIPLII--AGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502790984 197 SIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10908 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-237 |
1.95e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.72 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDIRDGKQwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQ---------PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEewrkaRSdiqMIFQDplASLNPRMTIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQ 170
Cdd:COG4525 75 GAD-----RG---VVFQK--DALLPWLNVLDNVAFGLRL--RGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVVkhISDRVLVM 237
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVM 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
33-283 |
3.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.87 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkategrVSWLGRNLLGQSE--------EEWRKARSDIQM 104
Cdd:PRK13645 21 PFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIVGDYAipanlkkiKEVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 105 IFQDPLASLNPRMTIGDIIAEPLrtyHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:PRK13645 95 VFQFPEYQLFQETIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 185 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQhpytkaLM 264
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE------LL 245
|
250 260
....*....|....*....|....*
gi 502790984 265 SAVPIPDPDLE------KNKQIQLL 283
Cdd:PRK13645 246 TKIEIDPPKLYqlmyklKNKGIDLL 270
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
39-253 |
7.07e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.09 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDplASLNPRMT 118
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA---VLPQH--SSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIA---EPLRtyhpeLSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALI------LEPKLIICDE 189
Cdd:PRK13548 93 VEEVVAmgrAPHG-----LSRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
36-241 |
8.90e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.00 E-value: 8.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDgvsLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRNLLGQseeewrkARSDIQMIFQDplASLNP 115
Cdd:PRK11247 28 LNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAE-------AREDTRLMFQD--ARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 116 RMTIGDIIAEPLRTyhpelsrqDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK11247 95 WKKVIDNVGLGLKG--------QWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502790984 196 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-256 |
8.98e-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: 108.15 E-value: 8.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG 89
Cdd:COG0410 3 MLEVENLHAGYG-------------GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEewRKARSDI------QMIFqdplaslnPRMTIgdiiAEPLRT-YHPELSRQDVKDRVKTMMmkvGLLPNLinrypH 162
Cdd:COG0410 70 LPPH--RIARLGIgyvpegRRIF--------PSLTV----EENLLLgAYARRDRAEVRADLERVY---ELFPRL-----K 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 163 EF--------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRV 234
Cdd:COG0410 128 ERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRA 206
|
250 260
....*....|....*....|..
gi 502790984 235 LVMYLGHAVELGTYDEVYTNPQ 256
Cdd:COG0410 207 YVLERGRIVLEGTAAELLADPE 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-287 |
1.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 30 WQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgQSEEEWrKARSDIQMIFQDP 109
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL--TAENVW-NLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 LASLnPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK13642 91 DNQF-VGATVEDDVAFGME--NQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYTNPQH--------PYTK 261
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDmveigldvPFSS 245
|
250 260 270
....*....|....*....|....*....|.
gi 502790984 262 ALM-----SAVPIPDPDLEKNKQIQLLEGEL 287
Cdd:PRK13642 246 NLMkdlrkNGFDLPEKYLSEDELVELLADKL 276
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-250 |
2.80e-27 |
|
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: 106.85 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTlaraIIGLVK----ATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDP-LA 111
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDI---RDLNLRWLRSQIGLVSQEPvLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SlnprMTIGDIIAeplrtyhpeLSRQDVKDrvkTMMMKVGLLPNL---INRYPHEF-----------SGGQCQRIGIARA 177
Cdd:cd03249 90 D----GTIAENIR---------YGKPDATD---EEVEEAAKKANIhdfIMSLPDGYdtlvgergsqlSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-237 |
3.39e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARsdIQMIFQDPlaSLN 114
Cdd:COG3845 17 GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG--IGMVHQHF--MLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGD-II--AEPLRtyHPELSRQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:COG3845 93 PNLTVAEnIVlgLEPTK--GGRLDRKAARARIRELSERYGLDVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502790984 192 SALDvsiQAQVVNLLQQLQR--EMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:COG3845 170 AVLT---PQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-241 |
4.46e-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: 104.82 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADLKVHfdirdgkqwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL 87
Cdd:cd03215 2 EPVLEVRGLSVK-----------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 LGQSEEEWRKARsdiqmifqdplaslnprmtigdiIAeplrtYHPElsrqdvkDRvktmmMKVGLLP------NLINryP 161
Cdd:cd03215 65 TRRSPRDAIRAG-----------------------IA-----YVPE-------DR-----KREGLVLdlsvaeNIAL--S 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 162 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:cd03215 103 SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-255 |
4.87e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 106.61 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG 89
Cdd:PRK11300 5 LLSVSGLMMRFG-------------GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEwrKARSDIQMIFQDplASLNPRMTI-------------GDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPnL 156
Cdd:PRK11300 72 LPGHQ--IARMGVVRTFQH--VRLFREMTVienllvaqhqqlkTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLE-H 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 157 INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK11300 147 ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYV 226
|
250
....*....|....*....
gi 502790984 237 MYLGHAVELGTYDEVYTNP 255
Cdd:PRK11300 227 VNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
39-237 |
8.61e-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: 103.84 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgqseeewrkaRSDiqmifqdplaslnprmt 118
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV------------------RLD----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 igdiiAEPLRTYHPELSRQdvkdRVKTMMMKVGLLPNLINRypHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:cd03246 63 -----GADISQWDPNELGD----HVGYLPQDDELFSGSIAE--NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 502790984 199 QAQVVNLLQQLqREMGLSLIFIAHDLAVVKhISDRVLVM 237
Cdd:cd03246 132 ERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVL 168
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-252 |
1.13e-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: 105.39 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 28 WFWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQ 107
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 DPLaslnprmTIGDIIAEPLRTYHPELSRQDVKDRVKTmmmkvGLLPNLINRYPHEF-----------SGGQCQRIGIAR 176
Cdd:cd03251 84 DVF-------LFNDTVAENIAYGRPGATREEVEEAARA-----ANAHEFIMELPEGYdtvigergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY 252
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
37-237 |
1.34e-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: 109.68 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKarsdiqmifQDPLASLNPR 116
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---------QIAWVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDiIAEPLRTYHPELSRQDVKDRVktmmMKVGL----------LPNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:TIGR02857 407 LFAGT-IAENIRLARPDASDAEIREAL----ERAGLdefvaalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502790984 187 CDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVkHISDRVLVM 237
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-251 |
1.45e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.84 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAV-DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRV--------SW----LGRNL--LGQsee 93
Cdd:COG4618 337 TVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQWdreeLGRHIgyLPQ--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 94 ewrkarsDIQmIFQDplaslnprmTIGDIIAeplRtyHPELSRQDVKD-----RVKTMMMKvglLPN----LINRYPHEF 164
Cdd:COG4618 414 -------DVE-LFDG---------TIAENIA---R--FGDADPEKVVAaaklaGVHEMILR---LPDgydtRIGEGGARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 244
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQA 546
|
....*..
gi 502790984 245 LGTYDEV 251
Cdd:COG4618 547 FGPRDEV 553
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
38-252 |
2.27e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVswLGRNLLgQSEEEWRKARSDIQMIFQDPlaslnPRM 117
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI--FYNNQA-ITDDNFEKLRKHIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDII----AEPLRTYhpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK13648 96 FVGSIVkydvAFGLENH--AVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 194 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY 252
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
38-251 |
6.49e-26 |
|
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: 102.99 E-value: 6.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwrKARSDI------QMIFqdpla 111
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIayvpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 slnPRMTIgdiiAEPLRT---YHPELSRQdVKDRVKTMMmkvGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:TIGR03410 88 ---PRLTV----EENLLTglaALPRRSRK-IPDEIYELF---PVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-260 |
6.73e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.70 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 6 EKKVLLEIADLKVHFdirdGKQwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAI------IGLVKATeGR 79
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKK---------KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlNPEVTIT-GS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 80 VSWLGRNLLGQSEE--EWRKarsDIQMIFQDPlaslNP-RMTIGDIIAEPLRTyhpelsrQDVKDR------VKTMMMKV 150
Cdd:PRK14239 67 IVYNGHNIYSPRTDtvDLRK---EIGMVFQQP----NPfPMSIYENVVYGLRL-------KGIKDKqvldeaVEKSLKGA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 151 GLLPNLINRYpHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAV 226
Cdd:PRK14239 133 SIWDEVKDRL-HDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQ 209
|
250 260 270
....*....|....*....|....*....|....
gi 502790984 227 VKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYT 260
Cdd:PRK14239 210 ASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-251 |
6.84e-26 |
|
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: 103.07 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDPLaslnprm 117
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---IGVVLQDTF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTYHPELSRQDVKDRVKT-----MMMKvglLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03254 88 LFSGTIMENIRLGRPNATDEEVIEAAKEagahdFIMK---LPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 251
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
37-246 |
7.17e-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: 102.36 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG-------RNLLGQSEEE---WRKARSDIQMIF 106
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaaRNRIGYLPEErglYPKMKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 107 qdpLASLNprmtigdiiaeplrtyhpELSRQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:cd03269 94 ---LAQLK------------------GLKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-241 |
7.68e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.12 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGrnllGQSEEEWRKARSDIQMIFQDplASLNPRMTIGDI 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLN----GQDHTTTPPSRRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 123 IAEPLrtyHPELS-RQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK10771 92 IGLGL---NPGLKlNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502790984 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-246 |
8.76e-26 |
|
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: 102.45 E-value: 8.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEewrkARSDIQMIFQD 108
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE----ARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 plASLNPRMTIGDIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03266 87 --TGLYDRLTARENLEYFAGLYG--LKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-256 |
9.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 9.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV---KATEGRVSWLGRNLlgQSEEEWrKARSDIQMI 105
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITL--TAKTVW-DIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 106 FQDPLASLnPRMTIGDIIAEPLRtyHPELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:PRK13640 90 FQNPDNQF-VGATVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
35-255 |
1.02e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPLASLN 114
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK13652 93 SPTVEQDIAFGPINL---GLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
34-246 |
1.14e-25 |
|
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: 101.89 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGeTLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEeewrKARSDIQMIFQDPlaSL 113
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLRRRIGYLPQEF--GV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPRMTIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:cd03264 84 YPNFTVREFLDYIAWLK--GIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502790984 194 LDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-292 |
1.80e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.16 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 7 KKVLLEIADLKVHFDirdGKQwfwqpPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRN 86
Cdd:PRK13631 18 DDIILRVKNLYCVFD---EKQ-----ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 87 LLGQSEEEWR--------------KARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGL 152
Cdd:PRK13631 89 YIGDKKNNHElitnpyskkiknfkELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAL---GVKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 153 LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISD 232
Cdd:PRK13631 166 DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVAD 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 233 RVLVMYLGHAVELGTYDEVYTNpQHPYTKALMSAVPI---------PDPDLEK--NKQIQLLEgELPSPIN 292
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEIFTD-QHIINSTSIQVPRViqvindlikKDPKYKKlyQKQPRTIE-QLADAIN 313
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-256 |
1.98e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLkvHFDIRDGKqwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQ 90
Cdd:PRK13647 5 IEVEDL--HFRYKDGT----------KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEEWrkARSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQ 170
Cdd:PRK13647 72 ENEKW--VRSKVGLVFQDPDDQVFSSTVWDDVAFGPVNM---GLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTyDE 250
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KS 223
|
....*.
gi 502790984 251 VYTNPQ 256
Cdd:PRK13647 224 LLTDED 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-243 |
3.74e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEeeWRKARsDIQMIFQDPLASLNPR 116
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE--YKRAK-YIGRVFQDPMMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTigdiIAEPL---------RTYHPELSRQD---VKDRVKTMMM--------KVGLLpnlinryphefSGGQCQRIGIAR 176
Cdd:COG1101 97 MT----IEENLalayrrgkrRGLRRGLTKKRrelFRELLATLGLglenrldtKVGLL-----------SGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVMYLGHAV 243
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
42-241 |
4.30e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.05 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARS-DIQMIFQdpLASLNPRMTIG 120
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 DIIAEPLRTYHpeLSRQDVKDRVKTMMMKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:PRK11629 106 ENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502790984 201 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISdRVLVMYLGH 241
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-246 |
5.54e-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: 100.26 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnLLGQSEEEWRKARSDIQMIFQDP--LASLNPRMTIG 120
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL-----INGVDVTAAPPADRPVSMLFQENnlFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 DIIAEPLRtyhpeLSRQDvKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:cd03298 93 LGLSPGLK-----LTAED-RQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502790984 201 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-224 |
7.74e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.93 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwrkarsdiQMIFQDplASLNPRM 117
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTyhPELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK11248 86 NVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*..
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHDL 224
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-237 |
8.96e-25 |
|
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: 99.59 E-value: 8.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQD 108
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI---RQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 P-LASlnprMTIGDIIAeplrtyhpeLSRQDVKDRVKTMMMKVGLLPNLINRYPHEF-----------SGGQCQRIGIAR 176
Cdd:cd03245 87 VtLFY----GTLRDNIT---------LGAPLADDERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 177 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVM 237
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVM 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-257 |
1.08e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.99 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSDIQMIFQDplASLNPRMTI 119
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDIIAEPLRTyHPELSRQDVKdrvKTMMMK---VGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK11831 102 FDNVAYPLRE-HTQLPAPLLH---STVMMKleaVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQH 257
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-251 |
3.59e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 103.28 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlGQSEEEWrkARSDIQMIFQ----- 107
Cdd:TIGR01846 467 PDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL-AIADPAW--LRRQMGVVLQenvlf 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 -----DPLASLNPRMTIGDII-AEPLRTYHPELSRQdvKDRVKTMMMKVGLLpnlinrypheFSGGQCQRIGIARALILE 181
Cdd:TIGR01846 544 srsirDNIALCNPGAPFEHVIhAAKLAGAHDFISEL--PQGYNTEVGEKGAN----------LSGGQRQRIAIARALVGN 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-250 |
5.31e-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: 102.49 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPla 111
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL---ADYTLASLRRQVALVSQDV-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 slnprMTIGDIIAEPLRTYHP-ELSRQDVKDRVKTMMMKvgllpNLINRYPHEF-----------SGGQCQRIGIARALI 179
Cdd:TIGR02203 416 -----VLFNDTIANNIAYGRTeQADRAEIERALAAAYAQ-----DFVDKLPLGLdtpigengvllSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 180 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-250 |
6.14e-24 |
|
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: 98.07 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 18 VHFDIRDGKQwfwqppkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRK 97
Cdd:cd03253 6 VTFAYDPGRP----------VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 98 ArsdIQMIFQD-PLaslnprmtIGDIIAEPLRTYHPELSRQDVKDRVKtmmmkVGLLPNLINRYPHEF-----------S 165
Cdd:cd03253 76 A---IGVVPQDtVL--------FNDTIGYNIRYGRPDATDEEVIEAAK-----AAQIHDKIMRFPDGYdtivgerglklS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 166 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 245
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
....*
gi 502790984 246 GTYDE 250
Cdd:cd03253 217 GTHEE 221
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
36-250 |
6.88e-24 |
|
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: 102.09 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkarSDIQMIFQDPLASLNP 115
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELR---ARMALVPQDPVLFAAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 116 RMtigdiiaEPLRTYHPELSRQDVKDRVKTMMMK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR02204 430 VM-------ENIRYGRPDATDEEVEAAARAAHAHefISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 190 PVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:TIGR02204 503 ATSALD----AESEQLVQQaLETLMkGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAE 560
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-252 |
1.44e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.27 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 28 WFWQP--PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwLGRNLLGQS--EEEWRKARSDIQ 103
Cdd:PRK13643 9 YTYQPnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTskQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 104 MIFQDPLASLNPRMTIGDIIAEPlrtYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPK 183
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 184 LIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 252
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| 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 502790984 243 VELGTYDEVYTNPQHPYTKALMSAVPIPDPdleKNKQIQLLEGELPSPINPPSGCVFRTRCPIAGPEC 310
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP---PKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
37-251 |
1.69e-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: 101.35 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDPLaslnpr 116
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQEPY------ 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHPELSRQDV---------KDRVKTMMMKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:TIGR01193 559 IFSGSILENLLLGAKENVSQDEIwaaceiaeiKDDIENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
41-223 |
1.78e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARS-DIQMIFQDPLasLNPRMTI 119
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkHVGFVFQSFM--LIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDIIAEP--LRTyhpELSRQDvKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK10584 106 LENVELPalLRG---ESSRQS-RNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHD 223
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-246 |
1.87e-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: 95.67 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVhfdIRDGKqwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRVSWLGRNLL 88
Cdd:cd03217 1 LEIKDLHV---SVGGK----------EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 89 GQSEEEwrKARSDIQMIFQDPlaslnprmtigdiiaeplrtyhPELSRqdvkdrVKTMMmkvgLLpnlinRYPHE-FSGG 167
Cdd:cd03217 68 DLPPEE--RARLGIFLAFQYP----------------------PEIPG------VKNAD----FL-----RYVNEgFSGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHI-SDRVLVMYLGHAVELG 246
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
42-256 |
2.26e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGrnllGQSEEEWRKARSDIQMIFQDplASLNPRMTIGD 121
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIG----EKRMNDVPPAERGVGMVFQS--YALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 122 IIAEPLRTyhPELSRQDVKDRVKTMMmKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK11000 95 NMSFGLKL--AGAKKEEINQRVNQVA-EVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK11000 172 MRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-255 |
2.68e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVswLGRNLLGQSEEEWRKARSDIQMIFQDPLAS 112
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV--LVSGIDTGDFSKLQGIRKLVGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LnprmtIGDIIAEPLrTYHPE---LSRQDVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK13644 90 F-----VGRTVEEDL-AFGPEnlcLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVkHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-250 |
3.11e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.42 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLaraiIGLVK----ATEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQD 108
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQrvfdPQSGRILIDGTDIRTVTRASLRRN---IAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 PLasLNPRMtigdiIAEPLRTYHPELSRQDVKDRVKT------MMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEP 182
Cdd:PRK13657 418 AG--LFNRS-----IEDNIRVGRPDATDEEMRAAAERaqahdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 183 KLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-243 |
4.91e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADLKVHfdirdgkqwfwqPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL 87
Cdd:COG3845 255 EVVLEVENLSVR------------DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 LGQSEEEWRKARsdIQMIFQDPLAS-LNPRMTIGDIIAepLRTYHPE-------LSRQDVKDRVKTMM--MKVgllpnli 157
Cdd:COG3845 323 TGLSPRERRRLG--VAYIPEDRLGRgLVPDMSVAENLI--LGRYRRPpfsrggfLDRKAIRAFAEELIeeFDV------- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 158 nRYPHE------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHIS 231
Cdd:COG3845 392 -RTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALS 469
|
250
....*....|..
gi 502790984 232 DRVLVMYLGHAV 243
Cdd:COG3845 470 DRIAVMYEGRIV 481
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
37-241 |
4.94e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.24 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV---KATEGRVSWLGRNLL--GQSEEEWRKARSDIQMIFQDplA 111
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQreGRLARDIRKSRANTGYIFQQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMT------IGDIIAEPL-RTYHPELSRQDvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:PRK09984 96 NLVNRLSvlenvlIGALGSTPFwRTCFSWFTREQ-KQRALQALTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 185 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
32-251 |
8.94e-23 |
|
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: 99.17 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNL--LGQSEeewrkARSDIQMIFQDP 109
Cdd:TIGR03375 474 PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqIDPAD-----LRRNIGYVPQDP 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 ---LASLNPRMTIGDiiaeplrtyhPELSRQDVKDRVKtmmmKVGLLpNLINRYPHEF-----------SGGQCQRIGIA 175
Cdd:TIGR03375 549 rlfYGTLRDNIALGA----------PYADDEEILRAAE----LAGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALA 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 176 RALILEPKLIICDEPVSALDVSIQAQvvnLLQQLQREM-GLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEER---FKDRLKRWLaGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQV 686
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
54-259 |
1.17e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 54 VVGESGCGKSTLARAIIGLVKATEGRVSwLGRNLLGQSEE------EWRKarsdIQMIFQDplASLNPRMTI-GDIiaep 126
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIV-LNGRVLFDAEKgiclppEKRR----IGYVFQD--ARLFPHYKVrGNL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 127 lrTYHPELSRQDVKDRVktmmmkVGLL--PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN 204
Cdd:PRK11144 98 --RYGMAKSMVAQFDKI------VALLgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 205 LLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ-HPY 259
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-246 |
6.92e-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: 91.85 E-value: 6.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSeeewrKARSDIQMIFQDplASLNPRMTIGDI 122
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 123 IAEPLrtyHPELSRQDV-KDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:TIGR01277 91 IGLGL---HPGLKLNAEqQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502790984 202 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-249 |
7.69e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.61 E-value: 7.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ---SEEEW------------RK 97
Cdd:PRK13651 17 PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktKEKEKvleklviqktrfKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 98 A------RSDIQMIFQDPLASLNPRMTIGDIIAEPLRTyhpELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQR 171
Cdd:PRK13651 97 IkkikeiRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSM---GVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 172 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG-TYD 249
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGdTYD 251
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-251 |
9.04e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDIRDG-----KQWFWQPPKSLK----AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG--- 78
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslKELLLRRRRTRReefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrve 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 79 ---RVSWL------------GR-N------LLGQSEEEWRKARSDIqmI-FQDplaslnprmtIGDIIAEPLRTYhpels 135
Cdd:COG1134 85 vngRVSALlelgagfhpeltGReNiylngrLLGLSRKEIDEKFDEI--VeFAE----------LGDFIDQPVKTY----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 136 rqdvkdrvktmmmkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGL 215
Cdd:COG1134 148 -----------------------------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GR 197
|
250 260 270
....*....|....*....|....*....|....*.
gi 502790984 216 SLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:COG1134 198 TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
39-237 |
9.40e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 9.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnllgqseeewRKARSDIQMIFQDPlaslnpRMT 118
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RPAGARVLFLPQRP------YLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDiiaepLR---TYhPELSRQDVKDRVKTMMMKVGLlPNLINRY------PHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:COG4178 439 LGT-----LRealLY-PATAEAFSDAELREALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 190 PVSALDVSIQAQvvnLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:COG4178 512 ATSALDEENEAA---LYQLLREELpGTTVISVGHRSTLAAF-HDRVLEL 556
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
41-255 |
1.67e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPLASlnpRMTIG 120
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEPVLF---SGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 DIIAEPLRTYHPELSRQDVKDR-VKTMMMKvglLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMAAAKAAnAHDFIME---FPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 196 VSIQAqvvnLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:TIGR00958 650 AECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-265 |
1.77e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 1 MSSLAEKKVLLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARA------IIGLVK 74
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYG-------------SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 75 AtEGRVSWLGRNLLGqSEEEWRKARSDIQMIFQDPlaslNP-RMTIGDIIAEPLRT--YHPELS-------RQDVK-DRV 143
Cdd:PRK14243 68 V-EGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP----NPfPKSIYDNIAYGARIngYKGDMDelverslRQAALwDEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 144 KTMMMKVGLlpnlinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHD 223
Cdd:PRK14243 142 KDKLKQSGL----------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHN 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502790984 224 LAVVKHISDRVLVM---------YLGHAVELGTYDEVYTNPQHPYTKALMS 265
Cdd:PRK14243 210 MQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-252 |
1.88e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 28 WF-WQPPKSLKavdGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNlLGQSEEEWRKARSDIQMIF 106
Cdd:PRK13638 8 WFrYQDEPVLK---GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-LDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 107 QDPlaslNPRMTIGDI---IAEPLRTYHpeLSRQDVKDRVKTMMMKVGllpnlINRYPHE----FSGGQCQRIGIARALI 179
Cdd:PRK13638 84 QDP----EQQIFYTDIdsdIAFSLRNLG--VPEAEITRRVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 180 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 252
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
34-255 |
3.05e-21 |
|
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: 90.29 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRNLLGQsEEEWRKARSDIQMIFQDplASL 113
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGQDITK-LPMHKRARLGIGYLPQE--ASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPRMTIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:cd03218 87 FRKLTVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 194 LD-VSIQaQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:cd03218 164 VDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
38-247 |
3.86e-21 |
|
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: 89.86 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPL---ASLn 114
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHDLRSRISIIPQDPVlfsGTI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 pRMTIgdiiaEPLRTYHPE-----LSRQDVKDRVKTMmmkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:cd03244 95 -RSNL-----DPFGEYSDEelwqaLERVGLKEFVESL---PGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 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 |
3.93e-21 |
|
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: 90.47 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDIRDGKQWFWQPPKSL--------KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSW 82
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKSLfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 83 LGRN--------------LLGQSEEEWRkarsDIQmifqdPLASLNPRMTIGDIIAEPLRTYHPELSRqdvkdrvktmMM 148
Cdd:cd03267 81 AGLVpwkrrkkflrrigvVFGQKTQLWW----DLP-----VIDSFYLLAAIYDLPPARFKKRLDELSE----------LL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 149 KVGLLPNLINRyphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 228
Cdd:cd03267 142 DLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIE 218
|
250
....*....|...
gi 502790984 229 HISDRVLVMYLGH 241
Cdd:cd03267 219 ALARRVLVIDKGR 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
37-237 |
4.20e-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: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnLLGQSEEEWRKARSDIQMIFQDPlaSLNPR 116
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGKSYQKNIEALRRIGALIEAP--GFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIgdiiAEPLRTYHPELSRQdvKDRVKTMMMKVGLlpnliNRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03268 87 LTA----RENLRLLARLLGIR--KKRIDEVLDVVGL-----KDSAKKkvkgFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502790984 193 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGII 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-252 |
7.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSE-EEWRKARSDIQMIFQDPLASLNP 115
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 116 RMTIGDIiaeplrTYHPE---LSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:PRK13649 101 ETVLKDV------AFGPQnfgVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 193 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 252
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
33-247 |
1.02e-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: 88.62 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPLas 112
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 lnprmtigdIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLpNLinryphefSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03369 93 ---------LFSGTIRSNLDPFDEYSDEEIYGALRVSEGGL-NL--------SQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 193 ALDVSIQAqvvnLLQQLQREM--GLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGT 247
Cdd:cd03369 155 SIDYATDA----LIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
35-243 |
1.26e-20 |
|
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: 92.20 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK--ATEGRVSWLGRNLLGQSEEEwrKARSDIQMIFQDplAS 112
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRD--TERAGIVIIHQE--LT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTI------GDIIAEP-LRTYHPELSRqdvkdRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:TIGR02633 89 LVPELSVaeniflGNEITLPgGRMAYNAMYL-----RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
39-253 |
1.46e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWrkARSdIQMIFQDPLAslnPR-M 117
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--ARR-LALLPQHHLT---PEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIA---EPLRTYHPELSRQDvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK11231 92 TVRELVAygrSPWLSLWGRLSAED-NARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 195 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:PRK11231 170 DINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-260 |
1.90e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrVSWLGRNLLG-QSEEEWRKA---RSDIQMIFQDPlaslN 114
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGgRSIFNYRDVlefRRRVGMLFQRP----N 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 P-RMTIGDIIAEPLRTyHPELSRQDVKDRVKTMMMKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK14271 112 PfPMSIMDNVLAGVRA-HKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 191 VSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYT 260
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-251 |
2.11e-20 |
|
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: 91.64 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG-------RNLLGQSeeewrkarsdIQM 104
Cdd:TIGR01842 327 PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdRETFGKH----------IGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 105 IFQDplASLNPRmTIGDIIAEplrtyhpelSRQDVKDRVKTMMMKVGLLPNLINRYPHEF-----------SGGQCQRIG 173
Cdd:TIGR01842 397 LPQD--VELFPG-TVAENIAR---------FGENADPEKIIEAAKLAGVHELILRLPDGYdtvigpggatlSGGQRQRIA 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 174 IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
35-243 |
2.93e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 35 SLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrvswlgrnllgqseeEWRKARSDIQMIFQDPLASLN 114
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG---------------TYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 pRMTIGDIiaepLRTYH--PELS---------------RQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARA 177
Cdd:PRK10535 85 -REHFGFI----FQRYHllSHLTaaqnvevpavyagleRKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAV 243
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-253 |
2.97e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.22 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVhfdIRDGKqwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG-RVSWLGRNLL 88
Cdd:COG1119 3 LLELRNVTV---RRGGK----------TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 89 GQSEEEWRK----ARSDIQMIFQdplaslnPRMTIGDIIAeplrT-------YHPELSRQDvKDRVKTMMMKVGLLPnLI 157
Cdd:COG1119 70 GEDVWELRKriglVSPALQLRFP-------RDETVLDVVL----SgffdsigLYREPTDEQ-RERARELLELLGLAH-LA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 158 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHdlavvkHISD----- 232
Cdd:COG1119 137 DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVEEippgi 210
|
250 260
....*....|....*....|..
gi 502790984 233 -RVLVMYLGHAVELGTYDEVYT 253
Cdd:COG1119 211 tHVLLLKDGRVVAAGPKEEVLT 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-255 |
3.99e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFdirdgkqwfwqppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:PRK09536 4 IDVSDLSVEF-------------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEeewRKARSDIQMIFQDPLASLNPRmtiGDIIAEPLRTYH-PELSRQDVKDR--VKTMMMKVGlLPNLINRYPHEFSGG 167
Cdd:PRK09536 71 SA---RAASRRVASVPQDTSLSFEFD---VRQVVEMGRTPHrSRFDTWTETDRaaVERAMERTG-VAQFADRPVTSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 168 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
....*...
gi 502790984 248 YDEVYTNP 255
Cdd:PRK09536 223 PADVLTAD 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-236 |
5.13e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.37 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK--ATEGRVSWLGRNLLGQS--EEEwrkaRSDIQMIFQDpLAs 112
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNirDTE----RAGIAIIHQE-LA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDII---AEPlrTYHPELSRQDVKDRVKTMMMKVGLLPNlINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:PRK13549 93 LVKELSVLENIflgNEI--TPGGIMDYDAMYLRAQKLLAQLKLDIN-PATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502790984 190 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICV 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-224 |
5.45e-20 |
|
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: 90.50 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 4 LAEKKVLLEIADLKVHFdirdgkqwfwqpPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWL 83
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGY------------PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 84 GRNLLGQSEEEWRKArsdIQMIFQDP--LASlnprmTIGdiiaEPLRTYHPELSRQDVKDrvktMMMKVGLLpNLINRYP 161
Cdd:TIGR02868 396 GVPVSSLDQDEVRRR---VSVCAQDAhlFDT-----TVR----ENLRLARPDATDEELWA----ALERVGLA-DWLRALP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 162 H-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDL 224
Cdd:TIGR02868 459 DgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
37-237 |
1.49e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDPlaslnpr 116
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS---YCAQTP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLrtYHPELSRQDVKDRVKTM--MMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK10247 91 TLFGDTVYDNL--IFPWQIRNQQPDPAIFLddLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
38-246 |
1.61e-19 |
|
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: 85.66 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG------RVSWL------------GR-N------LLGQSE 92
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtvtvrgRVSSLlglgggfnpeltGReNiylngrLLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 93 EEWRKARSDIQMiFQDplaslnprmtIGDIIAEPLRTYhpelsrqdvkdrvktmmmkvgllpnlinryphefSGGQCQRI 172
Cdd:cd03220 117 KEIDEKIDEIIE-FSE----------LGDFIDLPVKTY----------------------------------SSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 173 GIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-243 |
1.74e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARsdIQMIFQDPLAS-LNP 115
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAG--IAYVPEDRKGEgLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 116 RMTIGD-IIAEPLRTY--HPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:COG1129 344 DLSIREnITLASLDRLsrGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502790984 193 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
42-251 |
2.90e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnLLGQSEEEWRK---ARSDIQMIFQDPLASlnpRMT 118
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-----LDAQPLESWSSkafARKVAYLPQQLPAAE---GMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRTYHPELSRQDVKDR--VKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK10575 102 VRELVAIGRYPWHGALGRFGAADRekVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
40-250 |
3.24e-19 |
|
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: 88.34 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnLLGQseeewrkarsDIQMIFQdplASLnpRMTI 119
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL-----IDGQ----------DIRDVTQ---ASL--RAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 G----------DIIAEPLRTYHPELSRQDVKDRVKtmmmkvglLPNLinrypHEF-------------------SGGQCQ 170
Cdd:COG5265 435 GivpqdtvlfnDTIAYNIAYGRPDASEEEVEAAAR--------AAQI-----HDFieslpdgydtrvgerglklSGGEKQ 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 171 RIGIARALILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELG 246
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSrterAIQAA----LREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
....
gi 502790984 247 TYDE 250
Cdd:COG5265 575 THAE 578
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-241 |
6.08e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.37 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKArsDIQMIFQDPLA------- 111
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN--GIVYISEDRKRdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTI---GDIIAEPLRTYHPElSRQDVKD-----RVKT--MMMKVGLLpnlinryphefSGGQCQRIGIARALILE 181
Cdd:PRK10762 346 SVKENMSLtalRYFSRAGGSLKHAD-EQQAVSDfirlfNIKTpsMEQAIGLL-----------SGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-246 |
6.37e-19 |
|
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: 82.75 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwLGRNLLGQSEEEWRKArsdIQMIFQD 108
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDLEKALSSL---ISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 PlaslnprmtigdiiaeplrtyhpelsrqdvkdrvktMMMKVGLLPNLINRypheFSGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03247 84 P------------------------------------YLFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELG 246
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
34-256 |
7.97e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRN--LLGQSEeewrKARSDIQMIFQDplA 111
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHA----RARRGIGYLPQE--A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGDIIAEPLRTYHpELSRQDVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFH-IEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 192 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
34-256 |
2.78e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGrnllgqsEEE------WRKARSDIQMIFQ 107
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLD-------GEDithlpmHKRARLGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 DPlaSLNPRMTIGD---IIAEPLrtyhpELSRQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:COG1137 86 EA--SIFRKLTVEDnilAVLELR-----KLSKKEREERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 185 IICDEPVSALD---VS-IQAQVVNLlqqlqREMGLSlIFIA-HD----LAVVkhisDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:COG1137 158 ILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIG-VLITdHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 502790984 256 Q 256
Cdd:COG1137 228 L 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-240 |
3.40e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 81.06 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 21 DIRDGKQWFWQPpKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK--ATEGRVSWLGRNLlgqSEEEWRKA 98
Cdd:cd03213 8 NLTVTVKSSPSK-SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPL---DKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 99 rsdIQMIFQDplaslnprmtigDIIaeplrtyHPELSrqdvkdrVKTMMMKVGLLPNLinryphefSGGQCQRIGIARAL 178
Cdd:cd03213 84 ---IGYVPQD------------DIL-------HPTLT-------VRETLMFAAKLRGL--------SGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 179 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDL-AVVKHISDRVLVMYLG 240
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-235 |
3.58e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG----QSEEEWRKarsdiqmifqdPLasl 113
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAyvpqRSEVPDSL-----------PL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 nprmTIGDIIA-------EPLRtyhpELSRQDvKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLII 186
Cdd:NF040873 73 ----TVRDLVAmgrwarrGLWR----RLTRDD-RAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 187 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL 235
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
34-246 |
5.13e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.55 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLV---KATEGRVSWLGRNLlgqSEEEWRKARSdiqmiFQDPL 110
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR---KPDQFQKCVA-----YVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 ASLNPRMTIgdiiAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNL-INRYPHEF----SGGQCQRIGIARALILEPKLI 185
Cdd:cd03234 90 DILLPGLTV----RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLaLTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 186 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
42-253 |
6.06e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRNLLGQ--SEEEWRKarsdIQMIFQDplASLNPRMTI 119
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHyaSKEVARR----IGLLAQN--ATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDIIAEPLRTYHPELSR--QDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK10253 99 QELVARGRYPHQPLFTRwrKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
36-254 |
6.45e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseEEWRKARsdiqmIFQDPLA---- 111
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-----TDWQTAK-----IMREAVAivpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 --SLNPRMTIGDIIAepLRTYHPElsRQDVKDRVKTMMmkvGLLPNLINRYPHE---FSGGQCQRIGIARALILEPKLII 186
Cdd:PRK11614 88 grRVFSRMTVEENLA--MGGFFAE--RDQFQERIKWVY---ELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 187 CDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTN 254
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-237 |
1.24e-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: 80.45 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 30 WQPpkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWR-KARSDIQMIFQD 108
Cdd:cd03290 10 WGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 PLAsLNPRMTIGDIIAEPLRtyhpelsrqdvKDRVKTMMMKVGLLPNlINRYPH-----------EFSGGQCQRIGIARA 177
Cdd:cd03290 88 PWL-LNATVEENITFGSPFN-----------KQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 178 LILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAM 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-247 |
1.30e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 80.84 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 6 EKKVLLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIG--LVKATEGRVSWL 83
Cdd:CHL00131 3 KNKPILEIKNLHASVN-------------ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 84 GRNLLGQSEEEwrKARSDIQMIFQDP-------------LASLNPRMTIGDIIAEPLRTYhpELSRQDVKdrvktmmmKV 150
Cdd:CHL00131 70 GESILDLEPEE--RAHLGIFLAFQYPieipgvsnadflrLAYNSKRKFQGLPELDPLEFL--EIINEKLK--------LV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 151 GLLPNLINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDVS---IQAQVVNLLQQLQRemglSLIFIAHDLAV 226
Cdd:CHL00131 138 GMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRL 213
|
250 260
....*....|....*....|..
gi 502790984 227 VKHIS-DRVLVMYLGHAVELGT 247
Cdd:CHL00131 214 LDYIKpDYVHVMQNGKIIKTGD 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-240 |
1.46e-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: 83.34 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGlvkATEGRvsWLGRNLLGQSEEEWRKA----RSDIQMIFQD-PLA 111
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG---AYPGK--FEGNVFINGKPVDIRNPaqaiRAGIAMVPEDrKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLL------PNL-INRypheFSGGQCQRIGIARALILEPKL 184
Cdd:TIGR02633 349 GIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLkvktasPFLpIGR----LSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 185 IICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 240
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-240 |
1.91e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVsWLGRNL----LGQS--EEEWRKARSDIQMIFQD----- 108
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLrigyLPQEppLDDDLTVLDTVLDGDAElrale 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 -PLASLNPRMTIGDIIAEPLRTYHPELSRQDVKD---RVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKL 184
Cdd:COG0488 94 aELEELEAKLAEPDEDLERLAELQEEFEALGGWEaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 185 IICDEPVSALDV-SIQaqvvnLLQQ-LQREMGlSLIFIAHD---L-AVVKHI---SDRVLVMYLG 240
Cdd:COG0488 174 LLLDEPTNHLDLeSIE-----WLEEfLKNYPG-TVLVVSHDryfLdRVATRIlelDRGKLTLYPG 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
42-256 |
1.98e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEeewrkarsdiQMIFQDPLASLNprmtigd 121
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVP----------QKLYLDTTLPLT------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 122 iiAEPLRTYHPELSRQDVK---DRVKTmmmkvgllPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:PRK09544 86 --VNRFLRLRPGTKKEDILpalKRVQA--------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 199 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYlGHAVELGTYDEVYTNPQ 256
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHPE 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
41-227 |
3.11e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNlLGQSEEEWRKArsdiqMIFQDPLASLNPRMTig 120
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-LDFQRDSIARG-----LLYLGHAPGIKTTLS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 diIAEPLRTYHPELSRQDVKDRVKTMMmkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:cd03231 90 --VLENLRFWHADHSDEQVEEALARVG-----LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|....*..
gi 502790984 201 QVVNLLQQLQREMGLSLIFIAHDLAVV 227
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
43-222 |
4.07e-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: 77.58 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnllgqseeewRKARSDIQMIfqdplaslnprmtigdi 122
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------MPEGEDLLFL----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 123 iaePLRTYhpelsrqdvkdrvktmmMKVGLLPNLINrYP--HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:cd03223 70 ---PQRPY-----------------LPLGTLREQLI-YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 502790984 201 QVVNLLqqlqREMGLSLIFIAH 222
Cdd:cd03223 129 RLYQLL----KELGITVISVGH 146
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
34-251 |
5.50e-17 |
|
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: 81.39 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRV----------------SWLGRN--------- 86
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEPcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 87 -----LLGQSEEEWRKARSDIQMIFQDPLASLNPRMTIGDII-AEPLRTYHPElsrqdvkdrvKTMMMKVGLLP--NLIN 158
Cdd:TIGR03269 91 peevdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLeALEEIGYEGK----------EAVGRAVDLIEmvQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 159 RYPH---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 235
Cdd:TIGR03269 161 RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*.
gi 502790984 236 VMYLGHAVELGTYDEV 251
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV 256
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-236 |
6.00e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.13 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 12 EIADLKVHFDIRDGKQWFWQPPKSL--------KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWL 83
Cdd:COG4586 3 EVENLSKTYRVYEKEPGLKGALKGLfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 84 GRN--------------LLGQseeewrkaRSdiQMIFQDPLA-SLNprmTIGDIiaeplrtYhpELSRQDVKDRVKTM-- 146
Cdd:COG4586 83 GYVpfkrrkefarrigvVFGQ--------RS--QLWWDLPAIdSFR---LLKAI-------Y--RIPDAEYKKRLDELve 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 147 MMKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAV 226
Cdd:COG4586 141 LLDLG---ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDD 217
|
250
....*....|
gi 502790984 227 VKHISDRVLV 236
Cdd:COG4586 218 IEALCDRVIV 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
36-251 |
6.51e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRnllgqseeEWRK------ARSDIQMIFQ-- 107
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI--------NYNKldhklaAQLGIGIIYQel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 ---DPLASLNP----RMTIGDIIAEPLRTYhpelsrQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALIL 180
Cdd:PRK09700 90 sviDELTVLENlyigRHLTKKVCGVNIIDW------REMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 181 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-240 |
6.96e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK-ATEGRVSWLGRNLLGQSEEEwrKARSDIQMIFQD------- 108
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDrkrdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 ---------PLASLNpRMTIGDII--AEPLRTYHPELSRQDVKdrVKTMMMKVGLLpnlinryphefSGGQCQRIGIARA 177
Cdd:PRK13549 354 pvmgvgkniTLAALD-RFTGGSRIddAAELKTILESIQRLKVK--TASPELAIARL-----------SGGNQQKAVLAKC 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 240
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-255 |
7.37e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.30 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkarSDIQMIFQD 108
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR---SRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 PLaslnprmTIGDIIAEPLRTYHPELSRQDVKdrvktmmmKVGLLPNL---INRYPHEF-----------SGGQCQRIGI 174
Cdd:PRK10789 398 PF-------LFSDTVANNIALGRPDATQQEIE--------HVARLASVhddILRLPQGYdtevgergvmlSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 175 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYTN 254
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQ 539
|
.
gi 502790984 255 P 255
Cdd:PRK10789 540 S 540
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
41-227 |
9.54e-17 |
|
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: 77.40 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkarsdiQMIFQDPLASLNPRMTIg 120
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLGHLPGLKPELSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 diiAEPLRTYHPELsrQDVKDRVKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 200
Cdd:TIGR01189 91 ---LENLHFWAAIH--GGAQRTIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....*...
gi 502790984 201 QVVNLL-QQLQREmGLSLIFIAHDLAVV 227
Cdd:TIGR01189 165 LLAGLLrAHLARG-GIVLLTTHQDLGLV 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-236 |
1.93e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLR-----LYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWlgrnllgqseeEWRKA------RSDIQMI 105
Cdd:PRK13409 348 KKLGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------ELKISykpqyiKPDYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 106 FQDPLASLNPRMT---IGDIIAEPLRtyhpelsrqdvkdrvktmmmkvglLPNLINRYPHEFSGGQCQRIGIARALILEP 182
Cdd:PRK13409 417 VEDLLRSITDDLGssyYKSEIIKPLQ------------------------LERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502790984 183 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
41-237 |
2.07e-16 |
|
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: 77.13 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDPLasLNPRmTIG 120
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEPV--LFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 DIIAEPLrtyhpelsrQDVK-DRVKTMMMKVGLlPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 188
Cdd:cd03248 106 DNIAYGL---------QSCSfECVKEAAQKAHA-HSFISELASGYdtevgekgsqlSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVL 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-250 |
2.18e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADLKVHFDirdgkqwfwqppkSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWlGRNL 87
Cdd:COG0488 313 KKVLELEGLSKSYG-------------DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 -LG---QSEEEwrkarsdiqmifqdplasLNPRMTIGDIIAEplrtYHPELSRQDVK----------DRVKTmmmKVGLL 153
Cdd:COG0488 379 kIGyfdQHQEE------------------LDPDKTVLDELRD----GAPGGTEQEVRgylgrflfsgDDAFK---PVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 154 pnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQAqVVNLLQQLQremGlSLIFIAHDLAVVKHISD 232
Cdd:COG0488 434 -----------SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP---G-TVLLVSHDRYFLDRVAT 497
|
250
....*....|....*....
gi 502790984 233 RVLVMYLGHAVE-LGTYDE 250
Cdd:COG0488 498 RILEFEDGGVREyPGGYDD 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-236 |
2.87e-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: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLR-----LYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgqsEEEWRKA------RSDIQMI 105
Cdd:COG1245 349 KSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKISykpqyiSPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 106 FQDPLASLNPRMTIGDI----IAEPLRtyhpelsrqdvkdrvktmmmkvglLPNLINRYPHEFSGGQCQRIGIARALILE 181
Cdd:COG1245 418 VEEFLRSANTDDFGSSYykteIIKPLG------------------------LEKLLDKNVKDLSGGELQRVAIAACLSRD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 182 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
39-246 |
3.04e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.33 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSeeewRKARSDIQMIFQdpLASLNPRMT 118
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA----RLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 igdiIAEPLRTY--HPELSRQDVKDRVKTmMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PRK13536 131 ----VRENLLVFgrYFGMSTREIEAVIPS-LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502790984 197 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:PRK13536 206 HARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-229 |
4.92e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.30 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDIRdgkqwfwqppKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQ 90
Cdd:PTZ00265 383 IQFKNVRFHYDTR----------KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SEEEWrkARSDIQMIFQDPL-----------------------------------ASLNPRMTIGDIIAEPL-------- 127
Cdd:PTZ00265 453 INLKW--WRSKIGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqENKNKRNSCRAKCAGDLndmsnttd 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 128 -------RTYHPELSRQDVKDRVKTMMMK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PTZ00265 531 sneliemRKNYQTIKDSEVVDVSKKVLIHdfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
250 260 270
....*....|....*....|....*....|....*
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 229
Cdd:PTZ00265 611 DNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-250 |
1.11e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 29 FWQPPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMI--- 105
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQVALVsqn 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 106 ---FQDplaslnprmTIGDIIAEPLRTyhpELSRQDVKDRVKtmmMKVGLlpNLINRYPHEF-----------SGGQCQR 171
Cdd:PRK11176 426 vhlFND---------TIANNIAYARTE---QYSREQIEEAAR---MAYAM--DFINKMDNGLdtvigengvllSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 172 IGIARALILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQREMgLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGT 247
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQKNR-TSLV-IAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
...
gi 502790984 248 YDE 250
Cdd:PRK11176 562 HAE 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-255 |
1.37e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKaTEGRVSWLGRNLLGQSEEEWRKArsdIQMIFQDPLAslnPRMTIGD 121
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKH---LSWVGQNPQL---PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 122 IIAeplrtyhpeLSRQDVKD-RVKTMMMKVGL---LPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK11174 442 NVL---------LGNPDASDeQLQQALENAWVsefLPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 191 VSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYTNP 255
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-237 |
1.69e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG--RNLLG--QSEEewrkarSDIQMIFQDplas 112
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGpkSSQE------AGIGIIHQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LN--PRMTIGDII---AEPLRTY--------HPE----LSRQDVKDRVKTMmmkVGllpnlinryphEFSGGQCQRIGIA 175
Cdd:PRK10762 88 LNliPQLTIAENIflgREFVNRFgridwkkmYAEadklLARLNLRFSSDKL---VG-----------ELSIGEQQMVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 176 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
41-248 |
2.89e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 74.06 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGL--VKATEGRVSWLGRNLLGQSEEEwrKARSDIQMIFQDP--LASLNPR 116
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQYPveIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEpLRTY--HPELSRQDVKDRVKTMMMKVGLLPNLINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK09580 97 FFLQTALNA-VRSYrgQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 194 LDV---SIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHIS-DRVLVMYLGHAVELGTY 248
Cdd:PRK09580 176 LDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDF 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
49-253 |
3.31e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 49 GETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLG--------RNLLG---QSEE-EWRKArsdiqmifqdplaslnpr 116
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqalqKNLVAyvpQSEEvDWSFP------------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGDIIAEPLRTYHPELSRQDVKDR--VKTMMMKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLRRAKKRDRqiVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 195 DVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVlVMYLGHAVELGTYDEVYT 253
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFT 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-208 |
3.57e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 10 LLEIADLKVhfdIRDGKQWFwqppkslkavDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG 89
Cdd:PRK13538 1 MLEARNLAC---ERDERILF----------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 QSEEEWRkarsdiQMIFQDPLASLNPRMTIgdiiAEPLRTYHPeLSRQDVKDRVKTMMMKVGL-----LPnlinryPHEF 164
Cdd:PRK13538 68 QRDEYHQ------DLLYLGHQPGIKTELTA----LENLRFYQR-LHGPGDDEALWEALAQVGLagfedVP------VRQL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ 208
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
39-253 |
6.36e-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: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWrkARSdIQMIFQDPlaSLNPRMT 118
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--AKR-LAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIA---EPlrtYHP-ELSRQDvKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:COG4604 92 VRELVAfgrFP---YSKgRLTAED-REIIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 195 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:COG4604 167 DMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-236 |
7.84e-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: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLR-----LYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEeewrKARSDIQMIFQ 107
Cdd:cd03237 4 PTMKKTLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ----YIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 DPLASLNPRMTIgdiiaeplrtyHPELsrqdvkdrvKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:cd03237 80 DLLSSITKDFYT-----------HPYF---------KTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
42-241 |
1.21e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEeewrKARSDIQMIF--QDPLASlnprmti 119
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST----AQRLARGLVYlpEDRQSS------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDIIAEPLR------TYH-PELSRQDVKDR--VKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 190
Cdd:PRK15439 351 GLYLDAPLAwnvcalTHNrRGFWIKPARENavLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502790984 191 VSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGH 241
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-244 |
1.89e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 12 EIADLKVHFDI-RDGKQWFWqppkslkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWlgrnllgq 90
Cdd:COG2401 26 RVAIVLEAFGVeLRVVERYV--------LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 seeewrkarsDIqmifqdPLASLNPRMTIGDIIAeplrtyhpelSRQDVKDRVKTMMMkVGLL-PNLINRYPHEFSGGQC 169
Cdd:COG2401 90 ----------DV------PDNQFGREASLIDAIG----------RKGDFKDAVELLNA-VGLSdAVLWLRRFKELSTGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 170 QRIGIARALILEPKLIICDEPVSALDVSiQAQVVNL-LQQLQREMGLSLIFIAHDLAVVKHIS-DRVLVMYLGHAVE 244
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-250 |
2.63e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.71 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 2 SSLAEKKVLLEIADlkVHFDIRDGKQwfwqppkslKAVDGVSLRLYEGETLGVVGESGCGKSTLaraiIGLV----KATE 77
Cdd:PRK11160 330 STAAADQVSLTLNN--VSFTYPDQPQ---------PVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLtrawDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 78 GRVSWLGRNLLGQSEEEWRKARSDIQM---IFQDplaslnprmTIGD--IIAEPLRTyhpelsrqdvKDRVKTMMMKVGL 152
Cdd:PRK11160 395 GEILLNGQPIADYSEAALRQAISVVSQrvhLFSA---------TLRDnlLLAAPNAS----------DEALIEVLQQVGL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 153 lPNLINRYP----------HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAH 222
Cdd:PRK11160 456 -EKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
250 260
....*....|....*....|....*...
gi 502790984 223 DLAVVKHIsDRVLVMYLGHAVELGTYDE 250
Cdd:PRK11160 533 RLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
39-253 |
2.95e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDPLASLNprMT 118
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRA---YLSQQQSPPFA--MP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAeplRTYHPELSRQDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIARALI-------LEPKLIICDEPV 191
Cdd:COG4138 86 VFQYLA---LHQPAGASSEAVEQLLAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502790984 192 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:COG4138 162 NSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
40-237 |
3.67e-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: 68.63 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWlgrnllgqseeewrkarsdiqmifqdplaslNPRMTI 119
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------------------------GSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GdiiaeplrtyhpelsrqdvkdrvktmmmkvgllpnlinrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 199
Cdd:cd03221 66 G---------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190
....*....|....*....|....*....|....*...
gi 502790984 200 AQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLVM 237
Cdd:cd03221 107 EALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-256 |
4.75e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAtEGRVSWLGRNLLGQSEEEWRKARSdiQMIFQDPLASLNPrmtigd 121
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRA--YLSQQQTPPFAMP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 122 iIAEPLRTYHPELSR-QDVKDRVKTMMMKVGLLPNLiNRYPHEFSGGQCQRIGIA-------RALILEPKLIICDEPVSA 193
Cdd:PRK03695 86 -VFQYLTLHQPDKTRtEAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 194 LDVsiqAQVVnLLQQLQREM---GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PRK03695 164 LDV---AQQA-ALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-268 |
8.90e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDP-L 110
Cdd:PLN03232 1249 PP----VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS---IIPQSPvL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 ASLNPRMTIgdiiaEPLRTYH-----PELSRQDVKDRVKTMMMKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:PLN03232 1322 FSGTVRFNI-----DPFSEHNdadlwEALERAHIKDVIDRNPFG---LDAEVSEGGENFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 186 ICDEPVSALDVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYTNPQHPYTKAL 263
Cdd:PLN03232 1394 VLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
....*
gi 502790984 264 MSAVP 268
Cdd:PLN03232 1469 HSTGP 1473
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-238 |
1.95e-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: 68.93 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 48 EGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgQSEEEWRK-----ARSDIQMIFQDPL-----ASLNPRM 117
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---------DDPPDWDEildefRGSELQNYFTKLLegdvkVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TigDIIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:cd03236 96 V--DLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502790984 198 IQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:cd03236 174 QRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
41-207 |
3.26e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGrnllgqSEEEWRKARSDIQMIfqDPLASLNPRMTIG 120
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYL--GHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 DII---AEPLRTyhPELSRQDVKDRVKtmmmkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK13539 92 ENLefwAAFLGG--EELDIAAALEAVG--------LAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170
....*....|
gi 502790984 198 IQAQVVNLLQ 207
Cdd:PRK13539 162 AVALFAELIR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
55-250 |
3.38e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 55 VGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEeewRKARSDIQMIFQDPL---ASLNPRMTIGDIIAEplrtyh 131
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDPVvlaDTFLANVTLGRDISE------ 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 132 pelsrqdvkDRVKTMMMKVGL------LPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK10790 444 ---------EQVWQALETVQLaelarsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 202 VVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 250
Cdd:PRK10790 515 IQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
30-237 |
1.20e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.95 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 30 WQPPKSL--KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGR-----------------NLLGQ 90
Cdd:cd03250 10 WDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepwiqngtireNILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 91 SE--EEWRKA-------RSDIQMifqdplaslnprMTIGD--IIAEplrtyhpelsrqdvkdrvktmmmkvgllpNLINr 159
Cdd:cd03250 90 KPfdEERYEKvikacalEPDLEI------------LPDGDltEIGE-----------------------------KGIN- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 160 ypheFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVN-LLQQLQREMGLSL---IFIAHDLAVVKHiSDRVL 235
Cdd:cd03250 128 ----LSGGQKQRISLARAVYSDADIYLLDDPLSAVD----AHVGRhIFENCILGLLLNNktrILVTHQLQLLPH-ADQIV 198
|
..
gi 502790984 236 VM 237
Cdd:cd03250 199 VL 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-244 |
1.24e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.28 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAT--EGRVSWLGRNL----LGQSEEEwrkarsDIQMIFQDpL 110
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCrfkdIRDSEAL------GIVIIHQE-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 AsLNPRMTIGDII---AEPLRtyHPELSRQDVKDRVKTMMMKVGLLPNlinryPHEFSG----GQCQRIGIARALILEPK 183
Cdd:NF040905 88 A-LIPYLSIAENIflgNERAK--RGVIDWNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 184 LIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 244
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-236 |
2.76e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 37 KAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnLLGQSEEEWRKAR----SDIQMIFQDplAS 112
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI------LIDGQEMRFASTTaalaAGVAIIYQE--LH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTigdiIAE-------PLR--TYHPELSRQDVKDRVKTMMMKVGllPNLINRYpheFSGGQCQRIGIARALILEPK 183
Cdd:PRK11288 90 LVPEMT----VAEnlylgqlPHKggIVNRRLLNYEAREQLEHLGVDID--PDTPLKY---LSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502790984 184 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
39-195 |
3.57e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.98 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSeeewRKARSDIQMIFQdpLASLNPRMT 118
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHARQRVGVVPQ--FDNLDPDFT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 119 IgdiiAEPLRTY--HPELSRQDVKDRVKTMMmKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13537 97 V----RENLLVFgrYFGLSAAAARALVPPLL-EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-254 |
9.28e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVD---GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEewrKARS-DIQMIFQDP 109
Cdd:PRK15439 19 KQYSGVEvlkGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA---KAHQlGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 110 LasLNPRMTIGDIIAepLRTYHPELSRQDVKDRVKTMM------MKVGLLpNLINRyphefsggqcQRIGIARALILEPK 183
Cdd:PRK15439 96 L--LFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGcqldldSSAGSL-EVADR----------QIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 184 LIICDEPVSALdvsIQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTN 254
Cdd:PRK15439 161 ILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-250 |
1.51e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 25 GKQWFWQPPKSLkaVDGVSLRLYEGETLGVVGESGCGKSTLARAIIG-LVKATEGRVSwlgRNLLGQSEEEWR-KARSDI 102
Cdd:TIGR00955 29 GCFCRERPRKHL--LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGSGS---VLLNGMPIDAKEmRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 103 QMifQDPLasLNPRMTIGD--IIAEPLRTyHPELSRQDVKDRVKTMMMKVGLLP--NLINRYPHE---FSGGQCQRIGIA 175
Cdd:TIGR00955 104 VQ--QDDL--FIPTLTVREhlMFQAHLRM-PRRVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 176 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQL-QRemGLSLIFIAHD-LAVVKHISDRVLVMYLGHAVELGTYDE 250
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-254 |
1.72e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.91 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGR-NLLGQSeeewrkarsdiqmifqdplASLNPR 116
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAIS-------------------SGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MT-IGDIiaePLRTYHPELSRQDVKDrVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 195
Cdd:PRK13545 100 LTgIENI---ELKGLMMGLTKEKIKE-IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 196 VSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTN 254
Cdd:PRK13545 176 QTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-251 |
2.67e-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: 64.97 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGrNLLGQSEEEWrkarsdIQMifqdplA 111
Cdd:TIGR00957 651 PP----TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAW------IQN------D 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGDIIAEPlrtyhpelsrqdvkdRVKTMMMKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILE 181
Cdd:TIGR00957 714 SLRENILFGKALNEK---------------YYQQVLEACALLPDLeilpsgdrteIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 182 PKLIICDEPVSALDVSIQAQVvnlLQQLQREMGL----SLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 251
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
49-241 |
2.77e-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: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 49 GETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGrnllgqseeewrkarsdiqmifqdplaslnprmtigdiiAEPLR 128
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---------------------------------------GEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 129 TYHPELSRQDvkdrvktmmmkvgllpnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV-----V 203
Cdd:smart00382 43 EEVLDQLLLI-----------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502790984 204 NLLQQLQREMGLSLIFIAHDL-----AVVKHISDRVLVMYLGH 241
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
42-247 |
3.59e-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: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDP-LASLNPRMTIg 120
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI---AKIGLHDLRFKITIIPQDPvLFSGSLRMNL- 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 diiaEPLRTYhpelSRQDVKDRVKTMMMK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:TIGR00957 1381 ----DPFSQY----SDEEVWWALELAHLKtfVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 195 DVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVVKHISdRVLVMYLGHAVELGT 247
Cdd:TIGR00957 1453 DLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-261 |
3.89e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 123 IAEPLRTYHPELSRQDVKDRVKTMMMK--VGLLPNL----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 196
Cdd:PTZ00265 1312 IYENIKFGKEDATREDVKRACKFAAIDefIESLPNKydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 197 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM----YLGHAVEL-GTYDEVYTNPQHPYTK 261
Cdd:PTZ00265 1392 NSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAhGTHEELLSVQDGVYKK 1460
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-249 |
3.90e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgQSEEEWRKARsdIQmifQDPlaslnPRMTI 119
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI---------IYEQDLIVAR--LQ---QDP-----PRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 GDI----------IAEPLRTYHpELSRQ---DVKDRVKTMMMKV-------GL--LPNLINRY-------PH----EFSG 166
Cdd:PRK11147 81 GTVydfvaegieeQAEYLKRYH-DISHLvetDPSEKNLNELAKLqeqldhhNLwqLENRINEVlaqlgldPDaalsSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 167 GQCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL- 245
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYp 235
|
....
gi 502790984 246 GTYD 249
Cdd:PRK11147 236 GNYD 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
43-238 |
4.03e-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: 63.65 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLY------EGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgQSEEEWRK-----ARSDIQMIFQDpla 111
Cdd:COG1245 87 GFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---------DEEPSWDEvlkrfRGTELQDYFKK--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 slnprmtigdIIAEPLRTYH-P---ELSRQDVKDRVKTMMMKV---GL---------LPNLINRYPHEFSGGQCQRIGIA 175
Cdd:COG1245 155 ----------LANGEIKVAHkPqyvDLIPKVFKGTVRELLEKVderGKldelaeklgLENILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 176 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
33-229 |
4.74e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 63.61 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnllgqseeewRKARSDIQMIFQDPLAS 112
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT--------------KPAKGKLFYVPQRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNprmTIGDIIAEPLRTYhpELSRQDVKDRVKTMMMKVGLLPNLINR---------YPHEFSGGQCQRIGIARALILEPK 183
Cdd:TIGR00954 528 LG---TLRDQIIYPDSSE--DMKRRGLSDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502790984 184 LIICDEPVSALDVSIQAQVVNLLqqlqREMGLSLIFIAHDLAVVKH 229
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-237 |
6.79e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSE-EEWRKARSDIQMIFQD---- 108
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRRDngff 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 PLASLNPRMTIGDIIAE-----PLRTYHPELSRQDVKDRVKTMMMKVGLLPNLINryphEFSGGQCQRIGIARALILEPK 183
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502790984 184 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF 482
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-237 |
7.67e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEE-----------EWRKARSDIqmifqdPL 110
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagimlcpEDRKAEGII------PV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 111 ASLNPRMTI---------GDIIAEPLRTyhpELSRQDVKD-RVKTmmmkvgllPN---LINryphEFSGGQCQRIGIARA 177
Cdd:PRK11288 346 HSVADNINIsarrhhlraGCLINNRWEA---ENADRFIRSlNIKT--------PSreqLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
48-238 |
1.50e-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: 59.51 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 48 EGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWlgrnllgqseeewrkarsdiqmifqdplaslnPRMTIgdiiaepl 127
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--------------------------------DGITP-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 128 rTYHPElsrqdvkdrvktmmmKVGLlpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 207
Cdd:cd03222 64 -VYKPQ---------------YIDL------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|.
gi 502790984 208 QLQREMGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-220 |
1.56e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwlgrnLLGQSEEewrkARsDIQMifqdplaslnpRM 117
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW-----LFGQPVD----AG-DIAT-----------RR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIG------------------DIIAeplRTYHpeLSRQDVKDRVKTMMMKVGLLPnLINRYPHEFSGGQCQRIGIARALI 179
Cdd:NF033858 340 RVGymsqafslygeltvrqnlELHA---RLFH--LPAAEIAARVAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502790984 180 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSlIFI 220
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFI 453
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-265 |
2.14e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDP-LASLNPRMTI 119
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG---IIPQAPvLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 gdiiaEPLRTYH-----PELSRQDVKDRVKTMMMKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PLN03130 1334 -----DPFNEHNdadlwESLERAHLKDVIRRNSLG---LDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502790984 195 DVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMS 265
Cdd:PLN03130 1406 DVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
36-243 |
4.11e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.43 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVK---ATEGRVSWLGRnllgQSEEEWRKARSDIQMIFQDplas 112
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGI----PYKEFAEKYPGEIIYVSEE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 lnprmtigDIiaeplrtYHPELSrqdVKDRVKTMMMKVGllpnliNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:cd03233 92 --------DV-------HFPTLT---VRETLDFALRCKG------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502790984 193 ALDVSIQAQVVNLLQQLQREMGLSLIFI---AHDLAVvkHISDRVLVMYLGHAV 243
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIY--DLFDKVLVLYEGRQI 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-250 |
7.41e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 40 DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLG---QSEEE--------------WRKARSDI 102
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGyyaQDHAYdfendltlfdwmsqWRQEGDDE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 103 QMIfqdplaslnpRMTIGDIIaeplrtyhpeLSRQDVKDRVKTMmmkvgllpnlinryphefSGGQCQRIGIARALILEP 182
Cdd:PRK15064 416 QAV----------RGTLGRLL----------FSQDDIKKSVKVL------------------SGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 183 KLIICDEPVSALDV-SIQAqvvnLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVE-LGTYDE 250
Cdd:PRK15064 458 NVLVMDEPTNHMDMeSIES----LNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
39-246 |
8.20e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKAT--EGRVSWLGRNLLGQSEEEwrkarsdIQMIFQDPLasLNPR 116
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR-------TGFVTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 117 MTIGD-IIAEPLRTYHPELSRQDVKDRVKTMMMKVGLLP--NLI--NRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 191
Cdd:PLN03211 155 LTVREtLVFCSLLRLPKSLTKQEKILVAESVISELGLTKceNTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502790984 192 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 246
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-247 |
1.06e-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: 60.03 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 33 PKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqsEEEWRKARSDIQMIFQDPLas 112
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNI-- 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDIIaeplrTYHPEL---SRQDVKDRVKTMMMKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR01257 1014 LFHHLTVAEHI-----LFYAQLkgrSWEEAQLEMEAMLEDTG-LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 190 PVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 247
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-238 |
1.36e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 45 RLY------EGETLGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgQSEEEW-----RKARSDIQMIFQDpLASl 113
Cdd:PRK13409 89 KLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---------EEEPSWdevlkRFRGTELQNYFKK-LYN- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 nprmtiGDIiaeplRTYHP----ELSRQDVKDRVKTMMMKV---GL---------LPNLINRYPHEFSGGQCQRIGIARA 177
Cdd:PRK13409 158 ------GEI-----KVVHKpqyvDLIPKVFKGKVRELLKKVderGKldevverlgLENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502790984 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMY 238
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
11-265 |
2.05e-09 |
|
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: 57.23 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 11 LEIADLKVHFDirdgkqwfwqppKSLKAV-DGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlg 89
Cdd:cd03288 20 IKIHDLCVRYE------------NNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 90 qSEEEWRKARSDIQMIFQDPLA-------SLNPRMTIGDiiaeplRTYHPELSRQDVKDRVKTMmmkVGLLPNLINRYPH 162
Cdd:cd03288 86 -SKLPLHTLRSRLSIILQDPILfsgsirfNLDPECKCTD------DRLWEALEIAQLKNMVKSL---PGGLDAVVTEGGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 163 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHdlaVVKHI--SDRVLVMY 238
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAH---RVSTIldADLVLVLS 228
|
250 260
....*....|....*....|....*..
gi 502790984 239 LGHAVELGTYDEVYTNPQHPYTKALMS 265
Cdd:cd03288 229 RGILVECDTPENLLAQEDGVFASLVRT 255
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
34-251 |
2.13e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 34 KSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGrnllgqseeewrkarsDIQMIFQDplASL 113
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 114 NPRMTIGDIIAepLRTYHPELSRQDVKdRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 193
Cdd:PRK13546 97 SGQLTGIENIE--FKMLCMGFKRKEIK-AMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502790984 194 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 251
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-220 |
4.17e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 43 SLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEG-------RVSWLGRNLLGQ-SEEEWRKARSDIQMIFQDPLAsln 114
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITRLSFEQLQKlVSDEWQRNNTDMLSPGEDDTG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 prMTIGDIIAEPLRtyHPELSRQdvkdrvktMMMKVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIICDEPVSAL 194
Cdd:PRK10938 100 --RTTAEIIQDEVK--DPARCEQ--------LAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180
....*....|....*....|....*.
gi 502790984 195 DVSIQAQVVNLLQQLQREmGLSLIFI 220
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLV 191
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
39-257 |
9.55e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGlvkategrvswlgrNLLGQSEEEWRKARSDIQmIFQDPLASLNPRMt 118
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--------------DLTGGGAPRGARVTGDVT-LNGEPLAAIDAPR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 igdiIAEpLRTYHPELSRQDVKDRVKTMMmkvgllpnLINRYPH---------------------------------EFS 165
Cdd:PRK13547 81 ----LAR-LRAVLPQAAQPAFAFSAREIV--------LLGRYPHarragalthrdgeiawqalalagatalvgrdvtTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 166 GGQCQRIGIARAL---------ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 236
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
250 260
....*....|....*....|.
gi 502790984 237 MYLGHAVELGTYDEVYTnPQH 257
Cdd:PRK13547 228 LADGAIVAHGAPADVLT-PAH 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-280 |
9.62e-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: 56.84 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRnLLGQSEEEW---RKARSDIqmIFQDPLASLNPRMT 118
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSWimpGTIKDNI--IFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IGDIIAEPLRTYHPElsrqdvKDrvKTMMMKVGLlpnlinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 198
Cdd:TIGR01271 522 IKACQLEEDIALFPE------KD--KTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 199 QAQ-----VVNLLQQLQRemglslIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVyTNPQHPYTKALMSAVPIPDPD 273
Cdd:TIGR01271 584 EKEifescLCKLMSNKTR------ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL-QAKRPDFSSLLLGLEAFDNFS 655
|
....*..
gi 502790984 274 LEKNKQI 280
Cdd:TIGR01271 656 AERRNSI 662
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
36-253 |
9.86e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCG--KSTLARAIIGlvkATEGRVSW------LGRNLLGQSEEEWRKARSDIQMIFQ 107
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWrf*twcANRRALRRTIG*HRPVR*GRRESFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 108 dplASLNPRMtIGDIIaeplrtyhpELSRQDVKDRVKTMMMKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:NF000106 103 ---GRENLYM-IGR*L---------DLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYT 253
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-291 |
2.78e-08 |
|
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: 55.40 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSLKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLgqseeewrkarSDIQMIFQDplA 111
Cdd:TIGR01257 1948 SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-----------TNISDVHQN--M 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRM-TIGDIIAEPLRTY-HPELSRQDVKD--RVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 187
Cdd:TIGR01257 2015 GYCPQFdAIDDLLTGREHLYlYARLRGVPAEEieKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 188 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYTNPQHPYTKALMSAV 267
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKS 2173
|
250 260
....*....|....*....|....*.
gi 502790984 268 PIPD--PDLekNKQIQLLEGELPSPI 291
Cdd:TIGR01257 2174 PKDDllPDL--NPVEQFFQGNFPGSV 2197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
36-237 |
8.87e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEwrKARSDIQMIFQDplasLN- 114
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQE----LNl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 -------PRMTIGDIIAEPLRTYHPELSRQ----------DVKDRVKTMMMKVGllpnlinryphefsggQCQRIGIARA 177
Cdd:PRK10982 85 vlqrsvmDNMWLGRYPTKGMFVDQDKMYRDtkaifdeldiDIDPRAKVATLSVS----------------QMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 178 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
38-245 |
1.16e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 38 AVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqSEEEWRKARSDIQMIFQDplASLNPRM 117
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLFSAVFTD--FHLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 118 TIGDIIAEPLRTYHPELSRQDVKDRVKtmmMKVGLLPNLinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 197
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLE---LEDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502790984 198 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 245
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-235 |
1.40e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGR-NLLGQSEEEWRKARSDIQMI---------FQD 108
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPALEYVidgdreyrqLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 109 PLASLNPRMTiGDIIAeplrTYHPELSRQD---VKDRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 185
Cdd:PRK10636 97 QLHDANERND-GHAIA----TIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502790984 186 ICDEPVSALDVSiqaQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVL 235
Cdd:PRK10636 172 LLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKII 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
41-256 |
1.48e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 41 GVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRKARSdiqMIFQDP-LASLNPRMTI 119
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS---MIPQDPvLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 120 gdiiaEPLRTYHPE-----LSRQDVKDRVKTmmmKVGLLPNLINRYPHEFSGGQCQRIGIARALILE-PKLIICDEPVS- 192
Cdd:PTZ00243 1405 -----DPFLEASSAevwaaLELVGLRERVAS---ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATAn 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 193 ---ALDVSIQAQVVNLLQqlqremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYTNPQ 256
Cdd:PTZ00243 1477 idpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
42-237 |
1.50e-07 |
|
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: 51.49 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIglvkATEGR------VSWLGRNLLGQSEE---EWRKARSDIQMIFQDpLAS 112
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLAFDTI----YAEGQrryvesLSAYARQFLGQMDKpdvDSIEGLSPAIAIDQK-TTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 113 LNPRMTIGDI--IAEPLRTYHpelSRQDVKDRVKtMMMKVGLLPNLINRYPHEFSGGQCQRIGIARAL--ILEPKLIICD 188
Cdd:cd03270 89 RNPRSTVGTVteIYDYLRLLF---ARVGIRERLG-FLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502790984 189 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03270 165 EPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDI 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
53-237 |
1.61e-07 |
|
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: 50.40 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 53 GVVGESGCGKSTLARAIIGLVkategrvswlGRNLLgqseEEWRKARSDIQMIFQDPLASLnprmtigdiiaeplrtyhp 132
Cdd:cd03238 25 VVTGVSGSGKSTLVNEGLYAS----------GKARL----ISFLPKFSRNKLIFIDQLQFL------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 133 elsrqdvkdrvktmmMKVGL--LPnlINRYPHEFSGGQCQRIGIARALILEPK--LIICDEPVSALDVSIQAQVVNLLQQ 208
Cdd:cd03238 72 ---------------IDVGLgyLT--LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180
....*....|....*....|....*....
gi 502790984 209 LqREMGLSLIFIAHDLAVVKHiSDRVLVM 237
Cdd:cd03238 135 L-IDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
165-264 |
2.86e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKHIsDRVLVMYLGHAV 243
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
90 100
....*....|....*....|.
gi 502790984 244 ELGTYDEVYTNpqHPYTKALM 264
Cdd:PLN03130 819 EEGTYEELSNN--GPLFQKLM 837
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-223 |
7.43e-07 |
|
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: 50.70 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 32 PPKSlKAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGrvswlgrnllgqseEEWRKARSDIQMIFQDPla 111
Cdd:TIGR03719 15 PPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIKVGYLPQEP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 112 SLNPRMTIGDIIAEPLRTYHPELSR--------QDVKDRVKTMMMKVGLLPNLIN------------------RYP---- 161
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVAEIKDALDRfneisakyAEPDADFDKLAAEQAELQEIIDaadawdldsqleiamdalRCPpwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 162 --HEFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHD 223
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
42-251 |
2.90e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGR-----------------NLL-GQSEEEWRkARSDIQ 103
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssqfswimpgtikeNIIfGVSYDEYR-YKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 104 MI-FQDPLASLnprmtigdiiaeplrtyhPElsrqdvKDrvKTMMMKVGLLpnlinrypheFSGGQCQRIGIARALILEP 182
Cdd:cd03291 135 ACqLEEDITKF------------------PE------KD--NTVLGEGGIT----------LSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 183 KLIICDEPVSALDVSIQAQ-----VVNLLQQLQRemglslIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 251
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEifescVCKLMANKTR------ILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
42-228 |
3.51e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLlgqseeEWRKARSDIQMIFQDPLASLNPRMTIGD 121
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 122 IIAEPLRTYHPELSrqdvkdrvKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 201
Cdd:PRK13540 94 NCLYDIHFSPGAVG--------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*..
gi 502790984 202 VVNLLQQLQREMGLSLIFIAHDLAVVK 228
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
42-237 |
3.60e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQS------------EEEWRK----ARSDIQmi 105
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalvTEERRStgiyAYLDIG-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 106 FQDPLASLNPRMT-IGDIIAEPLRTyhpelSRQDVKD--RVKTMMMK--VGLLpnlinryphefSGGQCQRIGIARALIL 180
Cdd:PRK10982 345 FNSLISNIRNYKNkVGLLDNSRMKS-----DTQWVIDsmRVKTPGHRtqIGSL-----------SGGNQQKVIIGRWLLT 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 181 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 237
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM 464
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-196 |
4.75e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGvSLRLYEGETLGVVGESGCGKSTLAR-----AIIGLVKA-----TEGRV-------------SWLGRNLLGQSEEEW 95
Cdd:PLN03073 194 VDA-SVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNcqilhVEQEVvgddttalqcvlnTDIERTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 96 RKARSDIQMIFQDPLASLNPRMTI-GDIIAEPLRTYHPELSRQDV---KDRVKTMMMKVGLLPNLINRYPHEFSGGQCQR 171
Cdd:PLN03073 273 VAQQRELEFETETGKGKGANKDGVdKDAVSQRLEEIYKRLELIDAytaEARAASILAGLSFTPEMQVKATKTFSGGWRMR 352
|
170 180
....*....|....*....|....*
gi 502790984 172 IGIARALILEPKLIICDEPVSALDV 196
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-108 |
5.39e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.87 E-value: 5.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSWLGRNLLGQSEEEWRkarsdiQM---IFQD 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLfsaVFSD 414
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
36-251 |
5.81e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 36 LKAVDGVslrLYEGETLGVVGESGCGKSTLARAI----IGLVKATEGRVSWLGrnlLGQSEEEWRK-------ARSDIQM 104
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG---ITPEEIKKHYrgdvvynAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 105 ifqdplaslnPRMTIGDII--AEPLRTyhPE-----LSRQDVKDRVKTMMM-----------KVGllpnliNRYPHEFSG 166
Cdd:TIGR00956 151 ----------PHLTVGETLdfAARCKT--PQnrpdgVSREEYAKHIADVYMatyglshtrntKVG------NDFVRGVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 167 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREM-GLSLIFI------AHDLAvvkhisDRVLVMYL 239
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILdTTPLVAIyqcsqdAYELF------DKVIVLYE 286
|
250
....*....|..
gi 502790984 240 GHAVELGTYDEV 251
Cdd:TIGR00956 287 GYQIYFGPADKA 298
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-196 |
6.59e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.62 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwLGRNL----LGQSeeewRKARSDIQMIFQDpLASLN 114
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVklayVDQS----RDALDPNKTVWEE-ISGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 115 PRMTIGDIIAePLRTYhpeLSRQDVK--DRVKtmmmKVGLLpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVS 192
Cdd:TIGR03719 412 DIIKLGKREI-PSRAY---VGRFNFKgsDQQK----KVGQL-----------SGGERNRVHLAKTLKSGGNVLLLDEPTN 472
|
....
gi 502790984 193 ALDV 196
Cdd:TIGR03719 473 DLDV 476
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
165-254 |
7.71e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHIsDRVLVMYLGHA 242
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
90
....*....|..
gi 502790984 243 VELGTYDEVYTN 254
Cdd:PLN03232 818 KEEGTFAELSKS 829
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-227 |
1.14e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 8 KVLLEIADlkVHFDIrDGKQwfwqppkslkAVDGVSLRLYEGETLGVVGESGCGKSTLARAIIGLVKATEGRVSwLGRNL 87
Cdd:PRK11147 317 KIVFEMEN--VNYQI-DGKQ----------LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 88 lgqseeewrkarsDIQMiFQDPLASLNPRMTIGDIIAEPLRT------------------YHPELSRQDVKdrvktmmmk 149
Cdd:PRK11147 383 -------------EVAY-FDQHRAELDPEKTVMDNLAEGKQEvmvngrprhvlgylqdflFHPKRAMTPVK--------- 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 150 vgllpnlinryphEFSGGQCQRIGIARaLILEP-KLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVV 227
Cdd:PRK11147 440 -------------ALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-199 |
1.46e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 42 VSLRLYEGETLGVVGESGCGKSTLARAIIGLVkATEGRVSWLGRNLLGQSEEEWRKARSDI-QMIFqdpLASLNPRMTIg 120
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIpQKVF---IFSGTFRKNL- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 121 diiaEPlrtyHPELSRQDVKdRVKTmmmKVGlLPNLINRYPHE-----------FSGGQCQRIGIARALILEPKLIICDE 189
Cdd:TIGR01271 1313 ----DP----YEQWSDEEIW-KVAE---EVG-LKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170
....*....|.
gi 502790984 190 PVSALD-VSIQ 199
Cdd:TIGR01271 1380 PSAHLDpVTLQ 1390
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
39-222 |
9.55e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 43.74 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 39 VDGVslrLYEGETLGVVGESGCGKSTLARAIIglVKATEGRvSWLGRnllgqseeewrkarsdiqmifqdplaSLNPRMT 118
Cdd:COG3598 6 VPGL---LPEGGVTLLAGPPGTGKSFLALQLA--AAVAAGG-PWLGR--------------------------RVPPGKV 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 119 IgdIIAEplrtyhpELSRQDVKDRVKTMMMKVGLLPNLINRYPHEFSGGQC-QRIGIARALILE-----PKLIICDePVS 192
Cdd:COG3598 54 L--YLAA-------EDDRGELRRRLKALGADLGLPFADLDGRLRLLSLAGDlDDTDDLEALERAieeegPDLVVID-PLA 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 502790984 193 AL------DVSIQAQVVNLLQQLQREMGLSLIFIAH 222
Cdd:COG3598 124 RVfggdenDAEEMRAFLNPLDRLAERTGAAVLLVHH 159
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-243 |
2.38e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 9 VLLEIADLKVHFDIRDGKQwfwqppkslkAVDGVSLRLYEGETLGVVGESGCGK-------------------------- 62
Cdd:NF040905 256 VVFEVKNWTVYHPLHPERK----------VVDDVSLNVRRGEIVGIAGLMGAGRtelamsvfgrsygrnisgtvfkdgke 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 63 ---STLARAI-IGLVKATEGRVSwLGRNLLgqseeewrkarSDIQmiFQDPLASLnPRMTIGDIIAEplrtyHPELS--- 135
Cdd:NF040905 326 vdvSTVSDAIdAGLAYVTEDRKG-YGLNLI-----------DDIK--RNITLANL-GKVSRRGVIDE-----NEEIKvae 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 136 --RQDVKDRVKTMMMKVGllpNLinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREm 213
Cdd:NF040905 386 eyRKKMNIKTPSVFQKVG---NL--------SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE- 453
|
250 260 270
....*....|....*....|....*....|
gi 502790984 214 GLSLIFIAHDLAVVKHISDRVLVMYLGHAV 243
Cdd:NF040905 454 GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
52-265 |
2.84e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 52 LGVVGESGCGKSTLARAIIGLVKATEGRVswlgrnllgqseeeWRKARSDIQMIFQDPLASLnprmtigDIIAEPL---- 127
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHHVDGL-------DLSSNPLlymm 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 128 RTYhPELSRQdvkdRVKTMMMKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaQVVNLLQ 207
Cdd:PLN03073 597 RCF-PGVPEQ----KLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQ 668
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502790984 208 QLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVEL-GTYdevytnpqHPYTKALMS 265
Cdd:PLN03073 669 GLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKVTPFhGTF--------HDYKKTLQS 718
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
165-228 |
3.21e-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: 3.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502790984 165 SGGQCQRIGIARALILE---PKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK 228
Cdd:cd03271 171 SGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 236
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
165-290 |
3.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 165 SGGQCQRIGIARALIL---EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKhISDRVLvmYLG- 240
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVK-VADYVL--ELGp 886
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 502790984 241 HAVELGTYDEVYTNPQH------PYTKALMsavpipdPDLEKNKQIQLLEGELPSP 290
Cdd:PRK00635 887 EGGNLGGYLLASCSPEElihlhtPTAKALR-------PYLSSPQELPYLPDPSPKP 935
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
165-232 |
8.02e-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: 41.15 E-value: 8.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502790984 165 SGGQCQRIGIARALILE---PKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK---HISD 232
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIKtadYIID 903
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-222 |
1.12e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502790984 137 QDVKDRVKTMMMK----VGLLPNLINRYPHEFSGGQcQRIG-IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQR 211
Cdd:PRK10938 371 QAVSDRQQKLAQQwldiLGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIS 449
|
90
....*....|.
gi 502790984 212 EMGLSLIFIAH 222
Cdd:PRK10938 450 EGETQLLFVSH 460
|
|
| |
