|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-334 |
0e+00 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 791.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 4 VTEGRKVLLEIADLKVHFEIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAW 83
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 84 LGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPH 163
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 164 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 243
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 244 VELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFR 323
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFR 320
|
330
....*....|.
gi 15831001 324 HAVSCLKVDPL 334
Cdd:PRK15079 321 HAVSCLKVDPL 331
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-328 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 547.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 7 GRKVLLEIADLKVHFEIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGK 86
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGG--LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFS 166
Cdd:COG4608 81 DITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLR-IHGLASKAERRERVAELLELVGLRPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 167 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 246
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 247 GTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIqlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL-EGSFRHA 325
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAVPVPDPERRRERIV--LEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLrEVGPGHQ 317
|
...
gi 15831001 326 VSC 328
Cdd:COG4608 318 VAC 320
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-333 |
1.38e-179 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 499.19 E-value: 1.38e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA---TDGHVAWLGKE 87
Cdd:COG0444 1 LLEVRNLKVYFPTRRG---------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 88 LLGMKPDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGLLP--NLINRYPHE 164
Cdd:COG0444 72 LLKLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLR-IHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 165 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 244
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 245 ELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL-EGSFR 323
Cdd:COG0444 231 EEGPVEELFENPRHPYTRALLSSIPRLDPDGRRLIPI---PGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLrEVGPG 307
|
330
....*....|
gi 15831001 324 HAVSCLKVDP 333
Cdd:COG0444 308 HRVACHLYEE 317
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-332 |
6.00e-152 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 429.77 E-value: 6.00e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVHFEIKDGkqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL 88
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRG---LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 LGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGG 168
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLI-NTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 169 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 248
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 249 YDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTiqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHAVSC 328
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPRLNPDDRRERI--KLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVAC 316
|
....
gi 15831001 329 LKVD 332
Cdd:PRK11308 317 FAVE 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-272 |
5.78e-150 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 432.19 E-value: 5.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 3 AVTEGRKVLLEIADLKVHFEIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGHVA 82
Cdd:COG4172 267 PVPPDAPPLLEARDLKVWFPIKRG--LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 83 WLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRYP 162
Cdd:COG4172 344 FDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 163 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|
gi 15831001 243 AVELGTYDEVYHNPLHPYTRALMSAVPIPD 272
Cdd:COG4172 504 VVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-274 |
8.54e-145 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 418.54 E-value: 8.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 3 AVTEGRKVLLEIADLKVHFEIKdgkqwfwqPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVA 82
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYPVR--------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 83 WLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGLLPNLINRYP 162
Cdd:COG1123 324 FDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLR-LHGLLSRAERRERVAELLERVGLPPDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 163 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250 260 270
....*....|....*....|....*....|..
gi 15831001 243 AVELGTYDEVYHNPLHPYTRALMSAVPIPDPD 274
Cdd:COG1123 483 IVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-247 |
8.09e-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: 8.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLG 90
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSV---------KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 MKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQC 170
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-270 |
1.27e-111 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 324.45 E-value: 1.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlg 90
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV---------PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 mKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHpkmsRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQC 170
Cdd:COG1124 70 -TRRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 250
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250 260
....*....|....*....|
gi 15831001 251 EVYHNPLHPYTRALMSAVPI 270
Cdd:COG1124 225 DLLAGPKHPYTRELLAASLA 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-287 |
8.81e-105 |
|
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: 317.01 E-value: 8.81e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL----VKATDGHVAWLGK 86
Cdd:COG4172 6 LLSVEDLSVAFG---------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKMSRQEVRERVKAMMLKVGLlPN---LINRYP 162
Cdd:COG4172 77 DLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRL-HRGLSGAAARARALELLERVGI-PDperRLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 163 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15831001 243 AVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLEGE 287
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-319 |
1.06e-94 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 284.31 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 1 MNAVTEGRKVLLEIADLKVHFEIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA---T 77
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDG---------DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 78 DGHVAWLGKELLGMKPDEWRAVRSD-IQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQE-VRERVKamMLKVGLLP 155
Cdd:PRK09473 73 GGSATFNGREILNLPEKELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLM-LHKGMSKAEaFEESVR--MLDAVKMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 156 NL---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS 232
Cdd:PRK09473 150 EArkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 233 DRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQlleGELPSPINPPSGCVFRTRCPIAGPECA 312
Cdd:PRK09473 230 DKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIP---GNPPNLLRLPKGCPFQPRCPHAMEICS 306
|
....*..
gi 15831001 313 KTrPVLE 319
Cdd:PRK09473 307 SA-PPLE 312
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-325 |
1.46e-93 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 290.60 E-value: 1.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 2 NAVTEGRKVLlEIADLKVHFEIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHV 81
Cdd:PRK10261 305 DTVVDGEPIL-QVRNLVTRFPLRSG--LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 82 AWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKMSRQEVRERVKAMMLKVGLLPNLINRY 161
Cdd:PRK10261 382 IFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRV-HGLLPGKAAAARVAWLLERVGLLPEHAWRY 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 162 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 241
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 242 HAVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGS 321
Cdd:PRK10261 541 QIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRV-LLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYA 619
|
....
gi 15831001 322 FRHA 325
Cdd:PRK10261 620 FMRR 623
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-267 |
2.75e-93 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 278.26 E-value: 2.75e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDGkqWFWQppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELLG 90
Cdd:COG4167 4 LLEVRNLSKTFKYRTG--LFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEI-LINGHKLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 MKPDEWRAvrSDIQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQC 170
Cdd:COG4167 79 YGDYKYRC--KHIRMIFQDPNTSLNPRLNIGQILEEPLR-LNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 250
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTA 235
|
250
....*....|....*..
gi 15831001 251 EVYHNPLHPYTRALMSA 267
Cdd:COG4167 236 EVFANPQHEVTKRLIES 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-273 |
3.67e-80 |
|
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: 252.90 E-value: 3.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeikdgkqwfwqPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT---DGHVAWLGKE 87
Cdd:COG1123 4 LLEVRDLSVRY-----------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 88 LLGMKPDEWRAvrsDIQMIFQDPLASLNPrMTIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSG 167
Cdd:COG1123 73 LLELSEALRGR---RIGMVFQDPMTQLNP-VTVGDQIAEALEN--LGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 168 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260
....*....|....*....|....*.
gi 15831001 248 TYDEVYHNPlhpytrALMSAVPIPDP 273
Cdd:COG1123 226 PPEEILAAP------QALAAVPRLGA 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-328 |
1.04e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 243.50 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeiKDGKQWFwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATDGHVAWLGK 86
Cdd:PRK11022 3 LLNVDKLSVHF--GDESAPF-------RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDEWRA-VRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKMSRQEVRERVKAMMLKVGLlPNLINR---YP 162
Cdd:PRK11022 74 DLQRISEKERRNlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKV-HQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 163 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 243 AVELGTYDEVYHNPLHPYTRALMSAVpipdPDLEKNKT-IQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGS 321
Cdd:PRK11022 232 VVETGKAHDIFRAPRHPYTQALLRAL----PEFAQDKArLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNML 307
|
....*..
gi 15831001 322 FRHAVSC 328
Cdd:PRK11022 308 AGRQSKC 314
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
11-328 |
4.81e-76 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 236.73 E-value: 4.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGHVA-----WLG 85
Cdd:COG4170 3 LLDIRNLTIEIDTPQGR---------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTadrfrWNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 86 KELLGMKPDEWRA-VRSDIQMIFQDPLASLNPRMTIGEIIAE--PLRTYHPK-MSR-QEVRERVKAMMLKVGLLPN--LI 158
Cdd:COG4170 73 IDLLKLSPRERRKiIGREIAMIFQEPSSCLDPSAKIGDQLIEaiPSWTFKGKwWQRfKWRKKRAIELLHRVGIKDHkdIM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 159 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:COG4170 153 NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 239 YLGHAVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTrPVL 318
Cdd:COG4170 233 YCGQTVESGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PRL 311
|
330
....*....|
gi 15831001 319 EGSFRHAVSC 328
Cdd:COG4170 312 RKIKGHEFAC 321
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
40-273 |
6.99e-76 |
|
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: 233.93 E-value: 6.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMT 119
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAEPLRTYHpKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:TIGR02769 107 VRQIIGEPLRHLT-SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 200 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPlHPYTRALMSAVPIPDP 273
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFK-HPAGRNLQSAVLPEHP 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-266 |
3.17e-75 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 240.38 E-value: 3.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 4 VTEGRKVLLEIADLKVHFEIKDGKQWFWQPPKTlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGHVAW 83
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKGILKRTVDHNV--VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 84 LGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPH 163
Cdd:PRK15134 345 DGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 164 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 243
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
250 260
....*....|....*....|...
gi 15831001 244 VELGTYDEVYHNPLHPYTRALMS 266
Cdd:PRK15134 505 VEQGDCERVFAAPQQEYTRQLLA 527
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
40-274 |
3.33e-74 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 229.96 E-value: 3.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMT 119
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAEPLRtyH-PKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK10419 108 VREIIREPLR--HlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPlHPYTRALMSAVPIPDPD 274
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFS-SPAGRVLQNAVLPAFPV 260
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-267 |
1.18e-68 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 215.42 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVHFEIKDGkqWFWQppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL 88
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTG--WFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 lGMKPDEWRAVRsdIQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGG 168
Cdd:PRK15112 78 -HFGDYSYRSQR--IRMIFQDPSTSLNPRQRISQILDFPLR-LNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 169 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 248
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*....
gi 15831001 249 YDEVYHNPLHPYTRALMSA 267
Cdd:PRK15112 234 TADVLASPLHELTKRLIAG 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-263 |
1.96e-67 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 211.38 E-value: 1.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 8 RKVLLEIADLKVHFeikdGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKE 87
Cdd:COG1127 2 SEPMIEVRNLTKSF----GDR---------VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 88 LLGMKPDEWRAVRSDIQMIFQDP--LASlnprMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGlLPNLINRYPHEF 165
Cdd:COG1127 69 ITGLSEKELYELRRRIGMLFQGGalFDS----LTVFENVAFPLR-EHTDLSEAEIRELVLEKLELVG-LPGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 166 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 245
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|....*...
gi 15831001 246 LGTYDEVYHNPlHPYTRA 263
Cdd:COG1127 223 EGTPEELLASD-DPWVRQ 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
30-287 |
8.50e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 213.02 E-value: 8.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQD 109
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 plASLNPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 189
Cdd:COG1135 91 --FNLLSSRTVAENVALPLE--IAGVPKAEIRKRVAELLELVG-LSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 190 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVP 269
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVL 245
|
250
....*....|....*...
gi 15831001 270 IPDPDLEKNKTIQLLEGE 287
Cdd:COG1135 246 NDELPEELLARLREAAGG 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-269 |
1.03e-66 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 220.50 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVA----WLGK 86
Cdd:PRK10261 12 VLAVENLNIAFM---------QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ------ELLGMKPDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGL--LPNL 157
Cdd:PRK10261 83 rsrqviELSEQSAAQMRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIR-LHQGASREEAMVEAKRMLDQVRIpeAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 158 INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270
....*....|....*....|....*....|..
gi 15831001 238 MYLGHAVELGTYDEVYHNPLHPYTRALMSAVP 269
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-285 |
2.14e-63 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 209.56 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL-----VKATDGHVAWLG 85
Cdd:PRK15134 5 LLAIENLSVAFR---------QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 86 KELLGMKPDEWRAVRSD-IQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKMSRQEVRERVKAMMLKVGL--LPNLINRYP 162
Cdd:PRK15134 76 ESLLHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVL-SLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 163 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15831001 243 AVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLE 285
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLD 277
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-256 |
2.31e-63 |
|
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: 200.89 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 22 EIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRS 101
Cdd:cd03258 3 ELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 102 DIQMIFQ--DPLASLnprmTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 179
Cdd:cd03258 83 RIGMIFQhfNLLSSR----TVFENVALPLE--IAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 180 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
35-268 |
9.76e-63 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 200.04 E-value: 9.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKE-----LLGMKPDEWRAV-RSDIQMIFQ 108
Cdd:COG4107 23 GTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDggprdLFALSEAERRRLrRTDWGMVYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 DPLASLNPRMTIGEIIAEPL-----RTYhpkmsrQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEP 183
Cdd:COG4107 103 NPRDGLRMDVSAGGNIAERLmaageRHY------GDIRARALEWLERVEIPLERIDDLPRTFSGGMQQRVQIARALVTNP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRA 263
Cdd:COG4107 177 RLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLEDPQHPYTQL 256
|
....*
gi 15831001 264 LMSAV 268
Cdd:COG4107 257 LVSSV 261
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
41-262 |
2.93e-62 |
|
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: 198.11 E-value: 2.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDplASLNPRMTI 120
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS--GALFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 GEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:cd03261 95 FENVAFPLR-EHTRLSEEEIREIVLEKLEAVG-LRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 201 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPlHPYTR 262
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVR 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-260 |
3.37e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 196.47 E-value: 3.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 8 RKVLLEIADLKVHFeikdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKE 87
Cdd:COG3842 2 AMPALELENVSKRY-------------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 88 LLGMKPDEwravRsDIQMIFQDPlaSLNPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSG 167
Cdd:COG3842 69 VTGLPPEK----R-NVGMVFQDY--ALFPHLTVAENVAFGLR--MRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 168 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD----LAvvkhISDRVLVMYLGHA 243
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRI 214
|
250
....*....|....*..
gi 15831001 244 VELGTYDEVYHNPLHPY 260
Cdd:COG3842 215 EQVGTPEEIYERPATRF 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-328 |
3.50e-58 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 190.78 E-value: 3.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGHVAWLGK 86
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG---------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDEWRA-VRSDIQMIFQDPLASLNPRMTIGE--IIAEPLRTYHPK-MSRQEVRERVKAMML-KVGLL--PNLIN 159
Cdd:PRK15093 74 DLLRLSPRERRKlVGHNVSMIFQEPQSCLDPSERVGRqlMQNIPGWTYKGRwWQRFGWRKRRAIELLhRVGIKdhKDAMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 160 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 240 LGHAVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTrPVLE 319
Cdd:PRK15093 234 CGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRLT 312
|
....*....
gi 15831001 320 GSFRHAVSC 328
Cdd:PRK15093 313 GAKNHLYAC 321
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-268 |
8.39e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 186.74 E-value: 8.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 22 EIKDGKQWFwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELLGMKPDEWRAVRS 101
Cdd:COG1126 3 EIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-TVDGEDLTDSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 102 DIQMIFQdplaSLN--PRMTIGEIIAEPLRTYHpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARAL 179
Cdd:COG1126 78 KVGMVFQ----QFNlfPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 180 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 259
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*....
gi 15831001 260 YTRALMSAV 268
Cdd:COG1126 231 RTRAFLSKV 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
22-277 |
1.18e-57 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 189.63 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 22 EIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRS 101
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 102 DIQMIFQ--DPLASlnprMTIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 179
Cdd:PRK11153 83 QIGMIFQhfNLLSS----RTVFDNVALPLEL--AGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 180 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 259
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
250 260
....*....|....*....|.
gi 15831001 260 YTRALMSAV---PIPDPDLEK 277
Cdd:PRK11153 236 LTREFIQSTlhlDLPEDYLAR 256
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-245 |
2.88e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 179.85 E-value: 2.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVHFeiKDGKQwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL 88
Cdd:COG1136 2 SPLLELRNLTKSY--GTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 LGMKPDEWRAVRSD-IQMIFQDPlaSLNPRMTIGEIIAEPLRtYHpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSG 167
Cdd:COG1136 73 SSLSERELARLRRRhIGFVFQFF--NLLPELTALENVALPLL-LA-GVSRKERRERARELLERVGL-GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 168 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 245
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
39-247 |
7.25e-55 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 178.10 E-value: 7.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewravRSDIQMIFQDPlaSLNPRM 118
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIGMVFQDY--ALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:cd03259 88 TVAENIAFGLK--LRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
34-256 |
7.10e-54 |
|
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: 176.37 E-value: 7.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQDPLAS 113
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 L-NPrmTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:COG1122 88 LfAP--TVEEDVAFGPENL--GLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 193 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
36-268 |
7.85e-54 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 177.04 E-value: 7.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 36 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGK-----ELLGMKPDEWRAV-RSDIQMIFQD 109
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLlRTEWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 PLASLNPRMTIGEIIAEPL-----RTYhpkmsrQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPK 184
Cdd:PRK11701 98 PRDGLRMQVSAGGNIGERLmavgaRHY------GDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 185 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRAL 264
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
....
gi 15831001 265 MSAV 268
Cdd:PRK11701 252 VSSV 255
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-238 |
1.41e-53 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 175.35 E-value: 1.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgm 91
Cdd:cd03293 1 LEVRNVSKTYGGGGG---------AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 kpdewRAVRSDIQMIFQDPlaSLNPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQ 171
Cdd:cd03293 69 -----TGPGPDRGYVFQQD--ALLPWLTVLDNVALGLE--LQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 172 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVM 238
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
35-242 |
3.42e-53 |
|
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: 174.22 E-value: 3.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSD-IQMIFQDPlaS 113
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSF--N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:cd03255 93 LLPDLTALENVELPLL--LAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831001 194 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGH 242
Cdd:cd03255 170 NLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-238 |
7.95e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 174.51 E-value: 7.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 7 GRKVLLEIADLKVHFEIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGK 86
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG---------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDewRAvrsdiqMIFQDPlaSLNPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLLPnLINRYPHEFS 166
Cdd:COG1116 74 PVTGPGPD--RG------VVFQEP--ALLPWLTVLDNVALGLE--LRGVPKAERRERARELLELVGLAG-FEDAYPHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 167 GGQCQRIGIARALILEPKLIICDEPVSALDV----SIQaqvvNLLQQLQREMGLSLIFIAHDL--AVVkhISDRVLVM 238
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVdeAVF--LADRVVVL 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
39-256 |
3.08e-52 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 172.04 E-value: 3.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrsdIQMIFQDplASLNPRM 118
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-----VNTVFQN--YALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:cd03300 88 TVFENIAFGLRL--KKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
29-242 |
4.71e-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: 171.11 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 29 WFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQ 108
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 DPLASL-NPrmTIGEIIAEPLRTYHpkMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLII 187
Cdd:cd03225 83 NPDDQFfGP--TVEEEVAFGLENLG--LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 188 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
38-242 |
1.74e-50 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 165.82 E-value: 1.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKpDEWRAVRSDIQMIFQDPlaSLNPR 117
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLrtyhpkmsrqevrervkammlkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:cd03229 91 LTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831001 198 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-242 |
3.79e-49 |
|
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: 163.47 E-value: 3.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 21 FEIKDGKQWFwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDeWRAVR 100
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN-INELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 101 SDIQMIFQDplASLNPRMTIGEIIAEPLRTYHpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALI 180
Cdd:cd03262 76 QKVGMVFQQ--FNLFPHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 181 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-269 |
5.39e-49 |
|
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: 165.12 E-value: 5.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRS-DIQMIFQDplASLNPR 117
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYHpkMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:cd03294 117 RTVLENVAFGLEVQG--VPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 198 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVP 269
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
38-244 |
7.16e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 164.07 E-value: 7.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPlaSLNPR 117
Cdd:COG3638 17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIFQQF--NLVPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MT------IGEIIAEP-LRTYHPKMSRQEvRERVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:COG3638 95 LSvltnvlAGRLGRTStWRSLLGLFPPED-RERALEALERVGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 244
Cdd:COG3638 173 PVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
38-268 |
1.86e-48 |
|
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: 163.08 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGK-----ELLGM-KPDEWRAVRSDIQMIFQDPL 111
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLsEAERRRLMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 112 ASLNPRMTIGEIIAEPL-----RTYhpkmsrQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 186
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLmaigaRHY------GNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMS 266
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVS 250
|
..
gi 15831001 267 AV 268
Cdd:TIGR02323 251 SI 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
38-256 |
3.58e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.25 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwravRsDIQMIFQDPlaSLNPR 117
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----R-NIAMVFQSY--ALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTyhPKMSRQEVRERVKAM--MLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:COG3839 90 MTVYENIAFPLKL--RKVPKAEIDRRVREAaeLLG---LEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHD------LAvvkhisDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG3839 165 DAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
38-260 |
3.85e-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: 3.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwravrSDIQMIFQDplASLNPR 117
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYH--PKMSRQEVRERVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:cd03296 89 MTVFDNVAFGLRVKPrsERPPEAEIRAKVHEL-LKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 260
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
38-256 |
1.09e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.08 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkpDEWRAVR-SDIQMIFQDPLasLNP 116
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-----FTNLPPReRRVGFVFQHYA--LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:COG1118 89 HMTVAENIAFGLR--VRPPSKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 197 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG1118 166 AKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
34-245 |
2.07e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.05 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDplAS 113
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:COG2884 90 LLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831001 194 ALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 245
Cdd:COG2884 167 NLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-256 |
2.07e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 158.57 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 1 MNAVTEGRKVLLEIADLKVHFeikDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGH 80
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSF---DGKE----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 81 VAWLGKELLGMkPDEWRavrsDIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKMSRQEVRERVKAMmLKVGLLPNLINR 160
Cdd:PRK09452 71 IMLDGQDITHV-PAENR----HVNTVFQS--YALFPHMTVFENVAFGLRM--QKTPAAEITPRVMEA-LRMVQLEEFAQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 161 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYL 240
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD 220
|
250
....*....|....*.
gi 15831001 241 GHAVELGTYDEVYHNP 256
Cdd:PRK09452 221 GRIEQDGTPREIYEEP 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-242 |
2.95e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 20 HFEIKDGKQWFWQPpktlkavdgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRav 99
Cdd:COG4619 5 GLSFRVGGKPILSP---------VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 100 rSDIQMIFQDPLAslnPRMTIGEIIAEPLRTYHPKMSRqevrERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARAL 179
Cdd:COG4619 74 -RQVAYVPQEPAL---WGGTVRDNLPFPFQLRERKFDR----ERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 180 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
38-262 |
4.02e-45 |
|
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: 154.00 E-value: 4.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavRSdIQMIFQDplASLNPR 117
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--RK-IGYVIQQ--IGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAeplrtYHPKM---SRQEVRERVKAMMLKVGLLP-NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:cd03295 90 MTVEENIA-----LVPKLlkwPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 194 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTR 262
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
38-252 |
3.97e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.37 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkPDEWRAVRSDIQMIFQDPlaSLNPR 117
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRRIGYVPQEP--ALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:COG1131 88 LTVRENLRFFARLY--GLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 198 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:COG1131 165 EARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
38-247 |
5.73e-44 |
|
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: 150.10 E-value: 5.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwravrSDIQMIFQDplASLNPR 117
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIAMVFQN--YALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYhpKMSRQEVRERVK--AMMLKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:cd03301 87 MTVYDNIAFGLKLR--KVPKDEIDERVRevAELLQIE---HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
38-252 |
9.34e-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: 9.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPlaSLNPR 117
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYHPKM-------SRQEvRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:cd03256 93 LSVLENVLSGRLGRRSTWrslfglfPKEE-KQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-256 |
1.50e-43 |
|
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: 150.57 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 10 VLLEIADLKVHFeikdGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELL 89
Cdd:COG0411 3 PLLEVRGLTKRF----GG---------LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 90 GMKPDEwRA----VRSdiqmiFQdpLASLNPRMTIGE-------------IIAEPLRTYHPKMSRQEVRERVKAMMLKVG 152
Cdd:COG0411 70 GLPPHR-IArlgiART-----FQ--NPRLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 153 LLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS 232
Cdd:COG0411 142 LAD-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
250 260
....*....|....*....|....
gi 15831001 233 DRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG0411 221 DRIVVLDFGRVIAEGTPAEVRADP 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
40-191 |
2.02e-43 |
|
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: 146.64 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQDPlaSLNPRMT 119
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 120 IGEIIAEPLRTYHpkMSRQEVRERVKAMMLKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:pfam00005 76 VRENLRLGLLLKG--LSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
40-252 |
1.89e-42 |
|
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: 147.50 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSdiqMIFQDPLASLNprMT 119
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA---YVPQEPPAPFG--LT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAepL-RT-YHPKMSR--QEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:COG1120 92 VRELVA--LgRYpHLGLFGRpsAEDREAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:COG1120 169 DLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
38-252 |
2.27e-42 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 146.56 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-----TDGHVAWLGKELLGMKPDEwRAVRSDIQMIFQDPla 112
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDV-LELRRRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 slNP-RMTIGEIIAEPLRtYHPKMSRQEVRERVKAMMLKVGLLPNLINR-YPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:cd03260 91 --NPfPGSIYDNVAYGLR-LHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-256 |
3.82e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 145.94 E-value: 3.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 17 LKVHFEIKDGKQWFwqppktlkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDew 96
Cdd:cd03299 1 LKVENLSKDWKEFK---------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 97 ravRSDIQMIFQDplASLNPRMTIGEIIAEPLRtyHPKMSRQEVRERVK--AMMLKVGllpNLINRYPHEFSGGQCQRIG 174
Cdd:cd03299 70 ---KRDISYVPQN--YALFPHMTVYKNIAYGLK--KRKVDKKEIERKVLeiAEMLGID---HLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 175 IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYH 254
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
..
gi 15831001 255 NP 256
Cdd:cd03299 220 KP 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-256 |
6.87e-42 |
|
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: 145.27 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFeikDGkqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGM 91
Cdd:cd03219 1 LEVRGLTKRF---GG----------LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 KPDEwRA----VRSdiqmiFQDPlaSLNPRMTIGE--IIAEPLRTYHP------KMSRQEVRERVKAMMLKVGLLPnLIN 159
Cdd:cd03219 68 PPHE-IArlgiGRT-----FQIP--RLFPELTVLEnvMVAAQARTGSGlllaraRREEREARERAEELLERVGLAD-LAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 160 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:cd03219 139 RPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLD 217
|
250
....*....|....*..
gi 15831001 240 LGHAVELGTYDEVYHNP 256
Cdd:cd03219 218 QGRVIAEGTPDEVRNNP 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-256 |
2.86e-41 |
|
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: 144.90 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNpR 117
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAeplrtYHPK---MSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:TIGR04521 98 ETVYKDIA-----FGPKnlgLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 195 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
39-252 |
3.30e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkpdewRAVRSDI----QMifqdplASL 114
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRARRRIgyvpQR------AEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPR--MTIGEIIAEPLRTYHP--KMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:COG1121 87 DWDfpITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMyLGHAVELGTYDEV 252
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEV 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
38-256 |
8.08e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 144.85 E-value: 8.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavRS---DIQMIfqdplaSL 114
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR--RRigyVIQQI------GL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEIIAeplrTYhPKM---SRQEVRERVKAMMLKVGLLPN-LINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:COG1125 88 FPHMTVAENIA----TV-PRLlgwDKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-253 |
2.24e-40 |
|
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: 141.67 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeiKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLG 90
Cdd:TIGR02315 1 MLEVENLSKVY--PNGKQ----------ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 MKPDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRTYHP-------KMSRQEvRERVKAMMLKVGLLpNLINRYPH 163
Cdd:TIGR02315 69 LRGKKLRKLRRRIGMIFQH--YNLIERLTVLENVLHGRLGYKPtwrsllgRFSEED-KERALSALERVGLA-DKAYQRAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 164 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 243
Cdd:TIGR02315 145 QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
250
....*....|
gi 15831001 244 VELGTYDEVY 253
Cdd:TIGR02315 225 VFDGAPSELD 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
41-256 |
7.96e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 140.23 E-value: 7.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwRAVRSDIQMIFQDplASLNPRMTI 120
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQEAGMVFQQ--FYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 GEIIA-EPLRTYhpKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:PRK09493 95 LENVMfGPLRVR--GASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 200 QAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK09493 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
40-267 |
8.53e-40 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 140.61 E-value: 8.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL----VKATDGHVAWLGKELLgmkPDEWRAVRsdIQMIFQDPLASLN 115
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA---PCALRGRK--IATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PRMTIGEIIAEPLRTyhpkMSRQEVRERVKAMMLKVGL--LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:PRK10418 94 PLHTMHTHARETCLA----LGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 194 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSA 267
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-252 |
1.31e-39 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 148.06 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrSDIQMIFQDPla 112
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR---RQIGVVLQDV-- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 slnprmtigEI----IAEPLRTYHPKMSRQEVRERVKAmmlkVGLLPnLINRYPH-----------EFSGGQCQRIGIAR 177
Cdd:COG2274 559 ---------FLfsgtIRENITLGDPDATDEEIIEAARL----AGLHD-FIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 252
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
39-268 |
1.59e-39 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 139.55 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewravRSDIQMIFQDplASLNPRM 118
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR-----DRKIGFVFQH--YALFKHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYhpKMSRQEVRERVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:TIGR00968 88 TVRDNIAFGLEIR--KHPKAKIKARVEEL-LELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAV 268
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-252 |
4.93e-39 |
|
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: 138.07 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeikdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLg 90
Cdd:COG4555 1 MIEVENLSKKY-------------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 mkpDEWRAVRSDIQMIFQDPlaSLNPRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQC 170
Cdd:COG4555 67 ---KEPREARRQIGVLPDER--GLYDRLTVRENIRYFAELY--GLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 250
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
..
gi 15831001 251 EV 252
Cdd:COG4555 218 EL 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
42-256 |
1.22e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 137.62 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELLGMKPD--------EWRAV---RSDIQMIFQdp 110
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEI-RVGGEEIRLKPDrdgelvpaDRRQLqriRTRLGMVFQ-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 laSLN--PRMTIGE-IIAEPLRTYhpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 187
Cdd:COG4598 103 --SFNlwSHMTVLEnVIEAPVHVL--GRPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 188 CDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG4598 178 FDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
39-255 |
2.28e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 143.36 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAvrsDIQMIFQDP-LaslnPR 117
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR---QIAWVPQNPyL----FA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTigeiIAEPLRTYHPKMSRQEVRERVKAmmlkVGLLpNLINRYPHEF-----------SGGQCQRIGIARALILEPKLI 186
Cdd:COG4988 425 GT----IRENLRLGRPDASDEELEAALEA----AGLD-EFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
55-270 |
2.88e-38 |
|
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: 138.40 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 55 VVGESGCGKSTFARAIIGLVKATDGHVAwLGKELLGMKPDEWRAvrsdIQMIFQDplASLNPRMTIGEIIAEPLRTyhPK 134
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM-LDGEDVTNVPPHLRH----INMVFQS--YALFPHMTVEENVAFGLKM--RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 135 MSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREM 214
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 215 GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVPI 270
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-242 |
4.50e-38 |
|
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: 133.29 E-value: 4.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFeikdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgm 91
Cdd:cd03230 1 IEVRNLSKRY-------------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 kPDEWRAVRSDIQMIFQDPlaSLNPRMTIGEIIaeplrtyhpkmsrqevrervkammlkvgllpnlinryphEFSGGQCQ 171
Cdd:cd03230 65 -KKEPEEVKRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 172 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
39-256 |
6.67e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 135.74 E-value: 6.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwravRsDIQMIFQDplASLNPRM 118
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD----R-DIAMVFQN--YALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYhpKMSRQEVRERVK--AMMLKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:PRK11650 92 SVRENMAYGLKIR--GMPKAEIEERVAeaARILELE---PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 197 VSIQAQVVNLLQQLQREMGLSLIFIAHD------LAvvkhisDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK11650 167 AKLRVQMRLEIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
33-238 |
8.33e-37 |
|
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: 130.20 E-value: 8.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVrsdIQMIFQDP-L 111
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN---IAYVPQDPfL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 112 ASlnprMTIGEiiaeplrtyhpkmsrqevrervkammlkvgllpNLinrypheFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:cd03228 88 FS----GTIRE---------------------------------NI-------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVM 238
Cdd:cd03228 124 TSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVL 167
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-262 |
8.55e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 135.73 E-value: 8.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeikDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLG 90
Cdd:PRK11607 19 LLEIRNLTKSF---DGQH----------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 MKPdewraVRSDIQMIFQDplASLNPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQC 170
Cdd:PRK11607 86 VPP-----YQRPINMMFQS--YALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSI----QAQVVNLLQQLqremGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 246
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250
....*....|....*.
gi 15831001 247 GTYDEVYHnplHPYTR 262
Cdd:PRK11607 232 GEPEEIYE---HPTTR 244
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
38-242 |
1.09e-36 |
|
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: 129.29 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrSDIQMIFQdplaslnpr 117
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---RRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 mtigeiiaeplrtyhpkmsrqevrervkammlkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831001 198 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
49-238 |
1.23e-36 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 131.26 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 49 EGETLGVVGESGCGKSTFARAIIGLVKATDGHVA-----WLGKELLGMKPDEWRAvrsdIQMIFQDplASLNPRMTIGEI 123
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLFDSRKKINLPPQQRK----IGLVFQQ--YALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 124 IAEPLRTYHPKMSRQEVRERVKAMMLKvgllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 203
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELLDLLGLD-----HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 15831001 204 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-263 |
1.45e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 132.08 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 1 MNAVTEGRKVLLEIADLKVHFeikDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAI------IGLV 74
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYY---GDKQ----------ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 75 KATdGHVAWLGKELL--GMKPDEwraVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTYHPKmSRQEVRERVKAMMLKV 151
Cdd:COG1117 68 RVE-GEILLDGEDIYdpDVDVVE---LRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIK-SKSELDEIVEESLRKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 152 GL-------LpnliNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHD 224
Cdd:COG1117 139 ALwdevkdrL----KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 15831001 225 LAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRA 263
Cdd:COG1117 213 MQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
42-266 |
2.52e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.63 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAI-----------------IGLVKATDGHVAWLGKELLgmkpdewRAVRSDIQ 104
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsivvngqtINLVRDKDGQLKVADKNQL-------RLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 105 MIFQDplASLNPRMTIGEIIAE-PLRTYhpKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEP 183
Cdd:PRK10619 96 MVFQH--FNLWSHMTVLENVMEaPIQVL--GLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRA 263
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
...
gi 15831001 264 LMS 266
Cdd:PRK10619 251 FLK 253
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
43-250 |
5.17e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 5.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL-LGMKPDE--WRAVRSDIQMIFQDplASLNPRMT 119
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKTPSDkaIRELRRNVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGE-IIAEPLRTYhpKMSRQEVRERVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK11124 99 VQQnLIEAPCRVL--GLSKDQALARAEKL-LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831001 199 IQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 250
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
40-256 |
5.57e-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: 133.20 E-value: 5.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA--TDGHVAWLGKELLGMKPDewravRSDIQMIFQDplASLNPR 117
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPH-----KRGLALLFQN--YALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYhpKMSRQEVRERVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:TIGR03258 94 LKVEDNVAFGLRAQ--KMPKADIAERV-ADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 198 SIQAQVVNLLQQLQREM-GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:TIGR03258 171 NIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-238 |
8.60e-36 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 128.81 E-value: 8.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkELLGMKPdewRAVRSDIQMIFQDPLASLNPRM 118
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----RVFGKPL---EKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPlRTYHPKMSR---QEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:cd03235 86 SVRDVVLMG-LYGHKGLFRrlsKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15831001 196 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-238 |
1.97e-35 |
|
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: 128.32 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAwlgkellg 90
Cdd:COG4778 4 LLEVENLSKTFTLHL------QGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 mkpdewraVRSDIQMIfqDpLASLNPRM-------TIG---------------EIIAEPLRtyHPKMSRQEVRERVKAMM 148
Cdd:COG4778 70 --------VRHDGGWV--D-LAQASPREilalrrrTIGyvsqflrviprvsalDVVAEPLL--ERGVDREEARARARELL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 149 LKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVV 228
Cdd:COG4778 137 ARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVR 215
|
250
....*....|
gi 15831001 229 KHISDRVLVM 238
Cdd:COG4778 216 EAVADRVVDV 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
40-256 |
4.42e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.61 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGmkpdewRAVRS-DIQMIFQDplASLNPRM 118
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQrDICMVFQS--YALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAeplrtYHPKM---SRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:PRK11432 94 SLGENVG-----YGLKMlgvPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-253 |
5.63e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkELLGMKPDE---WRaVRSDIQMIFQdplaslN 115
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----TVGGMVLSEetvWD-VRRQVGMVFQ------N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PR-----MTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:PRK13635 90 PDnqfvgATVQDDVAFGLENI--GVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY 253
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-238 |
5.97e-35 |
|
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: 126.75 E-value: 5.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLas 113
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFR-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEIIAEPLR-TYHPkmsRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:cd03292 89 LLPDRNVYENVAFALEvTGVP---PREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15831001 193 SALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
43-248 |
6.76e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.44 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL-LGMKPDE--WRAVRSDIQMIFQDplASLNPRMT 119
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdFSQKPSEkaIRLLRQKVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGE-IIAEPLRTYhpKMSRQEVRERvkAMMLKVGL-LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:COG4161 99 VMEnLIEAPCKVL--GLSKEQAREK--AMKLLARLrLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 198 SIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 248
Cdd:COG4161 175 EITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
28-245 |
1.12e-34 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 126.39 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 28 QWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSD-IQMI 106
Cdd:COG4181 16 KTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARhVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 107 FQdplaS--LNPRMTIGEIIAEPLrtyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK 184
Cdd:COG4181 96 FQ----SfqLLPTLTALENVMLPL----ELAGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 185 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 245
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
50-267 |
7.83e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.10 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwRAVrsdiQMIFQDplASLNPRMTIGEIIAEPLr 129
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RPV----SMLFQE--NNLFPHLTVAQNIGLGL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 130 tyHP--KMSRQEvRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 207
Cdd:COG3840 97 --RPglKLTAEQ-RAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 208 QQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSA 267
Cdd:COG3840 173 DELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
242-330 |
1.27e-33 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 119.00 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 242 HAVELGTYDEVYHNPLHPYTRALMSAVPIP-DPDlEKNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL-E 319
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRD-RKLISI---PGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALvE 76
|
90
....*....|.
gi 15831001 320 GSFRHAVSCLK 330
Cdd:TIGR01727 77 IAEGHRVACHL 87
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
40-247 |
1.27e-33 |
|
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: 122.16 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrsdiqmifqdplaslnprmt 119
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 igEIIAeplrtYHPkmsrQevrervkaMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:cd03214 73 --RKIA-----YVP----Q--------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15831001 200 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
42-266 |
2.05e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.71 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKP-----DEWRAVRSDIQMIFQDplASLNP 116
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkGLIRQLRQHVGFVFQN--FNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGE-IIAEPLRTyhPKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:PRK11264 99 HRTVLEnIIEGPVIV--KGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 196 DVSIQAQVVNLLQQLQREMgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMS 266
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
39-270 |
2.78e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 127.07 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVR-SDIQMIFQDplASLNPR 117
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:PRK10070 121 MTVLDNTAFGMEL--AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 198 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVPI 270
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
38-256 |
5.39e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.20 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrsdIQMIFQDplASLNPR 117
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-----VGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTY--HPKMSRQEVRERVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:PRK10851 89 MTVFDNIAFGLTVLprRERPNAAAIKAKV-TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
38-244 |
6.02e-33 |
|
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: 119.84 E-value: 6.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQdplaslnpr 117
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARRAGIAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 mtigeiiaeplrtyhpkmsrqevrervkammlkvgllpnlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831001 198 SIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 244
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
30-255 |
8.59e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.41 E-value: 8.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQD 109
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 P----LASlnprmTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKL 185
Cdd:PRK13632 92 PdnqfIGA-----TVEDDIAFGLE--NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL-AVVKhiSDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-255 |
8.66e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.85 E-value: 8.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGmKPDEWRAVRSDIQMIFQDPLASLNPR 117
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 mTIGEIIAeplrtYHPK---MSRQEVRERVKAMMLKVGL-LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:PRK13637 100 -TIEKDIA-----FGPInlgLSEEEIENRVKRAMNIVGLdYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 194 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
40-252 |
1.71e-32 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 120.65 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewRAVrsdiqmIFQDplASLNPRMT 119
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMV------VFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831001 200 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-238 |
4.47e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 4.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPlaSLNPR 117
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD--AQAAGIAIIHQEL--NLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIA---EPLRtyHPKMSRQEVRERVKAMMLKVGL-LPnlinryPH----EFSGGQCQRIGIARALILEPKLIICD 189
Cdd:COG1129 94 LSVAENIFlgrEPRR--GGLIDWRAMRRRARELLARLGLdID------PDtpvgDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 190 EPVSALDvsiQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:COG1129 166 EPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-261 |
7.32e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.56 E-value: 7.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATDGHVAWLGKELLGMKPDEWRaVRSDIQMIFQDPlaSL 114
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYP--NP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 261
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-251 |
7.66e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.28 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrSDIQMIFQDP-LASlnp 116
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR---RQIGVVPQDTfLFS--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 rMTIGEIIAeplrtY-HPKMSRQEVRERVKAMMLKvgllpNLINRYPH-----------EFSGGQCQRIGIARALILEPK 184
Cdd:COG1132 428 -GTIRENIR-----YgRPDATDEEVEEAAKAAQAH-----EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 185 LIICDEPVSALDVSIQAQVvnlLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 251
Cdd:COG1132 497 ILILDEATSALDTETEALI---QEALERLMkGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
11-238 |
1.41e-31 |
|
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: 118.26 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHV------AWL 84
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQ------QGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRIlvrhegAWV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 85 gkELLGMKPDEWRAVR-SDIQMIFQdpLASLNPRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPNLINRYPH 163
Cdd:TIGR02324 75 --DLAQASPREVLEVRrKTIGYVSQ--FLRVIPRVSALEVVAEPLLER--GVPREAARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 164 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
43-256 |
1.44e-31 |
|
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: 121.36 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAV-RSDIQMIFQDplASLNPRMTIg 121
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQE--ARLFPHLSV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 122 eiiAEPLRtY----HPKMSRQEVRERVKAMMlkvGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:COG4148 95 ---RGNLL-YgrkrAPRAERRISFDEVVELL---GIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 198 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
38-242 |
3.97e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.90 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNpr 117
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:PRK10908 94 RTVYDNVAIPLII--AGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831001 198 SIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK10908 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
43-260 |
4.65e-31 |
|
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: 119.83 E-value: 4.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMK-----PDEWRAvrsdIQMIFQDplASLNPR 117
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflPPEKRR----IGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYHPKmSRQEVRERVKAMMlkvGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPS-ERRISFERVIELL---GIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 198 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 260
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-248 |
4.89e-31 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 117.09 E-value: 4.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLkvHFEIkDGKQwfwqppkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDGHVAWLGKELL 89
Cdd:COG0396 1 LEIKNL--HVSV-EGKE-------ILK---GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 90 GMKPDEwRAvRSDIQMIFQDPLaslnprmtigEI----IAEPLRT-----YHPKMSRQEVRERVKAMMLKVGLLPNLINR 160
Cdd:COG0396 68 ELSPDE-RA-RAGIFLAFQYPV----------EIpgvsVSNFLRTalnarRGEELSAREFLKLLKEKMKELGLDEDFLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 161 YPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDV---SIQAQVVNLLqqlqREMGLSLIFIAHDLAVVKHIS-DRV 235
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYIKpDFV 211
|
250
....*....|...
gi 15831001 236 LVMYLGHAVELGT 248
Cdd:COG0396 212 HVLVDGRIVKSGG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-252 |
6.19e-31 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 122.22 E-value: 6.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHV-AWLGKELLGM---KPDEWRAVRSDIQMIFQDplA 112
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMtkpGPDGRGRAKRYIGILHQE--Y 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIGEIIAEPLRTYHPKmsrqEVRERVKAMMLK-VGL----LPNLINRYPHEFSGGQCQRIGIARALILEPKLII 187
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPD----ELARMKAVITLKmVGFdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 188 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-253 |
6.20e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.96 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEW-RAVRSDIQMIFQDPLA 112
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIGEIIAEPlrtYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:PRK13646 97 QLFEDTVEREIIFGP---KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 193 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 253
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
33-266 |
9.03e-31 |
|
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: 121.80 E-value: 9.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVrsdIQMIFQDP-- 110
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQRPhl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 -LASlnprmtigeiIAEPLRTYHPKMSRQEVRervkAMMLKVGLLPnLINRYPH-----------EFSGGQCQRIGIARA 178
Cdd:COG4987 421 fDTT----------LRENLRLARPDATDEELW----AALERVGLGD-WLAALPDgldtwlgeggrRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 179 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHNplH 258
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQ--N 560
|
....*...
gi 15831001 259 PYTRALMS 266
Cdd:COG4987 561 GRYRQLYQ 568
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
39-255 |
9.89e-31 |
|
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: 115.61 E-value: 9.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPlaSLNPRM 118
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE--RARAGIGYVPEGR--RIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TigeiIAEPLRTYHPKMSRQEVRERVKAMmlkVGLLPNLINRYPH---EFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:cd03224 91 T----VEENLLLGAYARRRAKRKARLERV---YELFPRLKERRKQlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 196 DVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:cd03224 164 APKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
40-226 |
2.02e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.50 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA---TDGHVaWLGKELLGMKPDEWRAvrsdIQMIFQDPLasLNP 116
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV-LLNGRRLTALPAEQRR----IGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEPLRtyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:COG4136 90 HLSVGENLAFALP---PTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190
....*....|....*....|....*....|
gi 15831001 197 VSIQAQVVNLLQQLQREMGLSLIFIAHDLA 226
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-238 |
4.87e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.96 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGm 91
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQ---------PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 kPDEWRAVrsdiqmIFQDplASLNPRMTIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQ 171
Cdd:COG4525 74 -PGADRGV------VFQK--DALLPWLNVLDNVAFGLRL--RGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 172 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVVkhISDRVLVM 238
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVM 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-261 |
5.39e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.62 E-value: 5.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFeikdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATDGHVAWLGK 86
Cdd:PRK14247 4 IEIRDLKVSF-------------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDEwraVRSDIQMIFQDPlaSLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRY---PH 163
Cdd:PRK14247 71 DIFKMDVIE---LRRRVQMVFQIP--NPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 164 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHA 243
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*...
gi 15831001 244 VELGTYDEVYHNPLHPYT 261
Cdd:PRK14247 224 VEWGPTREVFTNPRHELT 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
49-256 |
8.13e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.12 E-value: 8.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 49 EGETLGVVGESGCGKSTFARAIIGLVKATDGHVAwLGKELL--GMKPDEWRAVRSDIQMIFQDPLASLNPRmTIGEIIAe 126
Cdd:PRK13634 32 SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVItaGKKNKKLKPLRKKVGIVFQFPEHQLFEE-TVEKDIC- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 127 plrtYHPK---MSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 203
Cdd:PRK13634 109 ----FGPMnfgVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831001 204 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13634 185 MEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
39-251 |
8.25e-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: 113.23 E-value: 8.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLgmkpDEWRAVRSDIQMIFQDPlaSLNPRM 118
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDL--SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:cd03265 89 TGWENLYIHARLY--GVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 251
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-261 |
1.20e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 113.99 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVK------ATDGHVAWLGKELLGMKPDEwraVRSDIQMIFQDPlaSLNP 116
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIK---LRKEVGMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEPLRTYHPKMSRqEVRERVKAMMLKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKR-EIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 194 ALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 261
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
40-252 |
1.32e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.71 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEW---RAV-RSDIQMIFqdPLasln 115
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAVlPQHSSLSF--PF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 prmTIGEIIA---EPLRTyhpkmSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALI------LEPKLI 186
Cdd:PRK13548 92 ---TVEEVVAmgrAPHGL-----SRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-250 |
2.42e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.44 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPlaSLNP 116
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD--AIALGIGMVHQHF--MLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGE-II--AEPLRtyHPKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:COG3845 94 NLTVAEnIVlgLEPTK--GGRLDRKAARARIRELSERYGLDVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 194 ALDvsiQAQVVNLLQQLQR--EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVelGTYD 250
Cdd:COG3845 171 VLT---PQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV--GTVD 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
39-253 |
2.92e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkeLLGMKPDEWRA-----VRSDIQMIFQDPLAS 113
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI------LFDGKPIDYSRkglmkLRESVGMVFQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEIIAEPLRTYHPKmsrQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:PRK13636 95 LFSASVYQDVSFGAVNLKLPE---DEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 194 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 253
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
34-256 |
3.59e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDeWRAVRSDIQMIFQDPLAS 113
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS-LLEVRKTVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 L-NPrmTIGEIIA-EPLRTyhpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK13639 91 LfAP--TVEEDVAfGPLNL---GLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
39-255 |
6.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKpDEWRaVRSDIQMIFQdplaslNPRM 118
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWD-IRNKAGMVFQ------NPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYHPK---MSRQEVRERVKAMMLKVGLLPnlINRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:PRK13633 97 QIVATIVEEDVAFGPEnlgIPPEEIRERVDESLKKVGMYE--YRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 195 LDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAVVkhiSDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHymEEAVE---ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
40-238 |
6.78e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.52 E-value: 6.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQDPLASLnPRMT 119
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVFQNPDNQF-VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:PRK13650 99 VEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831001 200 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVLVM 238
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVM 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-262 |
1.08e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 111.67 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 36 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIiGLVKATDGHVAWLGK-ELLGMKPDEWRA----VRSDIQMIFQDP 110
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRvEFFNQNIYERRVnlnrLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 laSLNPrMTIGEIIAEPLRT--YHPKMsrqEVRERVKAMMLKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKL 185
Cdd:PRK14258 98 --NLFP-MSVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLwdeIKHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY-----LGHAVELGTYDEVYHNPLHPY 260
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSR 251
|
..
gi 15831001 261 TR 262
Cdd:PRK14258 252 TR 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-238 |
1.46e-28 |
|
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: 109.65 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 18 KVHFEIKDGKqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkeLLGMKPDEWR 97
Cdd:cd03226 4 NISFSYKKGT----------EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI------LLNGKPIKAK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 98 AVRSDIQMIFQDPLASLnprmtIGEIIAEPLRTYHPKMSrqEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIAR 177
Cdd:cd03226 68 ERRKSIGYVMQDVDYQL-----FTDSVREELLLGLKELD--AGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-256 |
1.65e-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: 110.07 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeikdGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLG 90
Cdd:COG0410 3 MLEVENLHAGY----GG---------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 MKPDewRAVRSDI------QMIFqdplaslnPRMTIGEIIAEPLRTYHPKMSRQEVRERVkammlkVGLLPNLinrypHE 164
Cdd:COG0410 70 LPPH--RIARLGIgyvpegRRIF--------PSLTVEENLLLGAYARRDRAEVRADLERV------YELFPRL-----KE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 165 F--------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL 236
Cdd:COG0410 129 RrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAY 207
|
250 260
....*....|....*....|
gi 15831001 237 VMYLGHAVELGTYDEVYHNP 256
Cdd:COG0410 208 VLERGRIVLEGTAAELLADP 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-252 |
4.00e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.58 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 36 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL-------LGMKPDEwRavrsdiqmifq 108
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrrIGYLPEE-R----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 dplaSLNPRMTIGEIIaeplrTYHPK---MSRQEVRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKL 185
Cdd:COG4152 81 ----GLYPKMKVGEQL-----VYLARlkgLSKAEAKRRADEWLERLG-LGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 186 IICDEPVSALD-VSiqaqvVNLLQQL---QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:COG4152 151 LILDEPFSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
39-252 |
5.53e-28 |
|
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: 108.73 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPdEWraVRSDIQMIFQDPLaslnprm 118
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AW--LRRQVGVVLQENV------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYHPKMSRQEVRERVK-----AMMLKvglLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICD 189
Cdd:cd03252 87 LFNRSIRDNIALADPGMSMERVIEAAKlagahDFISE---LPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 190 EPVSALDVSIQAqvvNLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 252
Cdd:cd03252 164 EATSALDYESEH---AIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
41-224 |
7.85e-28 |
|
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: 107.56 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlGMKPDEWRAvrsdiQMIFQDPLASLNPRMTI 120
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRR-----RLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 GEIiaepLRTYHPKMSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:COG4133 93 REN----LRFWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 15831001 201 AQVVNLLQQLQREmGLSLIFIAHD 224
Cdd:COG4133 168 ALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-256 |
1.88e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDE-WRAVRSDIQMIFQDPLA 112
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIGEIIAEPLRTyhpKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:PRK13641 97 QLFENTVLKDVEFGPKNF---GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 193 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
43-242 |
7.55e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.67 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRS-DIQMIFQdpLASLNPRMTIG 121
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 122 EIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 201
Cdd:PRK11629 106 ENVAMPLLI--GKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15831001 202 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISdRVLVMYLGH 242
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
43-256 |
7.67e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 108.58 E-value: 7.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELLGMKPDEWRAVrsdiQMIFQDplASLNPRMTIGE 122
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGV----GMVFQS--YALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIAEPLRTyhPKMSRQEVRERVK--AMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:PRK11000 95 NMSFGLKL--AGAKKEEINQRVNqvAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 201 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK11000 170 VQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
38-255 |
8.01e-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: 105.70 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrSDIQMIFQDP-LASlnp 116
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLR---SQIGLVSQEPvLFD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 rMTIGEIIAeplrtYHPKMSRQEVRERVKammlKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKL 185
Cdd:cd03249 91 -GTIAENIR-----YGKPDATDEEVEEAA----KKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE------VYHN 255
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDElmaqkgVYAK 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-256 |
8.14e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 106.23 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFeikdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLG 90
Cdd:PRK11300 5 LLSVSGLMMRF-------------GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 91 MkPDEWRAvRSDIQMIFQDplASLNPRMTIGE-------------IIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPnL 157
Cdd:PRK11300 72 L-PGHQIA-RMGVVRTFQH--VRLFREMTVIEnllvaqhqqlktgLFSGLLKTPAFRRAESEALDRAATWLERVGLLE-H 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 158 INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:PRK11300 147 ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYV 226
|
250
....*....|....*....
gi 15831001 238 MYLGHAVELGTYDEVYHNP 256
Cdd:PRK11300 227 VNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-284 |
1.08e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.63 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkatdghVAWLGKELLG--------MKPDEWRAVRSDIQM 105
Cdd:PRK13645 21 PFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIVGdyaipanlKKIKEVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 106 IFQDPLASLNPRMTIGEIIAEPLrtyHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKL 185
Cdd:PRK13645 95 VFQFPEYQLFQETIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNplhpytRALM 265
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELL 245
|
250 260
....*....|....*....|....*
gi 15831001 266 SAVPIPDPDLE------KNKTIQLL 284
Cdd:PRK13645 246 TKIEIDPPKLYqlmyklKNKGIDLL 270
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
50-247 |
1.19e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 104.50 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwRAVrsdiQMIFQDplASLNPRMTIGEIIAEPLr 129
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-RPV----SMLFQE--NNLFAHLTVEQNVGLGL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 130 tyHPKMS-RQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 208
Cdd:cd03298 96 --SPGLKlTAEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831001 209 QLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
37-242 |
2.06e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.14 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkeLLGMKPdeWRAVRSDIQMIFQDplASLNP 116
Cdd:PRK11247 28 LNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAP--LAEAREDTRLMFQD--ARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEPLRTYHpkmsRQEVRERVKAmmlkVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:PRK11247 95 WKKVIDNVGLGLKGQW----RDAALQALAA----VGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15831001 197 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
39-253 |
2.06e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWlgkELLGMKPDEWRAVRSDIQMIFQDPlaslnPRM 118
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEKLRKHIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIA-------EPLRTYHPKMSRqevreRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK13648 96 FVGSIVKydvafglENHAVPYDEMHR-----RVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY 253
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
39-252 |
2.15e-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: 104.53 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPdEWRAvRSDI------QMIFqdpla 112
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP-HERA-RAGIayvpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 slnPRMTIGEII---AEPLRTYHpkmsrQEVRERVKAMMlkvGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 189
Cdd:TIGR03410 88 ---PRLTVEENLltgLAALPRRS-----RKIPDEIYELF---PVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 190 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-242 |
3.49e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 102.51 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVHfeikdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL 88
Cdd:cd03215 2 EPVLEVRGLSVK-----------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 LGMKPDEwrAVRSDIQMIFQDPLAS-LNPRMTIGEiiaeplrtyhpkmsrqevrervkammlkvgllpNLINryPHEFSG 167
Cdd:cd03215 65 TRRSPRD--AIRAGIAYVPEDRKREgLVLDLSVAE---------------------------------NIAL--SSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 168 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
33-251 |
6.42e-26 |
|
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: 102.97 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLgmkpDEWRAVRSDIQMIFQDplA 112
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQSLGYCPQF--D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTigeiIAEPLRTYHP--KMSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:cd03263 85 ALFDELT----VREHLRFYARlkGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 251
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
31-288 |
1.03e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.02 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 31 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGmkPDEWRaVRSDIQMIFQDP 110
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA--ENVWN-LRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 laslnPRMTIGEIIAEPLR--TYHPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 188
Cdd:PRK13642 91 -----DNQFVGATVEDDVAfgMENQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 189 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLH--------PY 260
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDmveigldvPF 243
|
250 260 270
....*....|....*....|....*....|...
gi 15831001 261 TRALM-----SAVPIPDPDLEKNKTIQLLEGEL 288
Cdd:PRK13642 244 SSNLMkdlrkNGFDLPEKYLSEDELVELLADKL 276
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
38-247 |
1.20e-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: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGeTLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKpdewRAVRSDIQMIFQDPlaSLNPR 117
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP----QKLRRRIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:cd03264 87 FTVREFLDYIAWLK--GIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831001 198 SIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03264 164 EERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-242 |
1.96e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.97 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 44 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewravRSDIQMIFQDplASLNPRMTIGEI 123
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 124 IAEPLrtyHP--KMSRQEvRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 201
Cdd:PRK10771 92 IGLGL---NPglKLNAAQ-REKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15831001 202 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-261 |
2.80e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.16 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAI------IGLVKATdGHVAWL 84
Cdd:PRK14239 5 ILQVSDLSVYYNKK-------------KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlNPEVTIT-GSIVYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 85 GKELLGMKPDEWRaVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTYHPKmSRQEVRERVKAMMLKVGLLPNLINRYpH 163
Cdd:PRK14239 71 GHNIYSPRTDTVD-LRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIK-DKQVLDEAVEKSLKGASIWDEVKDRL-H 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 164 E----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:PRK14239 144 DsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|..
gi 15831001 240 LGHAVELGTYDEVYHNPLHPYT 261
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
30-247 |
3.34e-25 |
|
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: 100.91 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLgmkpDEWRAVRSDIQMIFQD 109
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 plASLNPRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICD 189
Cdd:cd03266 87 --TGLYDRLTARENLEYFAGLY--GLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 190 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
34-238 |
3.64e-25 |
|
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: 105.83 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAvrsdiqmifQDPLAS 113
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---------QIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEiIAEPLRTYHPKMSRQEVRE---RVKAMMLKVGL---LPNLINRYPHEFSGGQCQRIGIARALILEPKLII 187
Cdd:TIGR02857 403 QHPFLFAGT-IAENIRLARPDASDAEIREaleRAGLDEFVAALpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 188 CDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVkHISDRVLVM 238
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
40-238 |
4.60e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 99.21 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkellgmkpdewravrsdiqmifqdplaslnprmt 119
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-------------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 igEIIAEPLRTYHPKmsrqEVRERVKAMMLKVGLLPNLINRypHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:cd03246 60 --RLDGADISQWDPN----ELGDHVGYLPQDDELFSGSIAE--NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831001 200 QAQVVNLLQQLqREMGLSLIFIAHDLAVVKhISDRVLVM 238
Cdd:cd03246 132 ERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVL 168
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-252 |
5.46e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 100.76 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 19 VHFEIKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWra 98
Cdd:cd03254 8 VNFSYDEKKP----------VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 99 vRSDIQMIFQDPLasLNPRmTIGEIIaeplrtyhpKMSRQEVRERVKAMMLKVGLLPNLINRYP-----------HEFSG 167
Cdd:cd03254 76 -RSMIGVVLQDTF--LFSG-TIMENI---------RLGRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 168 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELG 247
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
....*
gi 15831001 248 TYDEV 252
Cdd:cd03254 220 THDEL 224
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
37-251 |
5.49e-25 |
|
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: 105.55 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVrsdIQMIFQDPLASLNP 116
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR---MALVPQDPVLFAAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMtigeiiaEPLRTYHPKMSRQEVRERVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDE 190
Cdd:TIGR02204 430 VM-------ENIRYGRPDATDEEVEAAARAAHAHefISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 191 PVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 251
Cdd:TIGR02204 503 ATSALD----AESEQLVQQaLETLMkGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAE 560
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-238 |
7.65e-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: 99.97 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwraVRSDIQMIFQD 109
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 PL---ASLNPRMTIGeiiaeplrtyHPKMSRQEVrerVKAMMLkVGLLPnLINRYPHEF-----------SGGQCQRIGI 175
Cdd:cd03245 87 VTlfyGTLRDNITLG----------APLADDERI---LRAAEL-AGVTD-FVNKHPNGLdlqigergrglSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 176 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVM 238
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVM 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-252 |
8.22e-25 |
|
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: 104.83 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHV--------AWlGKELLGmkpdewravr 100
Cdd:COG4618 337 TVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQW-DREELG---------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 101 sdiQMIF---QDPlaSLNPRmTIGEIIAeplRtyHPKMSRQEVRE-----RVKAMMLKvglLPN----LINRYPHEFSGG 168
Cdd:COG4618 406 ---RHIGylpQDV--ELFDG-TIAENIA---R--FGDADPEKVVAaaklaGVHEMILR---LPDgydtRIGEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 169 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT 248
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGP 549
|
....
gi 15831001 249 YDEV 252
Cdd:COG4618 550 RDEV 553
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
35-247 |
1.43e-24 |
|
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: 98.89 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGK-------ELLGMKPDEwRAvrsdiqmif 107
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarNRIGYLPEE-RG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 108 qdplasLNPRMTIGEI---IAEpLRtyhpKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPK 184
Cdd:cd03269 81 ------LYPKMKVIDQlvyLAQ-LK----GLKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 185 LIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
39-225 |
1.50e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGmkPDEWRAVrsdiqmIFQDplASLNPRM 118
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERGV------VFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTyhPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK11248 86 NVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*..
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDL 225
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-251 |
2.29e-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: 99.23 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 19 VHFEIKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewrA 98
Cdd:cd03253 6 VTFAYDPGRP----------VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLD---S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 99 VRSDIQMIFQD-PLasLNPrmTIGEIIAeplrtY-HPKMSRQEVRERVKAMMLKvgllpNLINRYPHEF----------- 165
Cdd:cd03253 73 LRRAIGVVPQDtVL--FND--TIGYNIR-----YgRPDATDEEVIEAAKAAQIH-----DKIMRFPDGYdtivgerglkl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 166 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 245
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
....*.
gi 15831001 246 LGTYDE 251
Cdd:cd03253 216 RGTHEE 221
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
244-311 |
4.45e-24 |
|
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: 93.23 E-value: 4.45e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 244 VELGTYDEVYHNPLHPYTRALMSAVPIPDPdleKNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPEC 311
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP---PKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
34-252 |
4.46e-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: 102.90 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDeWraVRSDIQMIFQDPLas 113
Cdd:TIGR01846 467 PDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA-W--LRRQMGVVLQENV-- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMtigeiIAEPLRTYHPKMSRQEVRERVKAmmlkVGLLpNLINRYPHEF-----------SGGQCQRIGIARALILE 182
Cdd:TIGR01846 542 LFSRS-----IRDNIALCNPGAPFEHVIHAAKL----AGAH-DFISELPQGYntevgekganlSGGQRQRIAIARALVGN 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 183 PKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-253 |
8.21e-24 |
|
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: 97.69 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 29 WFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwraVRSDIQMIFQ 108
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 DPLaslnprmTIGEIIAEPLRTYHPKMSRQEVRERVKAmmlkvGLLPNLINRYPHEF-----------SGGQCQRIGIAR 177
Cdd:cd03251 84 DVF-------LFNDTVAENIAYGRPGATREEVEEAARA-----ANAHEFIMELPEGYdtvigergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY 253
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-244 |
8.53e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMkPDEWRAvrSDIQMIFQDPLASLNPR 117
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRA--KYIGRVFQDPMMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGE--IIAE------PLRTYHPKMSRQEVRERVKAMML--------KVGLLpnlinryphefSGGQCQRIGIARALIL 181
Cdd:COG1101 97 MTIEEnlALAYrrgkrrGLRRGLTKKRRELFRELLATLGLglenrldtKVGLL-----------SGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 182 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL--AVvkHISDRVLVMYLGHAV 244
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-247 |
1.05e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 96.44 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVhfEIKDGKqwfwqppkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDGHVAWLGKELL 89
Cdd:cd03217 1 LEIKDLHV--SVGGKE--------ILK---GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 90 GMKPDEwRAvRSDIQMIFQDPlaslnPRMTiGEIIAEPLRTyhpkmsrqevrervkammLKVGllpnlinrypheFSGGQ 169
Cdd:cd03217 68 DLPPEE-RA-RLGIFLAFQYP-----PEIP-GVKNADFLRY------------------VNEG------------FSGGE 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 170 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHI-SDRVLVMYLGHAVELG 247
Cdd:cd03217 110 KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
30-256 |
1.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLgkELLGMKPDE---WRaVRSDIQMI 106
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKI--TVDGITLTAktvWD-IREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 107 FQDPLASLnPRMTIGEIIAEPLRtyHPKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLI 186
Cdd:PRK13640 90 FQNPDNQF-VGATVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-256 |
1.22e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 10 VLLEIADLKVHFeikDGKQwfwqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELL 89
Cdd:PRK13631 20 IILRVKNLYCVF---DEKQ-----ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 90 GMKPDEWRAV--------------RSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyhpKMSRQEVRERVKAMMLKVGLLP 155
Cdd:PRK13631 91 GDKKNNHELItnpyskkiknfkelRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAL---GVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 156 NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRV 235
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEV 246
|
250 260
....*....|....*....|.
gi 15831001 236 LVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQ 267
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
33-264 |
1.60e-23 |
|
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: 100.95 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRA----VRSDIqMIFQ 108
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRqvalVSQDV-VLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 DplaslnprmTIGEIIA-EPLRTYhpkmSRQEVRERVKAMMLKvgllpNLINRYPHEF-----------SGGQCQRIGIA 176
Cdd:TIGR02203 420 D---------TIANNIAyGRTEQA----DRAEIERALAAAYAQ-----DFVDKLPLGLdtpigengvllSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 177 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVY-HN 255
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLaRN 558
|
....*....
gi 15831001 256 PLHPYTRAL 264
Cdd:TIGR02203 559 GLYAQLHNM 567
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-247 |
2.21e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLkvHFEIKDGKqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgm 91
Cdd:PRK13647 5 IEVEDL--HFRYKDGT----------KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 KPDEWRAVRSDIQMIFQDPLASLNPrMTIGEIIA-EPLRTyhpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQC 170
Cdd:PRK13647 70 NAENEKWVRSKVGLVFQDPDDQVFS-STVWDDVAfGPVNM---GLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
42-224 |
3.20e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.00 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRS-DIQMIFQDPLasLNPRMTI 120
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkHVGFVFQSFM--LIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 GEIIAEP--LRtyhpKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK10584 106 LENVELPalLR----GESSRQSRNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHD 224
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
34-256 |
6.25e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawLGKELLGMKPDEWRAVRSDIQMIFQDPLAS 113
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV--LVSGIDTGDFSKLQGIRKLVGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LnprmtIGEIIAEPLrTYHPK---MSRQEVRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:PRK13644 90 F-----VGRTVEEDL-AFGPEnlcLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVkHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
34-250 |
6.81e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.69 E-value: 6.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGK-ELLGMKPDEW---------------- 96
Cdd:PRK13651 17 PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKdEKNKKKTKEKekvleklviqktrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 97 ----RAVRSDIQMIFQDPLASLNpRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQR 172
Cdd:PRK13651 97 ikkiKEIRRRVGVVFQFAEYQLF-EQTIEKDIIFGPVSM--GVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 173 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG-TYD 250
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGdTYD 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-244 |
1.02e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVHfeikdgkqwfwqPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL 88
Cdd:COG3845 255 EVVLEVENLSVR------------DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 LGMKPDEWRavRSDIQMIFQDPLAS-LNPRMTIGEIIAepLRTYHPK-------MSRQEVRERVKAMM-----------L 149
Cdd:COG3845 323 TGLSPRERR--RLGVAYIPEDRLGRgLVPDMSVAENLI--LGRYRRPpfsrggfLDRKAIRAFAEELIeefdvrtpgpdT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 150 KVGLLpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK 229
Cdd:COG3845 399 PARSL-----------SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEIL 466
|
250
....*....|....*
gi 15831001 230 HISDRVLVMYLGHAV 244
Cdd:COG3845 467 ALSDRIAVMYEGRIV 481
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
45-247 |
1.03e-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: 94.16 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 45 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPdewraVRSDIQMIFQDplASLNPRMTIGEII 124
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP-----YQRPVSMLFQE--NNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 125 AEPLrtyHPKMSRQEV-RERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 203
Cdd:TIGR01277 92 GLGL---HPGLKLNAEqQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15831001 204 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-251 |
1.29e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.49 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTfarAIIGLVKATD---GHVAWLGKELLGMKpdeWRAVRSDIQMIFQDPLasLN 115
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKST---LINLLQRVFDpqsGRILIDGTDIRTVT---RASLRRNIAVVFQDAG--LF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PRMtigeiIAEPLRTYHPKMSRQEVR---ERVKAMmlkvgllpNLINRYPHEF-----------SGGQCQRIGIARALIL 181
Cdd:PRK13657 422 NRS-----IEDNIRVGRPDATDEEMRaaaERAQAH--------DFIERKPDGYdtvvgergrqlSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 182 EPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 251
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-254 |
1.69e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 29 WFWQP--PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAwLGKELLGM--KPDEWRAVRSDIQ 104
Cdd:PRK13643 9 YTYQPnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSStsKQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 105 MIFQDPLASLNPRMTIGEIIAEPlrtYHPKMSRQEVrERVKAMMLK-VGLLPNLINRYPHEFSGGQCQRIGIARALILEP 183
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAFGP---QNFGIPKEKA-EKIAAEKLEmVGLADEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYH 254
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-253 |
2.10e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 29 WF-WQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDeWRAVRSDIQMIF 107
Cdd:PRK13638 8 WFrYQDEPVLK---GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRG-LLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 108 QDPLASLNpRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGllpnlINRYPHE----FSGGQCQRIGIARALILEP 183
Cdd:PRK13638 84 QDPEQQIF-YTDIDSDIAFSLRNL--GVPEAEITRRVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 253
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
38-252 |
2.54e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.89 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQDPLaslnpr 117
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL---KDIDRHTLRQFINYLPQEPY------ 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGllpnlINRYPHEF-----------SGGQCQRIGIARALILEPKLI 186
Cdd:TIGR01193 559 IFSGSILENLLLGAKENVSQDEIWAACEIAEIKDD-----IENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
33-252 |
3.24e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 97.24 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwraVRSDIQMIFQDP-- 110
Cdd:TIGR03375 474 PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD---LRRNIGYVPQDPrl 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 -LASLNPRMTIGEiiaeplrtyhPKMSRQEVRERVKAmmlkVGLLpNLINRYPHEF-----------SGGQCQRIGIARA 178
Cdd:TIGR03375 551 fYGTLRDNIALGA----------PYADDEEILRAAEL----AGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 179 LILEPKLIICDEPVSALDVSIQAQvvnLLQQLQREM-GLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEER---FKDRLKRWLaGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQV 686
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
36-244 |
5.49e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 36 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSD-IQMIFQDplASL 114
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQR--YHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEIIAEPlrTYHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:PRK10535 98 LSHLTAAQNVEVP--AVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831001 195 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAV 244
Cdd:PRK10535 175 LDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
41-271 |
8.13e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDplASLNPRMTI 120
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 GEIIAEPLRTyHPKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:PRK11831 102 FDNVAYPLRE-HTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 201 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPlHPYTRALMSAV---PIP 271
Cdd:PRK11831 180 GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGIadgPVP 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-237 |
8.89e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.77 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGHVAWLGKELL--GMKPDEwravRSDIQMIFQDpLAs 113
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQasNIRDTE----RAGIAIIHQE-LA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEII---AEPlrTYHPKMSRQEVRERVKAMMLKVGLLPNlINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:PRK13549 93 LVKELSVLENIflgNEI--TPGGIMDYDAMYLRAQKLLAQLKLDIN-PATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICV 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-256 |
1.19e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQDPLASLNPR 117
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPLRTyhpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:PRK13652 95 TVEQDIAFGPINL---GLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 198 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-261 |
2.38e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHvAWLGKELLGMKPD-EWRAV---RSDIQMIFQDPlaslN 115
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIfNYRDVlefRRRVGMLFQRP----N 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 P-RMTIGEIIAEPLRTyHPKMSRQEVRERVKAMMLKVGLLPNLINRY---PHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK14271 112 PfPMSIMDNVLAGVRA-HKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 261
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
39-238 |
2.97e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETL----------G----VVGESGCGKSTFARAIIGLVKATDGHVAwlgkellgmKPDEWRavrsdiq 104
Cdd:COG4178 364 ALEDLTLRTPDGRPLledlslslkpGerllITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAGAR------- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 105 MIF--QDPlaslnpRMTIGeiiaePLR---TYhPKMSRQEVRERVKAMMLKVGLlPNLINRY------PHEFSGGQCQRI 173
Cdd:COG4178 428 VLFlpQRP------YLPLG-----TLRealLY-PATAEAFSDAELREALEAVGL-GHLAERLdeeadwDQVLSLGEQQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 174 GIARALILEPKLIICDEPVSALDVSIQAQvvnLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVM 238
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREELpGTTVISVGHRSTLAAF-HDRVLEL 556
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
33-252 |
3.93e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 93.95 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkELLGMKPDEW--RAVRSDIQMIFQDp 110
Cdd:TIGR01842 327 PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-----RLDGADLKQWdrETFGKHIGYLPQD- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 lASLNPRmTIGEIIAEPLRTYHPkmsrQEVRERVKA-----MMLKvglLPNLINRYPHE----FSGGQCQRIGIARALIL 181
Cdd:TIGR01842 401 -VELFPG-TVAENIARFGENADP----EKIIEAAKLagvheLILR---LPDGYDTVIGPggatLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 182 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
42-256 |
4.15e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.02 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQDPLASlnpRMTIG 121
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEPVLF---SGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 122 EIIAEPLrTYHPKmsrQEVRERVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:TIGR00958 573 ENIAYGL-TDTPD---EEIMAAAKAANAHdfIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 196 DVSIQAqvvnLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:TIGR00958 649 DAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
34-248 |
6.98e-21 |
|
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: 89.01 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKpdeWRAVRSDIQMIFQDPLas 113
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSSLTIIPQDPT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 lnprmtigeIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLpNLinryphefSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:cd03369 93 ---------LFSGTIRSNLDPFDEYSDEEIYGALRVSEGGL-NL--------SQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 194 ALDVSIQAqvvnLLQQLQREM--GLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGT 248
Cdd:cd03369 155 SIDYATDA----LIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-244 |
1.13e-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: 92.58 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGHVAWLGKELL--GMKPDEwravRSDIQMIFQDplA 112
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKasNIRDTE----RAGIVIIHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIGEIIAEPLRTYHP--KMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:TIGR02633 88 TLVPELSVAENIFLGNEITLPggRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831001 191 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 244
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-244 |
1.21e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPLAS-LNP 116
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGIAYVPEDRKGEgLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGE-IIAEPLRTYHPK--MSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:COG1129 344 DLSIREnITLASLDRLSRGglLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 194 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 244
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
38-242 |
1.82e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV---KATDGHVAWLGKELL--GMKPDEWRAVRSDIQMIFQDplA 112
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQreGRLARDIRKSRANTGYIFQQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMT------IGEIIAEPL-RTYHPKMSRQEVRERVKAMMlKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKL 185
Cdd:PRK09984 96 NLVNRLSvlenvlIGALGSTPFwRTCFSWFTREQKQRALQALT-RVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
35-257 |
3.72e-20 |
|
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: 87.60 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELLGMKPDEWRAvRSDIQMIFQDplASL 114
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGQDITKLPMHKRA-RLGIGYLPQE--ASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:cd03218 87 FRKLTVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 195 LD-VSIQaQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 257
Cdd:cd03218 164 VDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
35-238 |
9.02e-20 |
|
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: 85.73 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEllgmkpdewravrsdiqmiFQDPLASL 114
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-------------------YQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NprmTIGEIIAEPlrTYHPKMSrqeVRERVKAMMLKVGLLPNLINR---------YPHE----FSGGQCQRIGIARALIL 181
Cdd:cd03268 72 R---RIGALIEAP--GFYPNLT---ARENLRLLARLLGIRKKRIDEvldvvglkdSAKKkvkgFSLGMKQRLGIALALLG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 182 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGII 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
39-248 |
9.86e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.01 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrSDIQMIFQDPL---ASLn 115
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLR---SRISIIPQDPVlfsGTI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 pRMTIgeiiaEPLRTYhpkmSRQEVRERVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICD 189
Cdd:cd03244 95 -RSNL-----DPFGEY----SDEELWQALERVGLKefVESLPGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 190 EPVSALDVsiqaQVVNLLQQLQREM--GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT 248
Cdd:cd03244 165 EATASVDP----ETDALIQKTIREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
39-266 |
1.17e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARA------IIGLVKAtDGHVAWLGKELLGMKPDEwRAVRSDIQMIFQDPla 112
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRV-EGKVTFHGKNLYAPDVDP-VEVRRRIGMVFQKP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 slNP-RMTIGEIIAEPLRTYHPKMSRQEVRER----------VKAMMLKVGLlpnlinryphEFSGGQCQRIGIARALIL 181
Cdd:PRK14243 101 --NPfPKSIYDNIAYGARINGYKGDMDELVERslrqaalwdeVKDKLKQSGL----------SLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 182 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVM---------YLGHAVELGTYDEV 252
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKI 246
|
250
....*....|....
gi 15831001 253 YHNPLHPYTRALMS 266
Cdd:PRK14243 247 FNSPQQQATRDYVS 260
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
35-247 |
1.21e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV---KATDGHVAWLGKEllgMKPDEWRavrSDIQMIFQDpl 111
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP---RKPDQFQ---KCVAYVRQD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 112 ASLNPRMTIGEIIaeplrTYHPKMS-RQEVRERVKAMMLKVGLLPNL-INRYPHEF----SGGQCQRIGIARALILEPKL 185
Cdd:cd03234 90 DILLPGLTVRETL-----TYTAILRlPRKSSDAIRKKRVEDVLLRDLaLTRIGGNLvkgiSGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
37-252 |
1.25e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgMKPDEWRAVRSDIQMIFQ-----DPL 111
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY--NKLDHKLAAQLGIGIIYQelsviDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 112 ASLNpRMTIGEIiaePLRTYH--PKMSRQEVRERVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 189
Cdd:PRK09700 96 TVLE-NLYIGRH---LTKKVCgvNIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 190 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
40-252 |
1.38e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.29 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV-KATDGHVAWLGKELLGMKPDEWRA----VRSDIQMIFQdplasl 114
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWELRKriglVSPALQLRFP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 nPRMTIGEIIA-------EPLRTYHPKMsrqevRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLII 187
Cdd:COG1119 93 -RDETVLDVVLsgffdsiGLYREPTDEQ-----RERARELLELLGLAH-LADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 188 CDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHdlavvkHISD------RVLVMYLGHAVELGTYDEV 252
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVEEippgitHVLLLKDGRVVAAGPKEEV 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
55-260 |
1.79e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.62 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 55 VVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAV-RSDIQMIFQDplASLNPRMTI-GEIiaeplrTYH 132
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPeKRRIGYVFQD--ARLFPHYKVrGNL------RYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 133 PKMSRQEVRERVkammlkVGLL--PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 210
Cdd:PRK11144 101 MAKSMVAQFDKI------VALLgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 211 QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP-LHPY 260
Cdd:PRK11144 175 AREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSaMRPW 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-252 |
2.73e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKDG-----KQWFWQPPKTLK----AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT----- 77
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslKELLLRRRRTRReefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTsgrve 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 78 -DGHVAWL------------GKE-------LLGMKPDEWRAVRSDIqmI-FQDplaslnprmtIGEIIAEPLRTYhpkms 136
Cdd:COG1134 85 vNGRVSALlelgagfhpeltGREniylngrLLGLSRKEIDEKFDEI--VeFAE----------LGDFIDQPVKTY----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 137 rqevrervkammlkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGL 216
Cdd:COG1134 148 -----------------------------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GR 197
|
250 260 270
....*....|....*....|....*....|....*.
gi 15831001 217 SLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:COG1134 198 TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
43-252 |
3.03e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWLGKELLGMKPDEWRAVRsdIQMIFQDplASLNPRMTIGE 122
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARR--IGLLAQN--ATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIAEPLRTYHPKMSR--QEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:PRK10253 101 LVARGRYPHQPLFTRwrKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831001 201 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
38-253 |
3.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.95 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELL-GMKPDEWRAVRSDIQMIFQDPLASLNP 116
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEPlrtYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:PRK13649 101 ETVLKDVAFGP---QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 197 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 253
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-241 |
3.34e-19 |
|
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: 87.96 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 31 WQPPKT-LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGlvkATDGhvAWLGKELLGMKPDEWR----AVRSDIQM 105
Cdd:TIGR02633 266 WDVINPhRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG---AYPG--KFEGNVFINGKPVDIRnpaqAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 106 IFQD-PLASLNPRMTIGE-IIAEPLRTYHPKM------SRQEVRERVKAMMLKVGLlPNL-INRypheFSGGQCQRIGIA 176
Cdd:TIGR02633 341 VPEDrKRHGIVPILGVGKnITLSVLKSFCFKMridaaaELQIIGSAIQRLKVKTAS-PFLpIGR----LSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 177 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 241
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-237 |
4.91e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.94 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 47 LYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWlgKELLGMKPDEwraVRSDIQMIFQDPLASLNPRMT---IGEI 123
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQY---IKPDYDGTVEDLLRSITDDLGssyYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 124 IAEPLRtyhpkmsrqevrervkammlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 203
Cdd:PRK13409 437 IIKPLQ------------------------LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|....
gi 15831001 204 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-247 |
6.35e-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: 84.12 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKDGK-QWFWQP--------PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGH-- 80
Cdd:cd03220 1 IELENVSKSYPTYKGGsSSLKKLgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 81 ----VAWL------------GKE-------LLGMKPDEWRAVRSDIQMiFQDplaslnprmtIGEIIAEPLRTYhpkmsr 137
Cdd:cd03220 81 vrgrVSSLlglgggfnpeltGREniylngrLLGLSRKEIDEKIDEIIE-FSE----------LGDFIDLPVKTY------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 138 qevrervkammlkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLS 217
Cdd:cd03220 144 ----------------------------SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKT 194
|
250 260 270
....*....|....*....|....*....|
gi 15831001 218 LIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:cd03220 195 VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-256 |
6.50e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.46 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWR---AVRSDIQMI 106
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRsrlAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 107 FQDPLASL----NPRMTIGEI-IAEPLRTYH------PKMSRQEVRERvkAMMLkvgllpnlinryphefSGGQCQRIGI 175
Cdd:PRK10789 401 FSDTVANNialgRPDATQQEIeHVARLASVHddilrlPQGYDTEVGER--GVML----------------SGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 176 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQ 539
|
.
gi 15831001 256 P 256
Cdd:PRK10789 540 S 540
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
40-252 |
9.16e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 9.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPdewRAVRSDIQMIFQDPLAslnPR-M 118
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQHHLT---PEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIA---EPLRTYHPKMSrQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:PRK11231 92 TVRELVAygrSPWLSLWGRLS-AEDNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 196 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK11231 170 DINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-237 |
2.88e-18 |
|
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: 85.61 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLR-----LYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAwlGKELLGMKPDEwraVRSDIQMIFQDPLA 112
Cdd:COG1245 349 KSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQY---ISPDYDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIGEI----IAEPLRtyhpkmsrqevrervkammlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 188
Cdd:COG1245 424 SANTDDFGSSYykteIIKPLG------------------------LEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831001 189 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
40-242 |
3.34e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPLA------- 112
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD--GLANGIVYISEDRKRdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIgeiiaeplrTYHPKMSRQEVRERVKAMMLKVGLLPNLIN-RYPH------EFSGGQCQRIGIARALILEPKL 185
Cdd:PRK10762 346 SVKENMSL---------TALRYFSRAGGSLKHADEQQAVSDFIRLFNiKTPSmeqaigLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
38-236 |
6.52e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrSDIQMIFQDPlaslnpr 117
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQVSYCAQTP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPL------RTYHPKMsrqevrERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK10247 91 TLFGDTVYDNLifpwqiRNQQPDP------AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVL 236
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
30-247 |
7.06e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 80.05 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKpdewRAVRSDIQMIFQD 109
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE----KALSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 PlaslnprmtigeiiaeplrtyhpkmsrqevrervkaMMLKVGLLPNLINRypheFSGGQCQRIGIARALILEPKLIICD 189
Cdd:cd03247 84 P------------------------------------YLFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 190 EPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELG 247
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-252 |
9.10e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 30 FWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkeLLGMKP-DEWRA---VRSDIQM 105
Cdd:PRK10575 19 FRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI------LLDAQPlESWSSkafARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 106 IFQDPLASlnpRMTIGEIIAEPLRTYHPKMSR--QEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEP 183
Cdd:PRK10575 91 PQQLPAAE---GMTVRELVAIGRYPWHGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
40-247 |
1.05e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkPDEWRAVRSDIQMIFQdpLASLNPRMT 119
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAEPLRTYhpKMSRQEVrERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:PRK13536 131 VRENLLVFGRYF--GMSTREI-EAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15831001 200 QAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:PRK13536 208 RHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
37-244 |
2.47e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkpDEW---RAVRSDIQMIFQDplAS 113
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-----TDWqtaKIMREAVAIVPEG--RR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEIIAeplrtyhpkM-----SRQEVRERVKAMMlkvGLLPNLINRYPHE---FSGGQCQRIGIARALILEPKL 185
Cdd:PRK11614 91 VFSRMTVEENLA---------MggffaERDQFQERIKWVY---ELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 186 IICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 244
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-225 |
2.87e-17 |
|
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: 82.41 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVHfeikdgkqWFWQPPktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL 88
Cdd:TIGR02868 332 KPTLELRDLSAG--------YPGAPP----VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 LGMKPDEWRAVrsdIQMIFQDPlaslnprMTIGEIIAEPLRTYHPKMSRQEVRervkAMMLKVGLLpNLINRYPH----- 163
Cdd:TIGR02868 400 SSLDQDEVRRR---VSVCAQDA-------HLFDTTVRENLRLARPDATDEELW----AALERVGLA-DWLRALPDgldtv 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 164 ------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDL 225
Cdd:TIGR02868 465 lgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
41-251 |
3.46e-17 |
|
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: 82.18 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewrAVRSDIQMIFQDPLasL-NprMT 119
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA---SLRAAIGIVPQDTV--LfN--DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAeplrtY-HPKMSRQEVRERVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARAL 179
Cdd:COG5265 448 IAYNIA-----YgRPDASEEEVEAAARAAQI-------------HDFieslpdgydtrvgerglklSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 180 ILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 251
Cdd:COG5265 510 LKNPPILIFDEATSALDSrterAIQAA----LREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAE 578
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
43-236 |
3.59e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPdewravrsdiQMIFQDPLASLnprmTIGE 122
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVP----------QKLYLDTTLPL----TVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIaeplrTYHPKMSRQEVR---ERVKAmmlkvgllPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 199
Cdd:PRK09544 89 FL-----RLRPGTKKEDILpalKRVQA--------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 15831001 200 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 236
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
39-236 |
4.23e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewravRSDIQMIFqdPLaslnprm 118
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-----RSEVPDSL--PL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIA-------EPLRTYhpkmsRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:NF040873 73 TVRDLVAmgrwarrGLWRRL-----TRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL 236
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-242 |
4.30e-17 |
|
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: 79.30 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKDGKQW-------FWQPPKTLK-AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaw 83
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGligslksLFKRKYREVeALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 84 lgkELLGMKPDEWR-AVRSDIQMIF--QDPLA-SLNPRMTIgEIIAEPLRtyhpkMSRQEVRERVK--AMMLKVGLLPNL 157
Cdd:cd03267 79 ---RVAGLVPWKRRkKFLRRIGVVFgqKTQLWwDLPVIDSF-YLLAAIYD-----LPPARFKKRLDelSELLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 158 INRyphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:cd03267 150 PVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLV 226
|
....*
gi 15831001 238 MYLGH 242
Cdd:cd03267 227 IDKGR 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-237 |
5.21e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.99 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLR-----LYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGkELLGMKPDEwraVRSDIQMIFQ 108
Cdd:cd03237 4 PTMKKTLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQY---IKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 DPLASLNPRMTIgeiiaeplrtyHPkmsrQEVRERVKAMMLKvGLLPNLINryphEFSGGQCQRIGIARALILEPKLIIC 188
Cdd:cd03237 80 DLLSSITKDFYT-----------HP----YFKTEIAKPLQIE-QILDREVP----ELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831001 189 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-248 |
5.52e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.30 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 9 KVLLEIADLKVhfEIKDGKqwfwqppkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIG--LVKATDGHVAWLGK 86
Cdd:CHL00131 5 KPILEIKNLHA--SVNENE--------ILK---GLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 ELLGMKPDEwRAvRSDIQMIFQDPLaslnprmtigEII----AEPLRTYH---------PKMSRQEVRERVKAMMLKVGL 153
Cdd:CHL00131 72 SILDLEPEE-RA-HLGIFLAFQYPI----------EIPgvsnADFLRLAYnskrkfqglPELDPLEFLEIINEKLKLVGM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 154 LPNLINRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALDVS---IQAQVVNLLQQLQRemglSLIFIAHDLAVVK 229
Cdd:CHL00131 140 DPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLD 215
|
250 260
....*....|....*....|
gi 15831001 230 HIS-DRVLVMYLGHAVELGT 248
Cdd:CHL00131 216 YIKpDYVHVMQNGKIIKTGD 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-251 |
6.47e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 7 GRKVLlEIADLKVHFeikDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWlGK 86
Cdd:COG0488 312 GKKVL-ELEGLSKSY---GDKTLL----------DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 87 EL-LGmkpdewravrsdiqmIF-QDpLASLNPRMTIGEIIAEplrtYHPKMSRQEVRERVKAMMLKvgllPNLINRYPHE 164
Cdd:COG0488 377 TVkIG---------------YFdQH-QEELDPDKTVLDELRD----GAPGGTEQEVRGYLGRFLFS----GDDAFKPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 165 FSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQAqVVNLLQQLQremGlSLIFIAHDLAVVKHISDRVLVMYLGHA 243
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
....*....
gi 15831001 244 VE-LGTYDE 251
Cdd:COG0488 508 REyPGGYDD 516
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-241 |
7.46e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 7.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-ATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQD------- 109
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDrkrdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 110 ---------PLASLNpRMTIGEIIAEPLRTyhpKMSRQEV-RERVKA--MMLKVGLLpnlinryphefSGGQCQRIGIAR 177
Cdd:PRK13549 354 pvmgvgkniTLAALD-RFTGGSRIDDAAEL---KTILESIqRLKVKTasPELAIARL-----------SGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 241
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
31-238 |
1.36e-16 |
|
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: 77.37 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 31 WQPpkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEllgmkPDEWRAVRSDIQMIFQDP 110
Cdd:cd03290 10 WGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN-----ESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 LASLNPRM---TIGEIIaeplrTYHPKMSRQevreRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIA 176
Cdd:cd03290 83 YAAQKPWLlnaTVEENI-----TFGSPFNKQ----RYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 177 RALILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 238
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAM 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-241 |
1.50e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKP-----DEWRAVRSDIQMIFQDPLASLN 115
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPqepplDDDLTVLDTVLDGDAELRALEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PRMTIGEIIAEPLRTYHpKMSRQEVR----------ERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKL 185
Cdd:COG0488 95 ELEELEAKLAEPDEDLE-RLAELQEEfealggweaeARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 186 IICDEPVSALDV-SIQaqvvnLLQQ-LQREMGlSLIFIAHD---L-AVVKHI---SDRVLVMYLG 241
Cdd:COG0488 174 LLLDEPTNHLDLeSIE-----WLEEfLKNYPG-TVLVVSHDryfLdRVATRIlelDRGKLTLYPG 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
42-238 |
2.15e-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: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkeLLGMKP---DEWRAVRSDIQMIFQDPLasLNPRm 118
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV------LLDGKPisqYEHKYLHSKVSLVGQEPV--LFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYHpkmsrqevRERVKAMMLKVGLlPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLII 187
Cdd:cd03248 103 SLQDNIAYGLQSCS--------FECVKEAAQKAHA-HSFISELASGYdtevgekgsqlSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 188 CDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVM 238
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
31-241 |
2.62e-16 |
|
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: 76.05 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 31 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGlvKATDGHVAwlGKELLGMKPDEWRAVRSDIQMIFQDP 110
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVS--GEVLINGRPLDKRSFRKIIGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 LasLNPRMTigeiiaeplrtyhpkmsrqeVRErvkAMM----LKvGLlpnlinryphefSGGQCQRIGIARALILEPKLI 186
Cdd:cd03213 92 I--LHPTLT--------------------VRE---TLMfaakLR-GL------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDL-AVVKHISDRVLVMYLG 241
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-238 |
2.63e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAvrSDIQMIFQDplasLN-- 115
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGIGIIHQE----LNli 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PRMTIGEII---AEPLRTY----HPKMSRQEVRervkammlkvgLLPNL-INRYPH----EFSGGQCQRIGIARALILEP 183
Cdd:PRK10762 92 PQLTIAENIflgREFVNRFgridWKKMYAEADK-----------LLARLnLRFSSDklvgELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
40-252 |
3.52e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkeLLGMKPDE---WRAVRSDIQMIFQDPLASLNP 116
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV------LVAGDDVEalsARAASRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RmtiGEIIAEPLRTyhPKMSR-----QEVRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK09536 93 D---VRQVVEMGRT--PHRSRfdtwtETDRAAVERAMERTG-VAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 192 VSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
38-257 |
4.79e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.22 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVaWL-GKELLGMKPDEwRAvRSDIQMIFQDPlaSLNP 116
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLdGEDITHLPMHK-RA-RLGIGYLPQEA--SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGE---IIAEPLrtyhpKMSRQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:COG1137 92 KLTVEDnilAVLELR-----KLSKKEREERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 194 ALD---VS-IQAQVVNLlqqlqREMGLSlIFIA-HD----LAVVkhisDRVLVMYLGHAVELGTYDEVYHNPL 257
Cdd:COG1137 166 GVDpiaVAdIQKIIRHL-----KERGIG-VLITdHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-237 |
5.81e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawlgkELLGMKPdeWR---AVRSDIQMIF-Q-- 108
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGYVP--FKrrkEFARRIGVVFgQrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 109 ----D--PLASLNprmTIGEIiaeplrtYhpKMSRQEVRERVKAM--MLKVGllpNLINRYPHEFSGGQCQRIGIARALI 180
Cdd:COG4586 106 qlwwDlpAIDSFR---LLKAI-------Y--RIPDAEYKKRLDELveLLDLG---ELLDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 181 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
35-255 |
7.88e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAwLGKELLGMKPDEWRAVRSdIQMIFQDplASL 114
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII-IDDEDISLLPLHARARRG-IGYLPQE--ASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEIIAEPLRTYHpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:PRK10895 90 FRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 195 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PRK10895 168 VDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-223 |
8.66e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 73.73 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 44 TLRLYEGETLGVVGESGCGKSTFARAIIGLvkatdghvaW-LGKELLGMKPDEwravrsDIQMIFQdplaslnprmtige 122
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGL---------WpWGSGRIGMPEGE------DLLFLPQ-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 iiaeplrtyHPKMSRQEVRERVkammlkvgllpnlinRYP--HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:cd03223 72 ---------RPYLPLGTLREQL---------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 15831001 201 AQVVNLLqqlqREMGLSLIFIAH 223
Cdd:cd03223 128 DRLYQLL----KELGITVISVGH 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-242 |
9.76e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPLASlnprmtiGE 122
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ--RLARGLVYLPEDRQSS-------GL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIAEPLR------TYH-------PKMSRQeVRERVKAMMlkvGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 189
Cdd:PRK15439 353 YLDAPLAwnvcalTHNrrgfwikPARENA-VLERYRRAL---NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15831001 190 EPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGH 242
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-251 |
4.13e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.83 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKDGKqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGM 91
Cdd:PRK11176 333 RVIERAKGDIEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 KPDEWR---AVRSDIQMIFQDplaslnprmTIGEIIAEPLRTyhpKMSRQEVRERVK---AMmlkvgllpNLINRYPHEF 165
Cdd:PRK11176 411 TLASLRnqvALVSQNVHLFND---------TIANNIAYARTE---QYSREQIEEAARmayAM--------DFINKMDNGL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 166 -----------SGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQREMgLSLIfIAHDLAVVKH 230
Cdd:PRK11176 471 dtvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQKNR-TSLV-IAHRLSTIEK 544
|
250 260
....*....|....*....|.
gi 15831001 231 iSDRVLVMYLGHAVELGTYDE 251
Cdd:PRK11176 545 -ADEILVVEDGEIVERGTHAE 564
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-252 |
4.59e-15 |
|
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: 75.61 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDG----HVA------WL-------------GKELLGM 91
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyHVAlcekcgYVerpskvgepcpvcGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 KPDEW-------RAVRSDIQMIFQDPLASLNPRMTIGEII-AEPLRTYHPKmsrqevrervKAMMLKVGLLP--NLINRY 161
Cdd:TIGR03269 93 EVDFWnlsdklrRRIRKRIAIMLQRTFALYGDDTVLDNVLeALEEIGYEGK----------EAVGRAVDLIEmvQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 162 PH---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:TIGR03269 163 THiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250
....*....|....
gi 15831001 239 YLGHAVELGTYDEV 252
Cdd:TIGR03269 243 ENGEIKEEGTPDEV 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-245 |
6.07e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTfaraiigLVKATDG---HVAWLGKELLGMKPDEWRAVRSD----IQMIFQDp 110
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKST-------LMKVLSGvypHGSYEGEILFDGEVCRFKDIRDSealgIVIIHQE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 LAsLNPRMTIGEII---AEPLRtyHPKMSRQEVRERVKAMMLKVGLLPNlinryPHEFSG----GQCQRIGIARALILEP 183
Cdd:NF040905 87 LA-LIPYLSIAENIflgNERAK--RGVIDWNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 184 KLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 245
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-251 |
1.04e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 26 GKQWFWQPPKT-LKAVDGVtlrLYEGETLGVVGESGCGKSTFARAII-----GLVKatDGHVAwlgkeLLGMKPDEW--R 97
Cdd:TIGR00955 29 GCFCRERPRKHlLKNVSGV---AKPGELLAVMGSSGAGKTTLMNALAfrspkGVKG--SGSVL-----LNGMPIDAKemR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 98 AVRSDIQmifQDPLasLNPRMTIGE--IIAEPLRTyHPKMSRQEVRERVKAMMLKVGLLP--NLINRYPHE---FSGGQC 170
Cdd:TIGR00955 99 AISAYVQ---QDDL--FIPTLTVREhlMFQAHLRM-PRRVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 171 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL-QRemGLSLIFIAHD-LAVVKHISDRVLVMYLGHAVELGT 248
Cdd:TIGR00955 173 KRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGS 250
|
...
gi 15831001 249 YDE 251
Cdd:TIGR00955 251 PDQ 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
43-256 |
1.72e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATdGHVAWLGKELLGMKPDEWRAvrsDIQMIFQDPLAslnPRMTIGE 122
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRK---HLSWVGQNPQL---PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIAepLRtyHPKMSRQEVRERVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:PRK11174 442 NVL--LG--NPDASDEQLQQALENAWVSefLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 197 VSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
40-252 |
4.55e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.88 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwRAVRsdIQMIFQDPlaSLNPRMT 119
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE-LAKR--LAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIA---EPlrtYHPKMSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:COG4604 92 VRELVAfgrFP---YSKGRLTAEDREIIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 197 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:COG4604 168 MKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-228 |
6.71e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.31 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRavrsdiQMIFQDPLASLNPRMTIg 121
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLGHLPGLKPELSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 122 eiiAEPLRTYHPKMsrQEVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 201
Cdd:TIGR01189 91 ---LENLHFWAAIH--GGAQRTIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....*...
gi 15831001 202 QVVNLL-QQLQREmGLSLIFIAHDLAVV 228
Cdd:TIGR01189 165 LLAGLLrAHLARG-GIVLLTTHQDLGLV 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-251 |
1.61e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDewRAVRSDIQMIFQDPLasLNP 116
Cdd:PRK15439 27 LKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHQLGIYLVPQEPL--LFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEPLrtyhPKmsRQEVRERVKAMMLKVGLLPNLinryphEFSGGQC-----QRIGIARALILEPKLIICDEP 191
Cdd:PRK15439 100 NLSVKENILFGL----PK--RQASMQKMKQLLAALGCQLDL------DSSAGSLevadrQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 192 VSALdvsIQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDE 251
Cdd:PRK15439 168 TASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-238 |
2.16e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQD-------PLASLN 115
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRAGIMLCPEDrkaegiiPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PRMTI---------GEIIaeplrtyHPKMSRQEVRERVKAMMLKVGLLPNLINryphEFSGGQCQRIGIARALILEPKLI 186
Cdd:PRK11288 350 DNINIsarrhhlraGCLI-------NNRWEAENADRFIRSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15831001 187 ICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
39-233 |
2.61e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLgmkpdewRAVRSD-IQMIFQDPLASLNPR 117
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-------QALQKNlVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEIIAEPlRTYHPKMSRQ---EVRERVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:PRK15056 95 VLVEDVVMMG-RYGHMGWLRRakkRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831001 195 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISD 233
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
11-249 |
4.29e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.89 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 11 LLEIADLKVHFEIKDgkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL--VKATDGHVAWLGKEL 88
Cdd:PRK09580 1 MLSIKDLHVSVEDKA-------------ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 89 LGMKPDEwRAVRSdIQMIFQDP--LASLNPRMTIGEIIAEpLRTY--HPKMSRQEVRERVKAMMLKVGLLPNLINRYPHE 164
Cdd:PRK09580 68 LELSPED-RAGEG-IFMAFQYPveIPGVSNQFFLQTALNA-VRSYrgQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 165 -FSGGQCQRIGIARALILEPKLIICDEPVSALDV---SIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHIS-DRVLVMY 239
Cdd:PRK09580 145 gFSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLY 220
|
250
....*....|
gi 15831001 240 LGHAVELGTY 249
Cdd:PRK09580 221 QGRIVKSGDF 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
56-251 |
4.29e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.75 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 56 VGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPdewRAVRSDIQMIFQDPL---ASLNPRMTIGEIIAEplrtyh 132
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDPVvlaDTFLANVTLGRDISE------ 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 133 pkmsrqevrERVKAMMLKVGL------LPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 202
Cdd:PRK10790 444 ---------EQVWQALETVQLaelarsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831001 203 VVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDE 251
Cdd:PRK10790 515 IQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-228 |
4.42e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.13 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAvrsdiqMIFQDPLASLNPRMTIg 121
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG------LLYLGHAPGIKTTLSV- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 122 eiiAEPLRTYHPKMSRQEVRERVKAMMLKvgllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 201
Cdd:cd03231 91 ---LENLRFWHADHSDEQVEEALARVGLN-----GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|....*..
gi 15831001 202 QVVNLLQQLQREMGLSLIFIAHDLAVV 228
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-230 |
4.81e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 12 LEIADLKVHFEIKdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVawLGKELLGM 91
Cdd:PTZ00265 383 IQFKNVRFHYDTR----------KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI--IINDSHNL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 92 KPDEWRAVRSDIQMIFQDPL-----------------------------------ASLNPRMTIGEIIAEPL-------- 128
Cdd:PTZ00265 451 KDINLKWWRSKIGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqENKNKRNSCRAKCAGDLndmsnttd 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 129 -------RTYHPKMSRQEVRERVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 195
Cdd:PTZ00265 531 sneliemRKNYQTIKDSEVVDVSKKVLIHdfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
250 260 270
....*....|....*....|....*....|....*
gi 15831001 196 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 230
Cdd:PTZ00265 611 DNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
41-238 |
5.12e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKellgmkpdewravrsdiqmifqdplaslnprmti 120
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 geiiaeplrtyhpkmsrqevrervkammLKVGLLPNLinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 200
Cdd:cd03221 63 ----------------------------VKIGYFEQL--------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190
....*....|....*....|....*....|....*...
gi 15831001 201 AQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLVM 238
Cdd:cd03221 107 EALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
41-245 |
1.25e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWlgkellGMKPDEWRAVRSDIQMIF--QDPLASLnprm 118
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------DVPDNQFGREASLIDAIGrkGDFKDAV---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 tigEIIAeplrtyhpkmsrqevrervkammlKVGLL-PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:COG2401 117 ---ELLN------------------------AVGLSdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831001 198 SiQAQVVNL-LQQLQREMGLSLIFIAHDLAVVKHIS-DRVLVMYLGHAVE 245
Cdd:COG2401 170 Q-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-238 |
1.28e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 18 KVHFEIKDGKQwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEllgMKP-DEW 96
Cdd:PRK09700 263 ETVFEVRNVTS------RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD---ISPrSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 97 RAVRSDIQMIFQD-------PLASLNPRMTIGEIIAE-----PLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINryphE 164
Cdd:PRK09700 334 DAVKKGMAYITESrrdngffPNFSIAQNMAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNIT----E 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 165 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-239 |
1.35e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.62 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 49 EGETLGVVGESGCGKSTFARAIIGLVKATdghvawLGKEllgMKPDEWRAV-----RSDIQMIFQDPL-----ASLNPRM 118
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPN------LGKF---DDPPDWDEIldefrGSELQNYFTKLLegdvkVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 ----------TIGEIIAEplrtyhpKMSRQEVRERVKAMMLKvgllpNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 188
Cdd:cd03236 96 vdlipkavkgKVGELLKK-------KDERGKLDELVDQLELR-----HVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15831001 189 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-238 |
1.46e-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: 65.57 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 32 QPPKTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKelLGMKPDE-WravrsdIQmifqdp 110
Cdd:cd03250 16 ETSFTLKDIN---LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEpW------IQ------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 111 laslnpRMTIGEIIaeplrTYHPKMSRQEVRERVKAMMLKVGL--LPNLINRYPHE----FSGGQCQRIGIARALILEPK 184
Cdd:cd03250 79 ------NGTIRENI-----LFGKPFDEERYEKVIKACALEPDLeiLPDGDLTEIGEkginLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 185 LIICDEPVSALDvsiqAQVVN-LLQQLQREMGLSL---IFIAHDLAVVKHiSDRVLVM 238
Cdd:cd03250 148 IYLLDDPLSAVD----AHVGRhIFENCILGLLLNNktrILVTHQLQLLPH-ADQIVVL 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-252 |
1.62e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 29 WFWQPPKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKelLGMKPDE-WraVRSDiqmif 107
Cdd:TIGR00957 646 WARDLPPTL---NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQaW--IQND----- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 108 qdplaSLNPRMTIGEIIAEPlrtyhpkmsrqevreRVKAMMLKVGLLPNL----------INRYPHEFSGGQCQRIGIAR 177
Cdd:TIGR00957 714 -----SLRENILFGKALNEK---------------YYQQVLEACALLPDLeilpsgdrteIGEKGVNLSGGQKQRVSLAR 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVvnlLQQLQREMGL----SLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
40-196 |
1.77e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.14 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkPDEWRAVRSDIQMIFQdpLASLNPRMT 119
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQRVGVVPQ--FDNLDPDFT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 120 IgeiiAEPLRTY--HPKMSRQEVRERVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 196
Cdd:PRK13537 97 V----RENLLVFgrYFGLSAAAARALV-PPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-252 |
2.13e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.02 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGHVAWLGKELLGMKPDE---WRAVRSdiQMifQDPLASlnp 116
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElarHRAYLS--QQ--QSPPFA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 rMTIGEIIAeplrTYHPKMSRQEVRERVKAMML-KVGLLPNLiNRYPHEFSGGQCQRIGIARALI-------LEPKLIIC 188
Cdd:COG4138 84 -MPVFQYLA----LHQPAGASSEAVEQLLAQLAeALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 189 DEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
41-209 |
2.86e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkpdewRAVRSDIQmifQDPL-----ASLN 115
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRDEYH---QDLLylghqPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 PRMTigeiIAEPLRTYHPkMSRQEVRERVKAMMLKVGL-----LPnlinryPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:PRK13538 87 TELT----ALENLRFYQR-LHGPGDDEALWEALAQVGLagfedVP------VRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170
....*....|....*....
gi 15831001 191 PVSALDVSIQAQVVNLLQQ 209
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQ 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-237 |
5.55e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 38 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDplASLNPR 117
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAAGVAIIYQE--LHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEII---AEPLR--TYHPKMSRQEVRERVKAMMLKVGllPNLINRYpheFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:PRK11288 94 MTVAENLylgQLPHKggIVNRRLLNYEAREQLEHLGVDID--PDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15831001 193 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 237
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-269 |
6.35e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSdiqMIFQDP-L 111
Cdd:PLN03232 1249 PP----VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS---IIPQSPvL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 112 ASLNPRMTIgeiiaEPLrTYHPKMSRQEVRERVKammlkvglLPNLINRYP-----------HEFSGGQCQRIGIARALI 180
Cdd:PLN03232 1322 FSGTVRFNI-----DPF-SEHNDADLWEALERAH--------IKDVIDRNPfgldaevseggENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 181 LEPKLIICDEPVSALDVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLH 258
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
250
....*....|.
gi 15831001 259 PYTRALMSAVP 269
Cdd:PLN03232 1463 AFFRMVHSTGP 1473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
40-247 |
3.37e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATdghvAWLGKELL-GMKPDewRAVRSDIQMIFQDPLasLNPRM 118
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILAnNRKPT--KQILKRTGFVTQDDI--LYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGE--IIAEPLRTyhPK-MSRQEVRERVKAMMLKVGLLP--NLI--NRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PLN03211 156 TVREtlVFCSLLRL--PKsLTKQEKILVAESVISELGLTKceNTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15831001 192 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 247
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
42-208 |
4.42e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwravrsdiQMIFQDPLASLNPRMTIG 121
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--------ACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 122 EII---AEPLRTYhpkmsrqevRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK13539 92 ENLefwAAFLGGE---------ELDIAAALEAVG-LAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170
....*....|
gi 15831001 199 IQAQVVNLLQ 208
Cdd:PRK13539 162 AVALFAELIR 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-239 |
4.84e-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: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 46 RLY------EGETLGVVGESGCGKSTFARAIIGLVKATDGHVAwlgkellgmKPDEWRAV-----RSDIQMIFQDpLASl 114
Cdd:COG1245 89 RLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---------EEPSWDEVlkrfrGTELQDYFKK-LAN- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 nprmtiGEIiaeplRTYH--------PKMSRQEVR-------ERVKAMML--KVGLLpNLINRYPHEFSGGQCQRIGIAR 177
Cdd:COG1245 158 ------GEI-----KVAHkpqyvdliPKVFKGTVRellekvdERGKLDELaeKLGLE-NILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-251 |
5.06e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVKAtdghvAWL---GKELLGMKP-DEWR--AVRSDIQMI 106
Cdd:PRK11160 349 PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTR-----AWDpqqGEILLNGQPiADYSeaALRQAISVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 107 FQ----------DPLAslnprmtigeiIAEPLRTyhpkmsrqevRERVKAMMLKVGLlPNLINRYP----------HEFS 166
Cdd:PRK11160 420 SQrvhlfsatlrDNLL-----------LAAPNAS----------DEALIEVLQQVGL-EKLLEDDKglnawlgeggRQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 167 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVEL 246
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
....*
gi 15831001 247 GTYDE 251
Cdd:PRK11160 555 GTHQE 559
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-248 |
5.96e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.88 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkPDEWRAVRSDIQMIFQDPLas 113
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNI-- 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRMTIGEIIaeplrTYHPKM---SRQEVRERVKAMMLKVGlLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 190
Cdd:TIGR01257 1014 LFHHLTVAEHI-----LFYAQLkgrSWEEAQLEMEAMLEDTG-LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 191 PVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 248
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
36-244 |
1.62e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 36 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK---ATDGHVAWLGKELLGMKpdewRAVRSDIQMIFQDPLA 112
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFA----EKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 slNPRMTIGEIIaeplrtyhpkmsrqEVRERVKAmmlkvgllpnliNRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:cd03233 95 --FPTLTVRETL--------------DFALRCKG------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 193 SALDVSIQAQVVNLLQQLQREMGLSLIFI---AHDLAVvkHISDRVLVMYLGHAV 244
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIY--DLFDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
49-239 |
1.67e-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: 59.12 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 49 EGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWlgkellgmkpdewravrsdiqmifqdplaslnPRMTIgeiiaepl 128
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--------------------------------DGITP-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 129 rTYHPKmsrqevrervkammlKVGLlpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 208
Cdd:cd03222 64 -VYKPQ---------------YIDL------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|.
gi 15831001 209 QLQREMGLSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
50-252 |
1.78e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIIGLVKATdGHVAWLGKELLGMKPDE---WRA-----VRSDIQM-IFQDPLASLnprmti 120
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAElarHRAylsqqQTPPFAMpVFQYLTLHQ------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 121 geiiAEPLRTYHPKMSRQEVRERVKammlkvglLPNLINRYPHEFSGGQCQRIGIA-------RALILEPKLIICDEPVS 193
Cdd:PRK03695 95 ----PDKTRTEAVASALNEVAEALG--------LDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831001 194 ALDVsiqAQvVNLLQQLQREM---GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK03695 163 SLDV---AQ-QAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-242 |
1.91e-10 |
|
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: 58.54 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIIGLVKATDGHVAwlgkellgmkpdewravrsdiqmifqdplaslnprmtigEIIAEPLR 129
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------YIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 130 TYHPKMSRQEvrervkammlkvgllpnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV-----V 204
Cdd:smart00382 43 EEVLDQLLLI-----------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15831001 205 NLLQQLQREMGLSLIFIAHDL-----AVVKHISDRVLVMYLGH 242
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-237 |
3.01e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 154 LPNL----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 229
Cdd:PTZ00265 1344 LPNKydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
....*...
gi 15831001 230 HiSDRVLV 237
Cdd:PTZ00265 1424 R-SDKIVV 1430
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-250 |
3.10e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 45 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWlgkellgmkpdEWRAVRSDIQmifQDPlaslnPRMTIGEI- 123
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-----------EQDLIVARLQ---QDP-----PRNVEGTVy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 124 ---------IAEPLRTYHP---------------KMSR-QEVRE---------RVKAMMLKVGLLPN-LINryphEFSGG 168
Cdd:PRK11147 85 dfvaegieeQAEYLKRYHDishlvetdpseknlnELAKlQEQLDhhnlwqlenRINEVLAQLGLDPDaALS----SLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 169 QCQRIGIARALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL-G 247
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYpG 236
|
...
gi 15831001 248 TYD 250
Cdd:PRK11147 237 NYD 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-239 |
4.32e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 46 RLY------EGETLGVVGESGCGKSTFARAIIGLVKA----TDGHVAW-------LGKELL----GMKPDEWRAVRSdIQ 104
Cdd:PRK13409 89 KLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWdevlkrfRGTELQnyfkKLYNGEIKVVHK-PQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 105 MIFQDPLASlnpRMTIGEIiaepLRTYHPKMSRQEVRERVKammlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPK 184
Cdd:PRK13409 168 YVDLIPKVF---KGKVREL----LKKVDERGKLDEVVERLG--------LENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 185 LIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMY 239
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
39-252 |
4.50e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.67 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLgmkpdewRAVRSdiqmifqdplaSLNPRM 118
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL-------IAISS-----------GLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAepLRTYHPKMSRQEVRErVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK13545 101 TGIENIE--LKGLMMGLTKEKIKE-IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831001 199 IQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK13545 178 FTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-221 |
7.04e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHvAWL-GKELlgmkpdewravrsdiqmifqDPlASLNPR 117
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-AWLfGQPV--------------------DA-GDIATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIG----------EI-IAEPL----RTYHpkMSRQEVRERVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILE 182
Cdd:NF033858 339 RRVGymsqafslygELtVRQNLelhaRLFH--LPAAEIAARVAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190
....*....|....*....|....*....|....*....
gi 15831001 183 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSlIFI 221
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFI 453
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-248 |
8.89e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL--LGMkpdewRAVRSDIQMIFQDP-LASLNPRMT 119
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIakIGL-----HDLRFKITIIPQDPvLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IgeiiaEPLRTYhpkmSRQEVRERVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:TIGR00957 1380 L-----DPFSQY----SDEEVWWALELAHLKtfVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 194 ALDVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVVKHISdRVLVMYLGHAVELGT 248
Cdd:TIGR00957 1451 AVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-238 |
1.36e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDplasLN- 115
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQE----LNl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 116 -------PRMTIGEIIAEPLRTYHPKMSRQevrerVKAMMLKVGllpnlINRYPHE----FSGGQCQRIGIARALILEPK 184
Cdd:PRK10982 85 vlqrsvmDNMWLGRYPTKGMFVDQDKMYRD-----TKAIFDELD-----IDIDPRAkvatLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15831001 185 LIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
35-252 |
1.75e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 35 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGkellgmkpdewravrsDIQMIFQDplASL 114
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEIIAEPLRTYHPKmsrqevRERVKAMMLKV---GLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 191
Cdd:PRK13546 97 SGQLTGIENIEFKMLCMGFK------RKEIKAMTPKIiefSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831001 192 VSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
34-230 |
4.34e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.84 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 34 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLvkatdghvaWLGKELLGMKPDEwravrsdiQMIFQDPLas 113
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL---------WPVYGGRLTKPAK--------GKLFYVPQ-- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 lNPRMTIG---EIIAEPLRTYhpKMSRQEVRERVKAMMLKVGLLPNLINR---------YPHEFSGGQCQRIGIARALIL 181
Cdd:TIGR00954 523 -RPYMTLGtlrDQIIYPDSSE--DMKRRGLSDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15831001 182 EPKLIICDEPVSALDVSIQAQVVNLLqqlqREMGLSLIFIAHDLAVVKH 230
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
39-246 |
7.62e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVrsdIQMIFQDplASLNPRM 118
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL---FSAVFTD--FHLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIAEPLRTYHPKMSRQEVRERVKammLKVGLLPNLinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 198
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLE---LEDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15831001 199 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 246
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
45-221 |
8.54e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 45 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG-------HVAWLGKE-LLGMKPDEWRavRSDIQMIFQDPLaslNP 116
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITRLSFEqLQKLVSDEWQ--RNNTDMLSPGED---DT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 117 RMTIGEIIAEplrtyhpkmsrqEVRERVKAMML--KVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:PRK10938 99 GRTTAEIIQD------------EVKDPARCEQLaqQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180
....*....|....*....|....*..
gi 15831001 195 LDVSIQAQVVNLLQQLQREmGLSLIFI 221
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-292 |
1.45e-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: 56.56 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 39 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLgmkpdewravrSDIQMIFQDplASLNPRM 118
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-----------TNISDVHQN--MGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 -TIGEIIA--EPLRTYHP--KMSRQEVrERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 193
Cdd:TIGR01257 2021 dAIDDLLTgrEHLYLYARlrGVPAEEI-EKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 194 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVPIPD- 272
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDl 2178
|
250 260
....*....|....*....|.
gi 15831001 273 -PDLekNKTIQLLEGELPSPI 292
Cdd:TIGR01257 2179 lPDL--NPVEQFFQGNFPGSV 2197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
40-248 |
3.28e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGlvkatdghvawlgkELLGMKPDEWRAVRSDIQmIFQDPLASLNPRMT 119
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--------------DLTGGGAPRGARVTGDVT-LNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 igeiiaEPLRTYHPKMSRQ----EVRERVkammlkvgllpnLINRYPH-------------------------------- 163
Cdd:PRK13547 82 ------ARLRAVLPQAAQPafafSAREIV------------LLGRYPHarragalthrdgeiawqalalagatalvgrdv 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 164 -EFSGGQCQRIGIARAL---------ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 233
Cdd:PRK13547 144 tTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHAD 223
|
250
....*....|....*
gi 15831001 234 RVLVMYLGHAVELGT 248
Cdd:PRK13547 224 RIAMLADGAIVAHGA 238
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-255 |
3.70e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 23 IKDGkQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG-LVKATDGHVAWLGKEllgmkpdewrAVRS 101
Cdd:PLN03130 617 IKNG-YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTV----------AYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 102 DIQMIFQdplASLNPRMTIGEiiaeplrTYHPkmSRQEVRERVKAMMLKVGLLP----NLINRYPHEFSGGQCQRIGIAR 177
Cdd:PLN03130 686 QVSWIFN---ATVRDNILFGS-------PFDP--ERYERAIDVTALQHDLDLLPggdlTEIGERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 178 ALILEPKLIICDEPVSALDVSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
40-236 |
4.49e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 40 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHV--------AWLGKEL--LGMKPDEW-----RAVRSdiq 104
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlAWVNQETpaLPQPALEYvidgdREYRQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 105 miFQDPLASLNPRMTiGEIIAeplrTYHPKMSRQE---VRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALIL 181
Cdd:PRK10636 94 --LEAQLHDANERND-GHAIA----TIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 182 EPKLIICDEPVSALDVSiqaQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRVL 236
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKII 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
42-255 |
6.19e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL--LGMkpdewRAVRSDIQMIFQDP-LASLNPRM 118
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskFGL-----MDLRKVLGIIPQAPvLFSGTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIgeiiaEPLRTyHPKMSRQEVRERVKammlkvglLPNLINRYP-----------HEFSGGQCQRIGIARALILEPKLII 187
Cdd:PLN03130 1332 NL-----DPFNE-HNDADLWESLERAH--------LKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 188 CDEPVSALDVSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 255
Cdd:PLN03130 1398 LDEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
43-238 |
1.06e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEwrAVRSDIQMIFQDPLAS---LNPRMT 119
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE--AINHGFALVTEERRSTgiyAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 120 IGEIIAEpLRTYHPKMS-------RQEVRERVKAMMLKVGLLPNLINryphEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:PRK10982 345 FNSLISN-IRNYKNKVGlldnsrmKSDTQWVIDSMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15831001 193 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 238
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM 464
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
50-248 |
1.11e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.22 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKpdeWRAVRSDIQMIFQDPLA-------SLNPRMTIGE 122
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLDPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 iiaeplRTYHPKMSRQEVRERVKAMmlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaq 202
Cdd:cd03288 124 ------DRLWEALEIAQLKNMVKSL---PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831001 203 vvNLLQQ--LQREMGLSLIFIAHdlaVVKHI--SDRVLVMYLGHAVELGT 248
Cdd:cd03288 193 --NILQKvvMTAFADRTVVTIAH---RVSTIldADLVLVLSRGILVECDT 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-251 |
1.24e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 41 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKP-----------------DEWRAVRSDI 103
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAqdhaydfendltlfdwmSQWRQEGDDE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 104 QMIfqdplaslnpRMTIGEIIaeplrtyhpkMSRQEVRERVKAMmlkvgllpnlinryphefSGGQCQRIGIARALILEP 183
Cdd:PRK15064 416 QAV----------RGTLGRLL----------FSQDDIKKSVKVL------------------SGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 184 KLIICDEPVSALDV-SIQAqvvnLLQQLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVE-LGTYDE 251
Cdd:PRK15064 458 NVLVMDEPTNHMDMeSIES----LNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-224 |
3.00e-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: 51.86 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 33 PPKTlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHvAWLGKEL-LGMKP-----DEWRAVRSDIQMI 106
Cdd:TIGR03719 15 PPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIkVGYLPqepqlDPTKTVRENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 107 FQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQ-EVRERVKA-----MMLKVGLLPNLInRYP------HEFSGGQCQRIG 174
Cdd:TIGR03719 93 VAEIKDALDRFNEISAKYAEPDADFDKLAAEQaELQEIIDAadawdLDSQLEIAMDAL-RCPpwdadvTKLSGGERRRVA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15831001 175 IARALILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHD 224
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
37-252 |
5.50e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVTLRLYEGETLGVVGESGCgkSTFARAIIGLVKATD-GHVAWLGKELLGMKpdewRAVRSDI---QMIFQDPLA 112
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GA--A**RGALPAHV*GPDaGRRPWRF*TWCANR----RALRRTIg*hRPVR*GRRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIgEIIAEPLrtyhpKMSRQEVRERVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 192
Cdd:NF000106 100 SFSGRENL-YMIGR*L-----DLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 193 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 252
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
42-256 |
7.23e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 42 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKEL--LGMkpdewRAVRSDIQMIFQDP-LASLNPRM 118
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgaYGL-----RELRRQFSMIPQDPvLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 119 TIGEIIaeplrtyhpKMSRQEV---------RERV-------KAMMLKVGLlpnlinryphEFSGGQCQRIGIARALILE 182
Cdd:PTZ00243 1403 NVDPFL---------EASSAEVwaalelvglRERVasesegiDSRVLEGGS----------NYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831001 183 -PKLIICDEPVS----ALDVSIQAQVVNLLQqlqremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHNP 256
Cdd:PTZ00243 1464 gSGFILMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
54-238 |
7.25e-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: 48.47 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 54 GVVGESGCGKSTFARAIIglvkatdghvawlgKELLGMKPDEWRAVRSDIQMIFQDPLASLnprmtigeiiaeplrtyhp 133
Cdd:cd03238 25 VVTGVSGSGKSTLVNEGL--------------YASGKARLISFLPKFSRNKLIFIDQLQFL------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 134 kmsrqevrervkammLKVGL--LPnlINRYPHEFSGGQCQRIGIARALILEPK--LIICDEPVSALDVSIQAQVVNLLQQ 209
Cdd:cd03238 72 ---------------IDVGLgyLT--LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180
....*....|....*....|....*....
gi 15831001 210 LqREMGLSLIFIAHDLAVVKHiSDRVLVM 238
Cdd:cd03238 135 L-IDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-252 |
1.09e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKellgmkpdewravrsdiqmIFQDPLASLNPRMTIGE 122
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------------ISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIAEPLrtyhpkmSRQEVRER--VKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:TIGR01271 506 NIIFGL-------SYDEYRYTsvIKACQLEedIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 195 LDVSIQAQ-----VVNLLQQLQRemglslIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 252
Cdd:TIGR01271 579 LDVVTEKEifescLCKLMSNKTR------ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
43-229 |
4.67e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmkpDEWRAVRSDiQMIFQDPLASLNPRMTIGE 122
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQK-QLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 iiaEPLRTYHPKMSRQEVRERVKAMMLKvgllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 202
Cdd:PRK13540 94 ---NCLYDIHFSPGAVGITELCRLFSLE-----HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*..
gi 15831001 203 VVNLLQQLQREMGLSLIFIAHDLAVVK 229
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
166-255 |
7.89e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 166 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHIsDRVLVMYLGHA 243
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
90
....*....|..
gi 15831001 244 VELGTYDEVYHN 255
Cdd:PLN03232 818 KEEGTFAELSKS 829
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-252 |
9.91e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 37 LKAVDGVtlrLYEGETLGVVGESGCGKSTFARAI----IGLVKATDGHVAWLGKELLGMKPDewraVRSDIqmIFQDPLA 112
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKH----YRGDV--VYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 113 SLNPRMTIGEII--AEPLRTYHPK---MSRQEVRERVKAMML-----------KVGllpnliNRYPHEFSGGQCQRIGIA 176
Cdd:TIGR00956 148 VHFPHLTVGETLdfAARCKTPQNRpdgVSREEYAKHIADVYMatyglshtrntKVG------NDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 177 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREM-GLSLIFI------AHDLAvvkhisDRVLVMYLGHAVELGTY 249
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILdTTPLVAIyqcsqdAYELF------DKVIVLYEGYQIYFGPA 295
|
...
gi 15831001 250 DEV 252
Cdd:TIGR00956 296 DKA 298
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
115-238 |
1.24e-05 |
|
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: 45.71 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 115 NPRMTIGEI--IAEPLRTYHpkmSRQEVRERVKaMMLKVGLLPNLINRYPHEFSGGQCQRIGIARAL--ILEPKLIICDE 190
Cdd:cd03270 90 NPRSTVGTVteIYDYLRLLF---ARVGIRERLG-FLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDE 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15831001 191 PVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVM 238
Cdd:cd03270 166 PSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDI 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
43-109 |
1.85e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.33 E-value: 1.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELlgmKPDEWRAVRSDIQMIFQD 109
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYRQLFSAVFSD 414
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-197 |
5.44e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 5.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15831001 143 RVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 197
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-236 |
6.74e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 135 MSRQEVRERVKAM-MLKVGLLPnlINRYPHEFSGGQCQRIGIARALIL---EPKLIICDEPVSALDVSIQAQVVNLLQQL 210
Cdd:PRK00635 781 LDEPSIHEKIHALcSLGLDYLP--LGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL 858
|
90 100
....*....|....*....|....*.
gi 15831001 211 QREmGLSLIFIAHDLAVVKhISDRVL 236
Cdd:PRK00635 859 THQ-GHTVVIIEHNMHVVK-VADYVL 882
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
118-229 |
3.41e-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: 41.45 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 118 MTIGEiiAEPLRTYHPKmsrqeVRERVKAMMlKVGLLPNLINRYPHEFSGGQCQRIGIARALILE---PKLIICDEPVSA 194
Cdd:cd03271 131 MTVEE--ALEFFENIPK-----IARKLQTLC-DVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTG 202
|
90 100 110
....*....|....*....|....*....|....*
gi 15831001 195 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK 229
Cdd:cd03271 203 LHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
43-252 |
3.42e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.77 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 43 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKellgmkpdewravrsdiqMIFQDPLASLNPRMTIGE 122
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 123 IIAeplrtyhpKMSRQEVRER--VKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSA 194
Cdd:cd03291 118 IIF--------GVSYDEYRYKsvVKACQLEedITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831001 195 LDVSIQAQ-----VVNLLQQLQRemglslIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 252
Cdd:cd03291 190 LDVFTEKEifescVCKLMANKTR------ILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 245
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
53-266 |
4.92e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 53 LGVVGESGCGKSTFARAIIGLVKATDGHVawlgkellgmkpdeWRAVRSDIQMIFQ---DPL-ASLNPRMTIgeiiaepL 128
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQhhvDGLdLSSNPLLYM-------M 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 129 RTYhPKMSRQEVRervkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaQVVNLLQ 208
Cdd:PLN03073 597 RCF-PGVPEQKLR----AHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQ 668
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 209 QLQREMGlSLIFIAHDLAVVKHISDRVLVMYLGHAVElgtydevYHNPLHPYTRALMS 266
Cdd:PLN03073 669 GLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKVTP-------FHGTFHDYKKTLQS 718
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
141-223 |
6.97e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 141 RERVKAM--MLKVGLLPNLINRYPHEFSGGQcQRIG-IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLS 217
Cdd:PRK10938 376 RQQKLAQqwLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQ 454
|
....*.
gi 15831001 218 LIFIAH 223
Cdd:PRK10938 455 LLFVSH 460
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-244 |
7.79e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 10 VLLEIADLKVHFEIKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD--GHVAWLGKE 87
Cdd:NF040905 256 VVFEVKNWTVYHPLHPERK----------VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 88 LLGMKPDewRAVRSDIQMIFQDplaslnpRMTIGEIIAEPLRT-----YHPKMSR----QEVRERV------KAMMLK-- 150
Cdd:NF040905 326 VDVSTVS--DAIDAGLAYVTED-------RKGYGLNLIDDIKRnitlaNLGKVSRrgviDENEEIKvaeeyrKKMNIKtp 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 151 -----VGllpNLinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDL 225
Cdd:NF040905 397 svfqkVG---NL--------SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSEL 464
|
250
....*....|....*....
gi 15831001 226 AVVKHISDRVLVMYLGHAV 244
Cdd:NF040905 465 PELLGMCDRIYVMNEGRIT 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
166-233 |
7.79e-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: 7.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831001 166 SGGQCQRIGIARALILE---PKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK---HISD 233
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIKtadYIID 903
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-286 |
7.92e-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: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 114 LNPRmtiGEIIAEPLRtyhpkmsrQEVRERVKaMMLKVGLLPNLINRYPHEFSGGQCQRIGIARAL--ILEPKLIICDEP 191
Cdd:TIGR00630 450 LTPE---EKKIAEEVL--------KEIRERLG-FLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEP 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 192 VSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHiSDRVLVM------YLGHAVELGTYDEVYHNPlHPYTRALM 265
Cdd:TIGR00630 518 SIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANP-DSLTGQYL 594
|
170 180
....*....|....*....|....
gi 15831001 266 SA---VPIPDPDLEKNKTIQLLEG 286
Cdd:TIGR00630 595 SGrkkIEVPAERRPGNGKFLTLKG 618
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
166-322 |
2.06e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 166 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLqQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 245
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEF 861
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831001 246 LGTYDEVYHNPLHPYTRA-LMSAVPIPDPDLEKNKTIQLLEGELPSPINPPSGcvfrTRCPIAGPECAKTRPVLEGSF 322
Cdd:PTZ00243 862 SGSSADFMRTSLYATLAAeLKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVA----KQEGNAEGGDGAALDAAAGRL 935
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
50-200 |
2.70e-03 |
|
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: 39.51 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIIGLVkATDGHVAWLGKELLGMKPDEWRAVRSDI-QMIFqdpLASLNPRMTIgeiiaEPl 128
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIpQKVF---IFSGTFRKNL-----DP- 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 129 rtyHPKMSRQEVRERVKAMMLKvgllpNLINRYPHE-----------FSGGQCQRIGIARALILEPKLIICDEPVSALD- 196
Cdd:TIGR01271 1315 ---YEQWSDEEIWKVAEEVGLK-----SVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDp 1386
|
....
gi 15831001 197 VSIQ 200
Cdd:TIGR01271 1387 VTLQ 1390
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
53-73 |
7.10e-03 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 37.68 E-value: 7.10e-03
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
50-154 |
7.22e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 37.36 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831001 50 GETLGVVGESGCGKSTFARAIiglvkATdgHVAwLGKELLGMKP------------DEWRAVRSDIQMIFQDPlaSLNPR 117
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDL-----AV--AVA-TGRDWLGERRvkqgrvvylaaeDPRDGLRRRLKAIGAHL--GDEDA 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 15831001 118 MTIGEIIAEPLRTYHPKM-SRQEVRERVKAMMLKVGLL 154
Cdd:cd01125 71 ALAENLVIENLRGKPVSIdAEAPELERIIEELEGVRLI 108
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
53-73 |
7.47e-03 |
|
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.
Pssm-ID: 238984 [Multi-domain] Cd Length: 273 Bit Score: 37.70 E-value: 7.47e-03
|
| |
