|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-261 |
2.78e-117 |
|
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: 340.11 E-value: 2.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKP---TGGRLFFRGQDLTARGEAKD 85
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 86 EHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRqSGSRTDLAEEIARLLTSVGL-EPDLTRQKFPHELSGGQRQRV 164
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHG-GLSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250
....*....|....*..
gi 2006592715 245 SDPRHPYTRLLLSAVPD 261
Cdd:COG0444 240 ENPRHPYTRALLSSIPR 256
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-260 |
9.51e-115 |
|
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: 340.73 E-value: 9.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 3 AEANPVVTDAVIRLENIQRNF-----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDL 77
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 78 TARGEaKDEHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRQsGSRTDLAEEIARLLTSVGLEPDLtRQKFPHELS 157
Cdd:COG1123 330 TKLSR-RSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGL-LSRAERRERVAELLERVGLPPDL-ADRYPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 158 GGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEW 237
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
250 260
....*....|....*....|...
gi 2006592715 238 GDTDTVLSDPRHPYTRLLLSAVP 260
Cdd:COG1123 487 GPTEEVFANPQHPYTRALLAAVP 509
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-260 |
1.29e-112 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 328.61 E-value: 1.29e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNF-----------GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLT 78
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 79 ARGEAkDEHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRQsGSRTDLAEEIARLLTSVGLEPDlTRQKFPHELSG 158
Cdd:COG4608 84 GLSGR-ELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGL-ASKAERRERVAELLELVGLRPE-HADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 159 GQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260
....*....|....*....|..
gi 2006592715 239 DTDTVLSDPRHPYTRLLLSAVP 260
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVP 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-265 |
2.75e-101 |
|
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: 297.10 E-value: 2.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehQY 89
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----AF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRqsgsRTDLAEEIARLLTSVGLEPDLtRQKFPHELSGGQRQRVNIARA 169
Cdd:COG1124 78 RRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSF-LDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRH 249
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|....*.
gi 2006592715 250 PYTRLLLSAVPDGSRP 265
Cdd:COG1124 233 PYTRELLAASLAFERA 248
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-238 |
3.85e-101 |
|
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: 295.95 E-value: 3.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHq 88
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDLtRQKFPHELSGGQRQRVNIAR 168
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEV-LNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-262 |
4.90e-99 |
|
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: 301.22 E-value: 4.90e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 2 KAEANPVVTDA--VIRLENIQRNF-----------GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDkPTGG 68
Cdd:COG4172 262 RGDPRPVPPDAppLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 69 RLFFRGQDLTARGEAKDeHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDlT 148
Cdd:COG4172 341 EIRFDGQDLDGLSRRAL-RPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPA-A 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 149 RQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVV 228
Cdd:COG4172 419 RHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMV 498
|
250 260 270
....*....|....*....|....*....|....
gi 2006592715 229 MFAGQMVEWGDTDTVLSDPRHPYTRLLLSAVPDG 262
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLL 532
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-260 |
7.61e-88 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 265.67 E-value: 7.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 26 VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdEHQYRRAVQMVFQDPFSSLN 105
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEA-QKLLRQKIQIVFQNPYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPLQLHRQSgSRTDLAEEIARLLTSVGLEPDLTrQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSM 185
Cdd:PRK11308 107 PRKKVGQILEEPLLINTSL-SAAERREKALAMMAKVGLRPEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 186 LDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSAVP 260
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATP 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-282 |
7.95e-83 |
|
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: 259.23 E-value: 7.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLEN----IQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL----DKPTGGRLFFRGQDLTArg 81
Cdd:COG4172 3 SMPLLSVEDlsvaFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 82 eaKDEHQYRR----AVQMVFQDPFSSLNPAFTVSHHLARPLQLHRqSGSRTDLAEEIARLLTSVGLePDLTRQ--KFPHE 155
Cdd:COG4172 81 --LSERELRRirgnRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHR-GLSGAAARARALELLERVGI-PDPERRldAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 156 LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2006592715 236 EWGDTDTVLSDPRHPYTRLLLSAVPDGsRPFVTGGSARFLEQAEKVR 282
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLLAAEPRG-DPRPVPPDAPPLLEARDLK 282
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-260 |
1.65e-80 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 247.31 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTaRGEAKDEHQYRRAVQMVFQDPFSSLNPA 107
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL-GMKDDEWRAVRSDIQMIFQDPLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 FTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTrQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:PRK15079 115 MTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLI-NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 188 VSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSAVP 260
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-265 |
5.88e-69 |
|
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: 222.86 E-value: 5.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNF--GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTG---GRLFFRGQDLTARgeakD 85
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLEL----S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 86 EHQYRRAVQMVFQDPFSSLNPAfTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVN 165
Cdd:COG1123 78 EALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLS--RAEARARVLELLEAVGLERRLDR--YPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 166 IARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|
gi 2006592715 246 DPRhpytrlLLSAVPDGSRP 265
Cdd:COG1123 233 APQ------ALAAVPRLGAA 246
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
26-258 |
9.74e-67 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 209.69 E-value: 9.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 26 VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakdEHQYR-RAVQMVFQDPFSSL 104
Cdd:COG4167 26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG-----DYKYRcKHIRMIFQDPNTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 NPAFTVSHHLARPLQLHrqsgsrTDLAEE-----IARLLTSVGLEPDlTRQKFPHELSGGQRQRVNIARALAVAPSVLVA 179
Cdd:COG4167 101 NPRLNIGQILEEPLRLN------TDLTAEereerIFATLRLVGLLPE-HANFYPHMLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 180 DEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSA 258
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-301 |
1.02e-63 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 211.64 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 26 VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEhQYRRAVQMVFQDPFSSLN 105
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQ-ALRRDIQFIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPLQLHRQsGSRTDLAEEIARLLTSVGLEPDLTrQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSM 185
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGL-LPGKAAAARVAWLLERVGLLPEHA-WRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 186 LDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSAVP--DGS 263
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPvaDPS 573
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2006592715 264 RPFvtggSARFLEQAEKVRSLSR----PESTVIEQVGSNHFM 301
Cdd:PRK10261 574 RQR----PQRVLLSDDLPSNIHLrgeeVAAVSLQCVGPGHYV 611
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-238 |
1.18e-61 |
|
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: 194.66 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehqYRRAV 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLARPLQLHRqsGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVA 173
Cdd:cd03259 75 GMVFQDY--ALFPHLTVAENIAFGLKLRG--VPKAEIRARVRELLELVGLEGLLNR--YPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-261 |
1.25e-60 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 196.12 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCA-RIIARLDKP---TGGRLFFRGQDLTARGEA 83
Cdd:PRK11022 2 ALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSlAIMGLIDYPgrvMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 84 KDEHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHrQSGSRTDLAEEIARLLTSVGL-EPDLTRQKFPHELSGGQRQ 162
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVH-QGGNKKTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDT 242
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*....
gi 2006592715 243 VLSDPRHPYTRLLLSAVPD 261
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPE 259
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-259 |
6.28e-60 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 191.95 E-value: 6.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 1 MKAEANPVvtdavIRLENIQRNFGP----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRG-- 74
Cdd:COG4107 1 MTNEEQPL-----LSVRGLSKRYGPgcgtVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDrd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 75 ---QDLTARGEAKDEHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLhrqSGSR--TDLAEEIARLLTSVglEPDLTR 149
Cdd:COG4107 76 ggpRDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMA---AGERhyGDIRARALEWLERV--EIPLER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 150 QK-FPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVV 228
Cdd:COG4107 151 IDdLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMV 230
|
250 260 270
....*....|....*....|....*....|.
gi 2006592715 229 MFAGQMVEWGDTDTVLSDPRHPYTRLLLSAV 259
Cdd:COG4107 231 MKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-259 |
4.89e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 189.05 E-value: 4.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeaKDEHQYRRA 92
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK--KDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDpFSsLNPAFTVSHHLAR-PLQLHRQSgsrTDLAEEIAR-LLTSVGLEPDltRQKFPHELSGGQRQRVNIARAL 170
Cdd:COG1126 79 VGMVFQQ-FN-LFPHLTVLENVTLaPIKVKKMS---KAEAEERAMeLLERVGLADK--ADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHP 250
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*....
gi 2006592715 251 YTRLLLSAV 259
Cdd:COG1126 231 RTRAFLSKV 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
29-259 |
7.04e-59 |
|
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: 189.63 E-value: 7.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTaRGEAKDEHQYRRAVQMVFQDPFSSLNPAF 108
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY-QLDRKQRRAFRRDVQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQlHRQSGSRTDLAEEIARLLTSVGLEPDLTrQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:TIGR02769 106 TVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDA-DKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 189 SIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDpRHPYTRLLLSAV 259
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAV 253
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-265 |
7.64e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.83 E-value: 7.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEaKDEHQY 89
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE-RELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDP--FSSLnpafTVSHHLARPLQLhrqSG-SRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNI 166
Cdd:COG1135 81 RRKIGMIFQHFnlLSSR----TVAENVALPLEI---AGvPKAEIRKRVAELLELVGLS-DK-ADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
250
....*....|....*....
gi 2006592715 247 PRHPYTRLLLSAVPDGSRP 265
Cdd:COG1135 232 PQSELTRRFLPTVLNDELP 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-257 |
1.96e-58 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 195.69 E-value: 1.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLdKPTGGRLFFRGQDLTARGEaKDEHQYRRAV 93
Cdd:PRK15134 287 IRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLNR-RQLLPVRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPFSSLNPAFTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDlTRQKFPHELSGGQRQRVNIARALAVA 173
Cdd:PRK15134 365 QVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPE-TRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTR 253
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
....
gi 2006592715 254 LLLS 257
Cdd:PRK15134 524 QLLA 527
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-251 |
3.23e-58 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 190.31 E-value: 3.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehqY 89
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP------E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDPfsSLNPAFTVSHHLARPLQLHRQsgSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARA 169
Cdd:COG3842 76 KRNVGMVFQDY--ALFPHLTVAENVAFGLRMRGV--PKAEIRARVAELLELVGLEGLADR--YPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRH 249
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPAT 229
|
..
gi 2006592715 250 PY 251
Cdd:COG3842 230 RF 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
29-259 |
6.77e-58 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 187.20 E-value: 6.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTA--RGEAKDehqYRRAVQMVFQDPFSSLNP 106
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKA---FRRDIQMVFQDSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFTVSHHLARPLQlHRQSGSRTDLAEEIARLLTSVGLEPDLTrQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSML 186
Cdd:PRK10419 105 RKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVL-DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 187 DVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVE---WGDTDTVlsdpRHPYTRLLLSAV 259
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKLTF----SSPAGRVLQNAV 254
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-248 |
4.27e-57 |
|
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: 183.69 E-value: 4.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIqrNF---GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYR 90
Cdd:COG1122 1 IELENL--SFsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK----KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDPFSSL-NPafTVSHHLA---RPLQLhrqsgSRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNI 166
Cdd:COG1122 75 RKVGLVFQNPDDQLfAP--TVEEDVAfgpENLGL-----PREEIRERVEEALELVGLE-HL-ADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
..
gi 2006592715 247 PR 248
Cdd:COG1122 225 YE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-260 |
7.18e-57 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 186.47 E-value: 7.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL---DKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDP 100
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 101 FSSLNPAFTVSHHLARPLQLHRQSGSRTDLAEEIaRLLTSVGLEPDLTRQK-FPHELSGGQRQRVNIARALAVAPSVLVA 179
Cdd:PRK09473 107 MTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESV-RMLDAVKMPEARKRMKmYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 180 DEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSAV 259
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
.
gi 2006592715 260 P 260
Cdd:PRK09473 266 P 266
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-236 |
1.06e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 182.55 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDE 86
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 HQYRRAVQMVFQDPFssLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLtrQKFPHELSGGQRQRVNI 166
Cdd:COG1136 82 RLRRRHIGFVFQFFN--LLPELTALENVALPLLLAGVS--RKERRERARELLERVGLGDRL--DHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVE 236
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-229 |
2.79e-56 |
|
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: 181.15 E-value: 2.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQY 89
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQdpFSSLNPAFTVSHHLARPLQLhrqSGSRTDLAEEIAR-LLTSVGLEPDLTRqkFPHELSGGQRQRVNIAR 168
Cdd:cd03255 81 RRHIGFVFQ--SFNLLPDLTALENVELPLLL---AGVPKKERRERAEeLLERVGLGDRLNH--YPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIaTAAHVAEEIVVM 229
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-248 |
3.41e-56 |
|
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: 181.63 E-value: 3.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGP----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQ 88
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 yRRAVQMVFQ--DPFSSLnpafTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNI 166
Cdd:cd03258 81 -RRRIGMIFQhfNLLSSR----TVFENVALPLEIAGVP--KAEIEERVLELLELVGLED--KADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 2006592715 247 PR 248
Cdd:cd03258 232 PQ 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-276 |
2.07e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 187.61 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 31 GVSFSLFPGRALALVGESGCGKTTCARIIARLdKPT------GGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDPFSSL 104
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 NPAFTVSHHLARPLQLHRqsGSRTDLAE-EIARLLTSVGLEPDLTRQK-FPHELSGGQRQRVNIARALAVAPSVLVADEP 182
Cdd:PRK15134 106 NPLHTLEKQLYEVLSLHR--GMRREAARgEILNCLDRVGIRQAAKRLTdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 183 TSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSAVPDG 262
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSG 263
|
250
....*....|....
gi 2006592715 263 SRPFVTGGSARFLE 276
Cdd:PRK15134 264 DPVPLPEPASPLLD 277
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-289 |
2.11e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 180.29 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakd 85
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 86 ehqyRRAvqMVFQDPfsSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDltRQKFPHELSGGQRQRVN 165
Cdd:COG1116 81 ----DRG--VVFQEP--ALLPWLTVLDNVALGLELRGVP--KAERRERARELLELVGLAGF--EDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 166 IARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFA--GQMVEwgDTDTV 243
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE--EIDVD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2006592715 244 LSDPRHPYTRlllsavpdgsrpfvtgGSARFLEQAEKVRSLSRPES 289
Cdd:COG1116 227 LPRPRDRELR----------------TSPEFAALRAEILDLLREEA 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-243 |
2.28e-55 |
|
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: 179.30 E-value: 2.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL-----DKPTGGRLFFRGQDLTARGEakDEHQ 88
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV--DVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPfsslNP-AFTVSHHLARPLQLHRqSGSRTDLAEEIARLLTSVGLEPDLTRQKFPHELSGGQRQRVNIA 167
Cdd:cd03260 79 LRRRVGMVFQKP----NPfPGSIYDNVAYGLRLHG-IKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKREndLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTV 243
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-253 |
2.10e-54 |
|
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: 177.09 E-value: 2.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEaKDEHQY 89
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSE-KELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDP--FSSLnpafTVSHHLARPLQLHrqsgsrTDLAEEIAR-----LLTSVGLEPdlTRQKFPHELSGGQRQ 162
Cdd:COG1127 81 RRRIGMLFQGGalFDSL----TVFENVAFPLREH------TDLSEAEIRelvleKLELVGLPG--AADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDT 242
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
250
....*....|..
gi 2006592715 243 VL-SDprHPYTR 253
Cdd:COG1127 229 LLaSD--DPWVR 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-234 |
2.35e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.77 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRAV 93
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA----MPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPFsslnpAF--TVSHHLARPLQLHRQSGSRtdlaEEIARLLTSVGLEPDLTRQKFpHELSGGQRQRVNIARALA 171
Cdd:COG4619 77 AYVPQEPA-----LWggTVRDNLPFPFQLRERKFDR----ERALELLERLGLPPDILDKPV-ERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-229 |
4.60e-54 |
|
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: 175.74 E-value: 4.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdehqy 89
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 rRAVQMVFQDPfsSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARA 169
Cdd:cd03293 73 -PDRGYVFQQD--ALLPWLTVLDNVALGLELQGVP--KAEARERAEELLELVGLSG--FENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVM 229
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
31-258 |
7.38e-54 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 175.63 E-value: 7.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 31 GVSFSLFPGRALALVGESGCGKT-TCARIIARLDK---PTGGRLFFRGQDLTArgeakdeHQYR-RAVQMVFQDPFSSLN 105
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPgltQTSGEILLDGRPLLP-------LSIRgRHIATIMQNPRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPLQLHrqsGSRTDLAEE-IARLLTSVGLE-PDLTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPT 183
Cdd:TIGR02770 77 PLFTMGNHAIETLRSL---GKLSKQARAlILEALEAVGLPdPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 184 SMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSA 258
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-260 |
1.81e-53 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 184.29 E-value: 1.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 20 QRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGR-------LFFRGQDLTARGEAKDEhQYRRA 92
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmlLRRRSRQVIELSEQSAA-QMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 ----VQMVFQDPFSSLNPAFTVSHHLARPLQLHrQSGSRTDLAEEIARLLTSVGL-EPDLTRQKFPHELSGGQRQRVNIA 167
Cdd:PRK10261 102 rgadMAMIFQEPMTSLNPVFTVGEQIAESIRLH-QGASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
250
....*....|...
gi 2006592715 248 RHPYTRLLLSAVP 260
Cdd:PRK10261 261 QHPYTRALLAAVP 273
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-238 |
6.80e-53 |
|
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: 173.19 E-value: 6.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehqYRRAV 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP------HKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVA 173
Cdd:cd03300 75 NTVFQN--YALFPHLTVFENIAFGLRLKKLP--KAEIKERVAEALDLVQLEG--YANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-266 |
7.31e-53 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 175.86 E-value: 7.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKP----TGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQD 99
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 100 PFSSLNPAFTVSHHLARPLQLHRQSGS----RTDLAEEIARLLTSVGL-EPDLTRQKFPHELSGGQRQRVNIARALAVAP 174
Cdd:COG4170 98 PSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIkDHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 175 SVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRL 254
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257
|
250
....*....|..
gi 2006592715 255 LLSAVPDGSRPF 266
Cdd:COG4170 258 LLRSMPDFRQPL 269
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-259 |
8.83e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 176.14 E-value: 8.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEaKDEHQ 88
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE-KELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDpFSSLNpAFTVSHHLARPLQLhrQSGSRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNIAR 168
Cdd:PRK11153 80 ARRQIGMIFQH-FNLLS-SRTVFDNVALPLEL--AGTPKAEIKARVTELLELVGLS-DK-ADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPR 248
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|.
gi 2006592715 249 HPYTRLLLSAV 259
Cdd:PRK11153 234 HPLTREFIQST 244
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-252 |
5.80e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 174.18 E-value: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDehqyrRAV 93
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRE-----RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLA-----RPLqlhrqsgSRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNIAR 168
Cdd:COG1118 78 GFVFQHY--ALFPHMTVAENIAfglrvRPP-------SKAEIRARVEELLELVQLE-GL-ADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPR 248
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....
gi 2006592715 249 HPYT 252
Cdd:COG1118 227 TPFV 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-253 |
8.00e-52 |
|
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: 170.38 E-value: 8.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHqYRRAV 93
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYR-LRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDP--FSSLnpafTVSHHLARPLQLHRQsgsrtDLAEEIARL----LTSVGLEPDltRQKFPHELSGGQRQRVNIA 167
Cdd:cd03261 80 GMLFQSGalFDSL----TVFENVAFPLREHTR-----LSEEEIREIvlekLEAVGLRGA--EDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 168 RALAVAPSVLVADEPTSMLDvSIRKD-ILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:cd03261 149 RALALDPELLLYDEPTAGLD-PIASGvIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
....*..
gi 2006592715 247 PrHPYTR 253
Cdd:cd03261 228 D-DPLVR 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-253 |
1.37e-50 |
|
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: 167.48 E-value: 1.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVH-ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRA 92
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE----QDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDpfSSLNPAFTVSHHLARPLQLhrQSGSRTDLAEEIARLLTSVGLEPDLTRQKFPHELSGGQRQRVNIARALAV 172
Cdd:cd03295 77 IGYVIQQ--IGLFPHMTVEENIALVPKL--LKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYT 252
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFV 232
|
.
gi 2006592715 253 R 253
Cdd:cd03295 233 A 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-251 |
4.17e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 169.48 E-value: 4.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgEAKDehqyrR 91
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL-PPKD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPfsSLNPAFTVSHHLARPLQLHRQSGSRTD-LAEEIARLLtsvGLEPDLTRqkFPHELSGGQRQRVNIARAL 170
Cdd:COG3839 76 NIAMVFQSY--ALYPHMTVYENIAFPLKLRKVPKAEIDrRVREAAELL---GLEDLLDR--KPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLD----VSIRKDI--LHllatvkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:COG3839 149 VREPKVFLLDEPLSNLDaklrVEMRAEIkrLH------RRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELY 222
|
....*..
gi 2006592715 245 SDPRHPY 251
Cdd:COG3839 223 DRPANLF 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-251 |
6.69e-50 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 165.59 E-value: 6.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakdeHQYRRAV 93
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQLHRQSG--SRTDLAEEIARLLTSVGLepDLTRQKFPHELSGGQRQRVNIARALA 171
Cdd:cd03296 77 GFVFQH--YALFRHMTVFDNVAFGLRVKPRSErpPEAEIRAKVHELLKLVQL--DWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPY 251
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-259 |
3.90e-49 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 164.33 E-value: 3.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ-----DLTARGEAKDEHQY 89
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDPFSSLNPAFTVSHHLARPL--QLHRQSGsrtDLAEEIARLLTSVglEPDLTR-QKFPHELSGGQRQRVNI 166
Cdd:PRK11701 88 RTEWGFVHQHPRDGLRMQVSAGGNIGERLmaVGARHYG---DIRATAGDWLERV--EIDAARiDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDD 242
|
250
....*....|...
gi 2006592715 247 PRHPYTRLLLSAV 259
Cdd:PRK11701 243 PQHPYTQLLVSSV 255
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
28-233 |
2.54e-48 |
|
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: 160.33 E-value: 2.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRAVQMVFQDPFSSL-NP 106
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK----LSLKELRRKVGLVFQNPDDQFfGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 afTVSHHLA---RPLQLhrqsgSRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPT 183
Cdd:cd03225 92 --TVEEEVAfglENLGL-----PEEEIEERVEEALELVGLE-GL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2006592715 184 SMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-245 |
2.71e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 2.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeAKDEHQYRRAV 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-----ARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIARALAVA 173
Cdd:COG1131 76 GYVPQEP--ALYPDLTVRENLRFFARLYGLP--RKEARERIDELLELFGLTDAADRK--VGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-233 |
3.62e-48 |
|
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: 158.89 E-value: 3.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHqyRRAV 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL--RRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVshhlarplqlhrqsgsrtdlaeeiarlltsvglepdltRQKFPHELSGGQRQRVNIARALAVA 173
Cdd:cd03229 79 GMVFQDF--ALFPHLTV--------------------------------------LENIALGLSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-233 |
3.80e-48 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 160.00 E-value: 3.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeaKDEHQYRRAV 93
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK--KNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpFSsLNPAFTVSHHLARPLQLHRqsGSRTDLAEEIAR-LLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAV 172
Cdd:cd03262 79 GMVFQQ-FN-LFPHLTVLENITLAPIKVK--GMSKAEAEERALeLLEKVGLAD--KADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-258 |
7.14e-48 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 161.11 E-value: 7.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 26 VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeakDEHQYR-RAVQMVFQDPFSSL 104
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-----GDYSYRsQRIRMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 NPAFTVSHHLARPLQLHrqsgsrTDLAEE-----IARLLTSVGLEPDLTrQKFPHELSGGQRQRVNIARALAVAPSVLVA 179
Cdd:PRK15112 101 NPRQRISQILDFPLRLN------TDLEPEqrekqIIETLRQVGLLPDHA-SYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 180 DEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSA 258
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-238 |
6.35e-47 |
|
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: 157.03 E-value: 6.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgEAKDehqyrRAV 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKD-----RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSRTDL-AEEIARLLtsvGLEPDLTRQkfPHELSGGQRQRVNIARALAV 172
Cdd:cd03301 75 AMVFQN--YALYPHMTVYDNIAFGLKLRKVPKDEIDErVREVAELL---QIEHLLDRK--PKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
14-259 |
1.25e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 156.88 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakDEHQYRRAV 93
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDAT------RVHARDRKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSRTDlaEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVA 173
Cdd:TIGR00968 75 GFVFQH--YALFKHLTVRDNIAFGLEIRKHPKAKIK--ARVEELLELVQLEGLGDR--YPNQLSGGQRQRVALARALAVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTR 253
Cdd:TIGR00968 149 PQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVM 228
|
....*.
gi 2006592715 254 LLLSAV 259
Cdd:TIGR00968 229 SFLGEV 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-296 |
4.69e-46 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 159.05 E-value: 4.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehqyr 90
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDpfSSLNPAFTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLePDLTRqKFPHELSGGQRQRVNIARAL 170
Cdd:TIGR03265 76 RDYGIVFQS--YALFPNLTVADNIA--YGLKNRGMGRAEVAERVAELLDLVGL-PGSER-KYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHP 250
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 251 Y-------TRLLLSAVPDGSRPFVTGGS---ARFLEQA-EKVRSLSRPESTVIEQVG 296
Cdd:TIGR03265 230 FvadfvgeVNWLPGTRGGGSRARVGGLTlacAPGLAQPgASVRLAVRPEDIRVSPAG 286
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-247 |
1.98e-45 |
|
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: 157.18 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDL--TARGEAKDEHqyRRAVQMVFQDPfsSLNPAFT 109
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPH--RRRIGYVFQEA--RLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 110 VSHHLARPLQLHRQSGSRTDLaEEIARLLtsvGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVS 189
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISF-DEVVELL---GIGHLLDR--RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 190 IRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-245 |
4.63e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 153.28 E-value: 4.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehQYRRA 92
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR----ELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDPfsSLNPAFTVSH--HLAR-PLQLHRQSGSRTDLaEEIARLLTSVGLEpDLTRQKFpHELSGGQRQRVNIARA 169
Cdd:COG1120 77 IAYVPQEP--PAPFGLTVRElvALGRyPHLGLFGRPSAEDR-EAVEEALERTGLE-HLADRPV-DELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-254 |
4.70e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 150.63 E-value: 4.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDltARGEAKDEHQYRRA 92
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK--VNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDpFSsLNPAFTVSHHLA-RPLQLHRQSgsRTDlAEEIAR-LLTSVGLEPDLtrQKFPHELSGGQRQRVNIARAL 170
Cdd:PRK09493 79 AGMVFQQ-FY-LFPHLTALENVMfGPLRVRGAS--KEE-AEKQAReLLAKVGLAERA--HHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPrhP 250
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP--P 228
|
....
gi 2006592715 251 YTRL 254
Cdd:PRK09493 229 SQRL 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-246 |
6.28e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.04 E-value: 6.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIqrNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeaKDEHQY 89
Cdd:TIGR04520 1 IEVENV--SFsypeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT------LDEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 ---RRAVQMVFQdpfsslNP-----AFTVSHHLA---RPLQLhrqsgSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSG 158
Cdd:TIGR04520 73 weiRKKVGMVFQ------NPdnqfvGATVEDDVAfglENLGV-----PREEMRKRVDEALKLVGMEDFRDRE--PHLLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 159 GQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEG 218
|
....*...
gi 2006592715 239 DTDTVLSD 246
Cdd:TIGR04520 219 TPREIFSQ 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-184 |
1.76e-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: 145.87 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQYRRAVQMVFQDPFssLNPAF 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD----ERKSLRKEIGYVFQDPQ--LFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 109 TVSHHLARPLQLHRQsgSRTDLAEEIARLLTSVGLEPDLTR--QKFPHELSGGQRQRVNIARALAVAPSVLVADEPTS 184
Cdd:pfam00005 75 TVRENLRLGLLLKGL--SKREKDARAEEALEKLGLGDLADRpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-258 |
2.78e-43 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 149.08 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIqRNFGPVHALKGVSFSLFPGRALALVGESGCGKT-TCARIIARLD---KPTGGRLFFRGQDLTA---RGeakd 85
Cdd:PRK10418 4 QIELRNI-ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPcalRG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 86 ehqyrRAVQMVFQDPFSSLNPAFTVSHHLARPLqlhRQSGSRTDLAEeIARLLTSVGLE-PDLTRQKFPHELSGGQRQRV 164
Cdd:PRK10418 79 -----RKIATIMQNPRSAFNPLHTMHTHARETC---LALGKPADDAT-LTAALEAVGLEnAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....
gi 2006592715 245 SDPRHPYTRLLLSA 258
Cdd:PRK10418 230 NAPKHAVTRSLVSA 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-248 |
5.34e-43 |
|
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: 147.58 E-value: 5.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdEHQ-YRRA 92
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----PHEiARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDP--FSSL----NPAFTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNI 166
Cdd:cd03219 77 IGRTFQIPrlFPELtvleNVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRP--AGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
..
gi 2006592715 247 PR 248
Cdd:cd03219 234 PR 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-253 |
1.32e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.11 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 4 EANPVVTDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDK--P---TGGRLFFRGQDLT 78
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 79 ARGEakDEHQYRRAVQMVFQDPfsslNP-AFTVSHHLARPLQLHRQSgSRTDLAEEIARLLTSVGL----EPDLtrQKFP 153
Cdd:COG1117 82 DPDV--DVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIK-SKSELDEIVEESLRKAALwdevKDRL--KKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 154 HELSGGQRQRVNIARALAVAPSVLVADEPTSMLD-VSIRKdILHLLATVKreNDLAMLYITHDIATAAHVAEEIVVMFAG 232
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLG 229
|
250 260
....*....|....*....|.
gi 2006592715 233 QMVEWGDTDTVLSDPRHPYTR 253
Cdd:COG1117 230 ELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-253 |
2.08e-42 |
|
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: 147.02 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 17 ENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMV 96
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 97 FQDpFSsLNPAFTVSHHLARPLQLhrQSGSRTDLAEEIARLLTSVGLEPDLtrQKFPHELSGGQRQRVNIARALAVAPSV 176
Cdd:cd03294 108 FQS-FA-LLPHRTVLENVAFGLEV--QGVPRAEREERAAEALELVGLEGWE--HKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 177 LVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTR 253
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-236 |
3.02e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.20 E-value: 3.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVH-ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtARGEAKDEHQYRR 91
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL-SRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDpFSSLnPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNIARALA 171
Cdd:COG2884 80 RIGVVFQD-FRLL-PDRTVYENVALPLRVTGKS--RKEIRRRVREVLDLVGLS-DK-AKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVE 236
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-245 |
7.67e-42 |
|
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: 144.62 E-value: 7.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeAKDEHQYRRA 92
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-----RKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDPFssLNPAFTVSHHLARPLQLHRQSGSrtDLAEEIARLLTSVGLEPDLTRQKfpHELSGGQRQRVNIARALAV 172
Cdd:COG4555 76 IGVLPDERG--LYDRLTVRENIRYFAELYGLFDE--ELKKRIEELIELLGLEEFLDRRV--GELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-236 |
8.55e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 144.03 E-value: 8.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENI----QRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQ 88
Cdd:TIGR02211 1 LLKCENLgkryQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQdpFSSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLTrqKFPHELSGGQRQRVNIAR 168
Cdd:TIGR02211 81 RNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKS--VKEAKERAYEMLEKVGLEHRIN--HRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVE 236
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
12-259 |
1.51e-41 |
|
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: 144.20 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQD-----LTARGEAKDE 86
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 HQYRRAVQMVFQDPFSSLNPAFTVSHHLA-RPLQL-HRQSGsrtDLAEEIARLLTSVGLEPDLTRQKfPHELSGGQRQRV 164
Cdd:TIGR02323 82 RLMRTEWGFVHQNPRDGLRMRVSAGANIGeRLMAIgARHYG---NIRATAQDWLEEVEIDPTRIDDL-PRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
250
....*....|....*
gi 2006592715 245 SDPRHPYTRLLLSAV 259
Cdd:TIGR02323 238 DDPQHPYTQLLVSSI 252
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-236 |
2.00e-41 |
|
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: 143.34 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 7 PVVTDAVIRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGE 82
Cdd:COG4181 2 SSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 83 akDEHQYRRAVQM--VFQDpfSSLNPAFTVSHHLARPLQLhrqsGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQ 160
Cdd:COG4181 82 --DARARLRARHVgfVFQS--FQLLPTLTALENVMLPLEL----AGRRDARARARALLERVGLGHRLDH--YPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 161 RQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVE 236
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-256 |
6.59e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 145.61 E-value: 6.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTaRGEAKDehqyrRAV 93
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQL--HRQSGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALA 171
Cdd:PRK10851 77 GFVFQH--YALFRHMTVFDNIAFGLTVlpRRERPNAAAIKAKVTQLLEMVQLAHLADR--YPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLsdpRHPY 251
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW---REPA 229
|
....*
gi 2006592715 252 TRLLL 256
Cdd:PRK10851 230 TRFVL 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-247 |
1.12e-40 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 141.70 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHaLKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargEAKDEhqyRRAV 93
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT---NLPPE---KRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSRTDL-AEEIARLLtsvGLEPDLTRQkfPHELSGGQRQRVNIARALAV 172
Cdd:cd03299 74 SYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIERkVLEIAEML---GIDHLLNRK--PETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-248 |
2.27e-40 |
|
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: 141.33 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdehQY 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP------PH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQ-MV--FQDP--FSSLnpafTV-------------SHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDltRQK 151
Cdd:COG0411 75 RIARLgIArtFQNPrlFPEL----TVlenvlvaaharlgRGLLAALLRLPRARREEREARERAEELLERVGLADR--ADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 152 FPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFA 231
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
250
....*....|....*..
gi 2006592715 232 GQMVEWGDTDTVLSDPR 248
Cdd:COG0411 229 GRVIAEGTPAEVRADPR 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-235 |
5.22e-40 |
|
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: 137.56 E-value: 5.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARG--EAKdehqyRR 91
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASprDAR-----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQdpfsslnpaftvshhlarplqlhrqsgsrtdlaeeiarlltsvglepdltrqkfpheLSGGQRQRVNIARALA 171
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 172 VAPSVLVADEPTSMLDVsirKDILHLLATVKR--ENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03216 99 RNARLLILDEPTAALTP---AEVERLFKVIRRlrAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-233 |
7.29e-40 |
|
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: 136.99 E-value: 7.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRAVQ 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK----LPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 95 MVFQdpfsslnpaftvshhlarplqlhrqsgsrtdlaeeiarlltsvglepdltrqkfpheLSGGQRQRVNIARALAVAP 174
Cdd:cd00267 77 YVPQ---------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 175 SVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-265 |
1.52e-39 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 141.09 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKP----TGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQD 99
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 100 PFSSLNPAFTVSHHLARPL-------QLHRQSGSRTDLAEEiarLLTSVGLE--PDLTRQkFPHELSGGQRQRVNIARAL 170
Cdd:PRK15093 98 PQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWRKRRAIE---LLHRVGIKdhKDAMRS-FPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHP 250
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHP 253
|
250
....*....|....*
gi 2006592715 251 YTRLLLSAVPDGSRP 265
Cdd:PRK15093 254 YTQALIRAIPDFGSA 268
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-235 |
1.74e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 138.65 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNF-GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeAKDEHQYR 90
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR-GRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDpfsslnpaftvsHHLARPL---------QLHRQSGSRTDL----AEEIAR---LLTSVGLEPDLTRQkfPH 154
Cdd:COG3638 80 RRIGMIFQQ------------FNLVPRLsvltnvlagRLGRTSTWRSLLglfpPEDRERaleALERVGLADKAYQR--AD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
.
gi 2006592715 235 V 235
Cdd:COG3638 226 V 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-258 |
3.40e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.58 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGpvHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehqyrRAV 93
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDP--FSSLnpafTVSHHLA---RP-LQLhrqsgSRTDLAEeIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIA 167
Cdd:COG3840 74 SMLFQENnlFPHL----TVAQNIGlglRPgLKL-----TAEQRAQ-VEQALERVGLAGLLDR--LPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
250
....*....|.
gi 2006592715 248 RHPYTRLLLSA 258
Cdd:COG3840 222 PPPALAAYLGI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-233 |
3.47e-39 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 135.59 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENI--QRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeAKDEHQYRR 91
Cdd:cd03228 1 IEFKNVsfSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR----DLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFssLnpaFtvshhlarplqlhrqSGSrtdLAEEIarlltsvglepdltrqkfpheLSGGQRQRVNIARALA 171
Cdd:cd03228 77 NIAYVPQDPF--L---F---------------SGT---IRENI---------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLAtvKRENDLAMLYITHDIATAAHvAEEIVVMFAGQ 233
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALR--ALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-235 |
4.71e-39 |
|
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: 137.31 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFG-PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEaKDEHQYRRA 92
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG-KALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDPfsSLNPAFTV----------SHHLARPLqlhrqSGSRTDLAEEIAR-LLTSVGLEpDLTRQKfPHELSGGQR 161
Cdd:cd03256 80 IGMIFQQF--NLIERLSVlenvlsgrlgRRSTWRSL-----FGLFPKEEKQRALaALERVGLL-DKAYQR-ADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-252 |
7.81e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 137.35 E-value: 7.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL-----DKPTGGRLFFRGQDLTArgeaKDE 86
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFK----MDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 HQYRRAVQMVFQDPfsslNPAFTVS--HHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDL-TRQKFPH-ELSGGQRQ 162
Cdd:PRK14247 78 IELRRRVQMVFQIP----NPIPNLSifENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVkDRLDAPAgKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDT 242
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|
gi 2006592715 243 VLSDPRHPYT 252
Cdd:PRK14247 232 VFTNPRHELT 241
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-227 |
8.15e-39 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 135.82 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 16 LENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQM 95
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 96 VFQDpFSSLNPAfTVSHHLARPLQLHRqsGSRTDLAEEIARLLTSVGLEPDLtrQKFPHELSGGQRQRVNIARALAVAPS 175
Cdd:TIGR03608 81 LFQN-FALIENE-TVEENLDLGLKYKK--LSKKEKREKKKEALEKVGLNLKL--KQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 176 VLVADEPTSMLDVSIRKDILHLLATVKRENDLaMLYITHDIAtAAHVAEEIV 227
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKT-IIIVTHDPE-VAKQADRVI 204
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-247 |
1.39e-38 |
|
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: 137.20 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArGEAKDEHQ 88
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA-KKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFSSLnpaF--TVSHHLA-RPLQLhrqsGSRTDLAEEIAR-LLTSVGLEPDLtRQKFPHELSGGQRQRV 164
Cdd:TIGR04521 80 LRKKVGLVFQFPEHQL---FeeTVYKDIAfGPKNL----GLSEEEAEERVKeALELVGLDEEY-LERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
...
gi 2006592715 245 SDP 247
Cdd:TIGR04521 232 SDV 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-238 |
1.50e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.45 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF--GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakDEH--Q 88
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS------EETvwD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFSSLNPAfTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIAR 168
Cdd:PRK13635 79 VRRQVGMVFQNPDNQFVGA-TVQDDVA--FGLENIGVPREEMVERVDQALRQVGMEDFLNRE--PHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-234 |
1.89e-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: 133.68 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeaKDEHQYRRAV 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-----KEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLarplqlhrqsgsrtdlaeeiarlltsvglepdltrqkfphELSGGQRQRVNIARALAVA 173
Cdd:cd03230 76 GYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-235 |
5.07e-38 |
|
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: 133.96 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 33 SFSL-----FPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDpfSSLNPA 107
Cdd:cd03297 12 DFTLkidfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 FTVSHHLARPLQLHRQsGSRTDLAEEIarlLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:cd03297 90 LNVRENLAFGLKRKRN-REDRISVDEL---LDLLGLDHLLNR--YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2006592715 188 VSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-235 |
1.31e-37 |
|
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: 133.96 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGP-VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeAKDEHQYRR 91
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR-GKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDpfSSLNPAFTVSHHLARPlQLHRQSGSRTDLA----EEIAR---LLTSVGLEpDLTRQKfPHELSGGQRQRV 164
Cdd:TIGR02315 80 RIGMIFQH--YNLIERLTVLENVLHG-RLGYKPTWRSLLGrfseEDKERalsALERVGLA-DKAYQR-ADQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-235 |
1.58e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.40 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakdehqyrravq 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 95 mvfqdpfsslnpaftvshhlarplqlhrqsgSRTDLAEEIARL---LTSVGLEpDLTRQKFpHELSGGQRQRVNIARALA 171
Cdd:cd03214 67 -------------------------------SPKELARKIAYVpqaLELLGLA-HLADRPF-NELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-243 |
2.61e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 138.61 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARG--EAKdeh 87
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDAQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 qyRRAVQMVFQDPfsSLNPAFTV------SHHLARPLQLHRQsgsrtDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQR 161
Cdd:COG1129 78 --AAGIAIIHQEL--NLVPNLSVaeniflGREPRRGGLIDWR-----AMRRRARELLARLGLDIDPDTP--VGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSMLDvsiRKDILHLLATVK--RENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGD 239
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
....
gi 2006592715 240 TDTV 243
Cdd:COG1129 224 VAEL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-247 |
4.07e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakdehqy 89
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQdpFSSLNPAF------TVSHHLARPLQLHRqSGSRTDlAEEIARLLTSVGLEpDLTRQKFpHELSGGQRQR 163
Cdd:COG1121 74 RRRIGYVPQ--RAEVDWDFpitvrdVVLMGRYGRRGLFR-RPSRAD-REAVDEALERVGLE-DLADRPI-GELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMfAGQMVEWGDTDTV 243
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEV 225
|
....
gi 2006592715 244 LSDP 247
Cdd:COG1121 226 LTPE 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-267 |
4.49e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 133.06 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdeh 87
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 qyRRAVqmVFQDpfSSLNPAFTVSHHLARPLQLHRQS-GSRTDLAEEIARLltsVGLEPdlTRQKFPHELSGGQRQRVNI 166
Cdd:COG4525 77 --DRGV--VFQK--DALLPWLNVLDNVAFGLRLRGVPkAERRARAEELLAL---VGLAD--FARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVM--------------FAG 232
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspgpgriverleldFSR 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 2006592715 233 QMVEWGDTDTVLSDPRHPYTR-LLLSAVPDGSRPFV 267
Cdd:COG4525 226 RFLAGEDARAIKSDPAFIALReELLDIIFAQEEAEA 261
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
10-258 |
4.94e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 132.62 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARG------EA 83
Cdd:COG4598 5 APPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 84 KDEHQ---YRRAVQMVFQdpfsSLN--PAFTVSHHL-ARPLQLHRQSgsRTDLAEEIARLLTSVGLEPdlTRQKFPHELS 157
Cdd:COG4598 85 ADRRQlqrIRTRLGMVFQ----SFNlwSHMTVLENViEAPVHVLGRP--KAEAIERAEALLAKVGLAD--KRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 158 GGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHllatVKRenDLA-----MLYITHDIATAAHVAEEIVVMFAG 232
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLK----VMR--DLAeegrtMLVVTHEMGFARDVSSHVVFLHQG 230
|
250 260
....*....|....*....|....*.
gi 2006592715 233 QMVEWGDTDTVLSDPRHPYTRLLLSA 258
Cdd:COG4598 231 RIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
13-235 |
7.66e-37 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 130.91 E-value: 7.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGP----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEaKDEHQ 88
Cdd:TIGR02982 1 VISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASK-KQLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDpfSSLNPAFTVSHHLARPLQLHRQSgSRTDLAEEIARLLTSVGLEPDLtrQKFPHELSGGQRQRVNIAR 168
Cdd:TIGR02982 80 LRRRIGYIFQA--HNLLGFLTARQNVQMALELQPNL-SYQEARERARAMLEAVGLGDHL--NYYPHNLSGGQKQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDiATAAHVAEEIVVMFAGQMV 235
Cdd:TIGR02982 155 ALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-295 |
8.91e-37 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 133.77 E-value: 8.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 44 LVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehqYRRAVQMVFQDpfSSLNPAFTVSHHLARPLQLhrQ 123
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP------HLRHINMVFQS--YALFPHMTVEENVAFGLKM--R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 124 SGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKR 203
Cdd:TIGR01187 71 KVPRAEIKPRVLEALRLVQLEEFADRK--PHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 204 ENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYT----------RLLLSAVPDGSRPFVTGGSAR 273
Cdd:TIGR01187 149 QLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVarfigeinvfEATVIERKSEQVVLAGVEGRR 228
|
250 260
....*....|....*....|....*....
gi 2006592715 274 FL-------EQAEKVRSLSRPESTVIEQV 295
Cdd:TIGR01187 229 CDiytdvpvEKDQPLHVVLRPEKIVIEEE 257
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-251 |
1.11e-36 |
|
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: 134.08 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 27 HALKgVSFSLfPGRAL-ALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDpfSSLN 105
Cdd:TIGR02142 12 FSLD-ADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPLQLHRQSgSRTDLAEEIARLLtsvGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSM 185
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPS-ERRISFERVIELL---GIGHLLGR--LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 186 LDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPY 251
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-246 |
1.14e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 132.18 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENI--QRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQ 88
Cdd:PRK13648 5 NSIIVFKNVsfQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD----DNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFSSLNPAfTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLepdLTRQKF-PHELSGGQRQRVNIA 167
Cdd:PRK13648 81 LRKHIGIVFQNPDNQFVGS-IVKYDVA--FGLENHAVPYDEMHRRVSEALKQVDM---LERADYePNALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-302 |
2.48e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.81 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakDEHQYRRA 92
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS------HVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDpfSSLNPAFTVSHHLARPLQLHRQsgSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIARALAV 172
Cdd:PRK11607 93 INMMFQS--YALFPHMTVEQNIAFGLKQDKL--PKAEIASRVNEMLGLVHMQEFAKRK--PHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLsdpRHPYT 252
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTT 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2006592715 253 RLllsavpdgSRPFVtgGSARFLEQAEKVRslsRPESTVIEQVGSNHFMR 302
Cdd:PRK11607 244 RY--------SAEFI--GSVNVFEGVLKER---QEDGLVIDSPGLVHPLK 280
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-257 |
4.95e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.09 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 18 NIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLT----ARGEAK--DEHQY-- 89
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKvaDKNQLrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 -RRAVQMVFQDpFSSLNPAFTVSHHLARPLQLhrQSGSRTDLAEEIARLLTSVGLEpDLTRQKFPHELSGGQRQRVNIAR 168
Cdd:PRK10619 90 lRTRLTMVFQH-FNLWSHMTVLENVMEAPIQV--LGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPR 248
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
....*....
gi 2006592715 249 HPYTRLLLS 257
Cdd:PRK10619 245 SPRLQQFLK 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-239 |
9.42e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 9.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ--DLTARGEAKDEHQYRR 91
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDpfSSLNPAFTVSHHL-ARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARAL 170
Cdd:COG4161 83 KVGMVFQQ--YNLWPHLTVMENLiEAPCKVLGLS--KEQAREKAMKLLARLRLTDKADR--FPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRK---DILHLLAtvkrENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGD 239
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAqvvEIIRELS----QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-235 |
1.94e-35 |
|
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: 127.24 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 22 NFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeAKDEHQYRRAVQMVFQdpF 101
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----RTDRKAARQSLGYCPQ--F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSLNPAFTVSHHLARPLQLHrqSGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIARALAVAPSVLVADE 181
Cdd:cd03263 84 DALFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDKANKR--ARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 182 PTSMLDVSIRKDILHLLATVKREndLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-245 |
3.68e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.01 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 33 SFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehqyRRAVQMVFQDpfSSLNPAFTVSH 112
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQE--NNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 113 HLArpLQLH---RQSGSRTDLAEEIARlltSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVS 189
Cdd:PRK10771 91 NIG--LGLNpglKLNAAQREKLHAIAR---QMGIEDLLAR--LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 190 IRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-241 |
4.19e-35 |
|
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: 126.72 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeaKDEHQYRRAV 93
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-----REPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLARPLQLHRQSGSRtdLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVA 173
Cdd:cd03265 76 GIVFQDL--SVDDELTGWENLYIHARLYGVPGAE--RRERIDELLDFVGLLE--AADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTD 241
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-257 |
6.73e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.79 E-value: 6.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLffRGQDLTARGEAKDEHQ--- 88
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITIDTARSLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 ---YRRAVQMVFQDpfSSLNPAFTVSHHLAR-PLQLhrqSGSRTDLAEEIAR-LLTSVGLEPDLTRqkFPHELSGGQRQR 163
Cdd:PRK11264 80 irqLRQHVGFVFQN--FNLFPHRTVLENIIEgPVIV---KGEPKEEATARAReLLAKVGLAGKETS--YPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTV 243
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
250
....*....|....
gi 2006592715 244 LSDPRHPYTRLLLS 257
Cdd:PRK11264 232 FADPQQPRTRQFLE 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-233 |
7.72e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 129.68 E-value: 7.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 2 KAEANPVVTDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTarg 81
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 82 EAKDEHqyrRAVQMVFQDpfSSLNPAFTVSHHLARPLQLhrQSGSRTDLAEEIARLLTSVGLEpDLTRQKfPHELSGGQR 161
Cdd:PRK09452 80 HVPAEN---RHVNTVFQS--YALFPHMTVFENVAFGLRM--QKTPAAEITPRVMEALRMVQLE-EFAQRK-PHQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-263 |
1.77e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.30 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 16 LENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehqyrRAVQM 95
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ------RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 96 VFQDpfSSLNPAFTVSHHLARPLQLhrQSGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPS 175
Cdd:PRK11432 83 VFQS--YALFPHMSLGENVGYGLKM--LGVPKEERKQRVKEALELVDLAGFEDR--YVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 176 VLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLsdpRHPYTRLL 255
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQPASRFM 233
|
....*...
gi 2006592715 256 LSAVPDGS 263
Cdd:PRK11432 234 ASFMGDAN 241
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-233 |
4.00e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 123.90 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF-GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtARGEAKDEHQYRR 91
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV-NRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDpfSSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLtrQKFPHELSGGQRQRVNIARALA 171
Cdd:TIGR02673 80 RIGVVFQD--FRLLPDRTVYENVALPLEVRGKK--EREIQRRVGAALRQVGLEHKA--DAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLatvKRENDLAMLYI--THDIATAAHVAEEIVVMFAGQ 233
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLL---KRLNKRGTTVIvaTHDLSLVDRVAHRVIILDDGR 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-219 |
4.76e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.16 E-value: 4.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQdpFSSLNPAF 108
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQLhrqSGSRTDLAEEIAR-LLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:PRK11629 103 TALENVAMPLLI---GKKKPAEINSRALeMLAAVGLEH--RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|..
gi 2006592715 188 VSIRKDILHLLATVKRENDLAMLYITHDIATA 219
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-247 |
4.96e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.52 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDPFSSLnpa 107
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPEHQL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 F--TVSHHLA-RPLQLhrqsGSRTDLAEEIAR-LLTSVGLEPDLtRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPT 183
Cdd:PRK13634 99 FeeTVEKDICfGPMNF----GVSEEDAKQKAReMIELVGLPEEL-LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 184 SMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-241 |
8.48e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.59 E-value: 8.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ--DLTARGEAKDEHQYRR 91
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDpfSSLNPAFTVSHHL----ARPLQLhrqsgSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIA 167
Cdd:PRK11124 83 NVGMVFQQ--YNLWPHLTVQQNLieapCRVLGL-----SKDQALARAEKLLERLRLKPYADR--FPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRK---DILHLLAtvkrENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTD 241
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAqivSIIRELA----ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-235 |
3.54e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.21 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVH-ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakdehQYRRAV 93
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-------ERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPFSSLnpaFTVShhLARPLQL-HRQSGSRTDLAEEIARLltsvgLEPDLTRQKFPHELSGGQRQRVNIARALAV 172
Cdd:cd03226 74 GYVMQDVDYQL---FTDS--VREELLLgLKELDAGNEQAETVLKD-----LDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 173 APSVLVADEPTSMLD----VSIRKDILHLLATVKrendlAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03226 144 GKDLLIFDEPTSGLDyknmERVGELIRELAAQGK-----AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-215 |
5.48e-33 |
|
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: 120.66 E-value: 5.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehqYRR 91
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPfsSLNPAFTVSHHLArplQLHRQSGSRTDlAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALA 171
Cdd:COG4133 76 RLAYLGHAD--GLKPELTVRENLR---FWAALYGLRAD-REAIDEALEAVGLAG--LADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATvKRENDLAMLYITHD 215
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-254 |
5.51e-33 |
|
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: 128.41 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIqrNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQY 89
Cdd:COG2274 474 IELENV--SFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI----DPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDP--FSSlnpafTVSH--HLARPlqlhrqsgSRTDlaEEIARLLTSVGLEPDLtrQKFPH----------- 154
Cdd:COG2274 548 RRQIGVVLQDVflFSG-----TIREniTLGDP--------DATD--EEIIEAARLAGLHDFI--EALPMgydtvvgeggs 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLAtvKRENDLAMLYITHDIATAAHvAEEIVVMFAGQM 234
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR--RLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
250 260
....*....|....*....|
gi 2006592715 235 VEWGDTDTVLSDPRHpYTRL 254
Cdd:COG2274 688 VEDGTHEELLARKGL-YAEL 706
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-252 |
5.97e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.87 E-value: 5.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL-----DKPTGGRLFFRGQDLTArgEAKDEHQ 88
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS--PDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQ--DPFsslnPAFTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQ--KFPHELSGGQRQRV 164
Cdd:PRK14267 83 VRREVGMVFQypNPF----PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlnDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKreNDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
....*...
gi 2006592715 245 SDPRHPYT 252
Cdd:PRK14267 237 ENPEHELT 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-235 |
6.72e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 120.75 E-value: 6.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF-GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTaRGEAKDEHQYRR 91
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT-RLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFSSLNPafTVSHHLARPLQLHRQSGSrtDLAEEIARLLTSVGLepdLTRQK-FPHELSGGQRQRVNIARAL 170
Cdd:PRK10908 80 QIGMIFQDHHLLMDR--TVYDNVAIPLIIAGASGD--DIRRRVSAALDKVGL---LDKAKnFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVG-VTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-246 |
6.83e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVH--ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQ 88
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK----ENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFSSLNPAfTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIAR 168
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGA-TVEDDIA--FGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKE--PQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAhVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-238 |
7.58e-33 |
|
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: 120.33 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakdehQYRRAVQ 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE---------KERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 95 MVFQdpFSSLNPAF--TVSHHLARPLQLHR---QSGSRTDlAEEIARLLTSVGLEpDLTRQKFpHELSGGQRQRVNIARA 169
Cdd:cd03235 72 YVPQ--RRSIDRDFpiSVRDVVLMGLYGHKglfRRLSKAD-KAKVDEALERVGLS-ELADRQI-GELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEiVVMFAGQMVEWG 238
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-236 |
1.51e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 120.20 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeAKDEhQYR 90
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST---LKPE-IYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDP--FSSlnpafTVSHHLARPLQLHRQSGSRTDLAEEIARLltsvGLePDLTRQKFPHELSGGQRQRVNIAR 168
Cdd:PRK10247 81 QQVSYCAQTPtlFGD-----TVYDNLIFPWQIRNQQPDPAIFLDDLERF----AL-PDTILTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRK---DILHLLAtvkRENDLAMLYITHDIATAAHvAEEIVVM--FAGQMVE 236
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHnvnEIIHRYV---REQNIAVLWVTHDKDEINH-ADKVITLqpHAGEMQE 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-286 |
1.29e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.26 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehqyRRAV 93
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 qmVFQDpfSSLNPAFTVSHHLARPLQLhrqSGSRTDLAEEIAR-LLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAV 172
Cdd:PRK11248 75 --VFQN--EGLLPWRNVQDNVAFGLQL---AGVEKMQRLEIAHqMLKKVGLEG--AEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMF--AGQMVEwgdtdtvlsdprhp 250
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE-------------- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2006592715 251 ytRLLLsavpDGSRPFVTGGSAR-------FLEQAEKVrsLSR 286
Cdd:PRK11248 212 --RLPL----NFARRFVAGESSRsiksdpqFIAMREYV--LSR 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-249 |
1.32e-31 |
|
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: 117.57 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehqyrravQMVFQDpfSSLNPAF 108
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR---------MVVFQN--YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTE--AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 189 SIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTV-LSDPRH 249
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-238 |
1.54e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 123.35 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQYRRAVQMVFQDPF---SSL 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL----TLESLRRQIGVVPQDTFlfsGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 --NPAFtvshhlARPlqlhrqsgSRTDlaEEIARLLTSVGLEPDLtrQKFPH-----------ELSGGQRQRVNIARALA 171
Cdd:COG1132 431 reNIRY------GRP--------DATD--EEVEEAAKAAQAHEFI--EALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-235 |
2.03e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.44 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARG--EAkdeh 87
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprDA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 qyRRA-VQMVFQDPfsSLNPAFTVSHHLA---RPLQLHRQsgSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQR 163
Cdd:COG3845 78 --IALgIGMVHQHF--MLVPNLTVAENIVlglEPTKGGRL--DRKAARARIRELSERYGLDVDPDA--KVEDLSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 164 VNIARALAVAPSVLVADEPTSML-----DvsirkdilHLLATVKR--ENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtpqeaD--------ELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-245 |
2.93e-31 |
|
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: 122.56 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 3 AEANPVVTDAVIRLENIQ-RNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTarg 81
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 82 eAKDEHQYRRAVQMVFQDPF---SSL-------NPAFTvSHHLARPLQlhrqsgsRTDLAEEIARLltSVGLEPDLTRQK 151
Cdd:COG4988 403 -DLDPASWRRQIAWVPQNPYlfaGTIrenlrlgRPDAS-DEELEAALE-------AAGLDEFVAAL--PDGLDTPLGEGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 152 FPheLSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEEIVVMFA 231
Cdd:COG4988 472 RG--LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDD 546
|
250
....*....|....
gi 2006592715 232 GQMVEWGDTDTVLS 245
Cdd:COG4988 547 GRIVEQGTHEELLA 560
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-252 |
3.52e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 117.46 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDK------PTGGRLFFRGQDLTArgeaKDEHQYRRAVQMVFQDPfs 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ----IDAIKLRKEVGMVFQQP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 103 SLNPAFTVSHHLARPLQLHRQSGSRtDLAEEIARLLTSVGLEPDL-TRQKFP-HELSGGQRQRVNIARALAVAPSVLVAD 180
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKEKR-EIKKIVEECLRKVGLWKEVyDRLNSPaSQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 181 EPTSMLDVSIRKDILHLLATVKREndLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYT 252
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-247 |
1.07e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 25 PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL---DKPTGGRLFFRGQDLTArgeaKDEHQYRRAVQMVFQDPF 101
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA----KTVWDIREKVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSLNPAfTVSHHLARPLQlHRQSgSRTDLAEEIARLLTSVGLepdLTRQKF-PHELSGGQRQRVNIARALAVAPSVLVAD 180
Cdd:PRK13640 95 NQFVGA-TVGDDVAFGLE-NRAV-PRPEMIKIVRDVLADVGM---LDYIDSePANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 181 EPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-252 |
3.16e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDK-----PTGGRLFFRGQDLTARgeAK 84
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSP--RT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 85 DEHQYRRAVQMVFQDPfsslNP-AFTVSHHLARPLQLH-RQSGSRTDLAEEIARLLTSVGLEPDLTRQKFPHELSGGQRQ 162
Cdd:PRK14239 80 DTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKgIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAPSVLVADEPTSMLD-VSIRK--DILHLLatvkrENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGD 239
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDpISAGKieETLLGL-----KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
250
....*....|...
gi 2006592715 240 TDTVLSDPRHPYT 252
Cdd:PRK14239 231 TKQMFMNPKHKET 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-255 |
3.45e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 119.49 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 3 AEANPVVTDAVIRLENIqrNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLT 78
Cdd:COG4987 323 AEPAPAPGGPSLELEDV--SFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 79 ARgeakDEHQYRRAVQMVFQDP--FSSlnpafTVSH--HLARPlqlhrqsgSRTDlaEEIARLLTSVGLEPDLTRQK--- 151
Cdd:COG4987 401 DL----DEDDLRRRIAVVPQRPhlFDT-----TLREnlRLARP--------DATD--EELWAALERVGLGDWLAALPdgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 152 --FPHE----LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEE 225
Cdd:COG4987 462 dtWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDR 538
|
250 260 270
....*....|....*....|....*....|
gi 2006592715 226 IVVMFAGQMVEWGDTDTVLSDPRHpYTRLL 255
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGR-YRQLY 567
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-273 |
3.90e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.44 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 17 ENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMV 96
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 97 FQDpfSSLNPAFTVSHHLARPLQLHRQSGSrtDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSV 176
Cdd:PRK10070 112 FQS--FALMPHMTVLDNTAFGMELAGINAE--ERREKALDALRQVGLEN--YAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 177 LVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLL 256
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
250
....*....|....*..
gi 2006592715 257 SAVpDGSRPFVTGGSAR 273
Cdd:PRK10070 266 RGV-DISQVFSAKDIAR 281
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-253 |
4.96e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGP---VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDE 86
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE----ENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 HQYRRAVQMVFQDPFSSLNPAfTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNI 166
Cdd:PRK13650 77 WDIRHKIGMVFQNPDNQFVGA-TVEDDVA--FGLENKGIPHEEMKERVNEALELVGMQDFKERE--PARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAhVAEEIVVMFAGQmVEwgdtdtVLSD 246
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VE------STST 223
|
....*..
gi 2006592715 247 PRHPYTR 253
Cdd:PRK13650 224 PRELFSR 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-243 |
5.37e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 5.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEhqYRRAVQMVFQDPFSSLnpa 107
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSD--IRKKVGLVFQYPEYQL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 F--TVSHHLA---RPLQLhrqsgSRTDLAEEIARLLTSVGLEPDLTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEP 182
Cdd:PRK13637 97 FeeTIEKDIAfgpINLGL-----SEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 183 TSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTV 243
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-267 |
5.72e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.06 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLT-------ARgeakde 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspwelAR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 hqyRRAV--QmvfqdpFSSLNPAFTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRV 164
Cdd:COG4559 76 ---RRAVlpQ------HSSLAFPFTVEEVVA--LGRAPHGSSAAQDRQIVREALALVGLAH--LAGRSYQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALA-------VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVEW 237
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRG-GGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
250 260 270
....*....|....*....|....*....|...
gi 2006592715 238 GDTDTVLSDP--RHPY-TRLLLSAVPDGSRPFV 267
Cdd:COG4559 222 GTPEEVLTDEllERVYgADLRVLAHPEGGCPQV 254
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-246 |
6.04e-30 |
|
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: 112.91 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeAKDEHQYRRAV 93
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG---LPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDP--FSSLnpafTVSHHlarpLQLHRQSGSRTDLAEEIARLLTsvgLEPDL-TRQKFP-HELSGGQRQRVNIARA 169
Cdd:cd03224 78 GYVPEGRriFPEL----TVEEN----LLLGAYARRRAKRKARLERVYE---LFPRLkERRKQLaGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-246 |
8.90e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.17 E-value: 8.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGP-VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ--DLTARGEAKdeh 87
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 qYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRqsgSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIA 167
Cdd:PRK13636 80 -LRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKL---PEDEVRKRVDNALKRTGIEH--LKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-238 |
9.02e-30 |
|
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: 113.09 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRA 92
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE----VTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDpfsslNPAF--TVSHHLA--RPlqlhrqsgSRTDlaEEIARLLTSVGLEPDLTRQKFPHE---------LSGG 159
Cdd:cd03253 77 IGVVPQD-----TVLFndTIGYNIRygRP--------DATD--EEVIEAAKAAQIHDKIMRFPDGYDtivgerglkLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 160 QRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLamLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-238 |
1.18e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.90 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehqyrR 91
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSRTD-LAEEIARLLTsvgLEPDLTRQkfPHELSGGQRQRVNIARAL 170
Cdd:PRK11000 76 GVGMVFQS--YALYPHLSVAENMSFGLKLAGAKKEEINqRVNQVAEVLQ---LAHLLDRK--PKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 171 AVAPSVLVADEPTSMLD----VSIRKDILHLLATVKRendlAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-236 |
1.51e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.65 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNF---GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEH 87
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----ENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRAVQMVFQDPFSSLNPAfTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIA 167
Cdd:PRK13642 78 NLRRKIGMVFQNPDNQFVGA-TVEDDVA--FGMENQGIPREEMIKRVDEALLAVNMLDFKTRE--PARLSGGQKQRVAVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVE 236
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-246 |
2.69e-29 |
|
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: 116.83 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 2 KAEANPVVTDAVIRLENIQRNF-----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFR-GQ 75
Cdd:TIGR03269 268 EKECEVEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 76 ---DLT-----ARGEAKdehqyrRAVQMVFQDpfSSLNPAFTVSHHLARPLQLhrqsgsrtDLAEEIARL-----LTSVG 142
Cdd:TIGR03269 348 ewvDMTkpgpdGRGRAK------RYIGILHQE--YDLYPHRTVLDNLTEAIGL--------ELPDELARMkavitLKMVG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 143 LEPDLTRQ---KFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATA 219
Cdd:TIGR03269 412 FDEEKAEEildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFV 491
|
250 260
....*....|....*....|....*..
gi 2006592715 220 AHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:TIGR03269 492 LDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-238 |
4.85e-29 |
|
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: 110.36 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGrALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehqYRRAV 93
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLARPLQLHRQSGSRTDlaEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVA 173
Cdd:cd03264 75 GYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVK--ARVDEVLELVNLGD--RAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLATVKrENDLAMLYiTHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILS-THIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
39-238 |
4.91e-29 |
|
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: 110.28 E-value: 4.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 39 GRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehqyRRAVQMVFQDpfSSLNPAFTVSHH--LAR 116
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQE--NNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 117 PLQLHRQSGSRtdlaEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILH 196
Cdd:cd03298 96 SPGLKLTAEDR----QAIEVALARVGLAGLEKRL--PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2006592715 197 LLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-253 |
1.02e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.90 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTG-----GRLFFRGQDLTARgeAKDEHQ 88
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYER--RVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPfsSLNPaFTVSHHLARPLQLhrqSGSRTDLaeEIARLLTSVGLEPDLTRQ------KFPHELSGGQRQ 162
Cdd:PRK14258 86 LRRQVSMVHPKP--NLFP-MSVYDNVAYGVKI---VGWRPKL--EIDDIVESALKDADLWDEikhkihKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFA-----GQMVEW 237
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEF 237
|
250
....*....|....*.
gi 2006592715 238 GDTDTVLSDPRHPYTR 253
Cdd:PRK14258 238 GLTKKIFNSPHDSRTR 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-253 |
1.28e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.64 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDK--PTG---GRLFFRGQDLTARGeaK 84
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPD--V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 85 DEHQYRRAVQMVFQ--DPFSSL---NPAFTVshhlarplqlhRQSGSRTDLAEEIARLLTSVGLEpDLTRQKFPHE---L 156
Cdd:PRK14243 85 DPVEVRRRIGMVFQkpNPFPKSiydNIAYGA-----------RINGYKGDMDELVERSLRQAALW-DEVKDKLKQSglsL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLD-VSIRKdILHLLATVKRenDLAMLYITHDIATAAHVAeEIVVMF----- 230
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHELKE--QYTIIIVTHNMQQAARVS-DMTAFFnvelt 228
|
250 260
....*....|....*....|....*...
gi 2006592715 231 -----AGQMVEWGDTDTVLSDPRHPYTR 253
Cdd:PRK14243 229 egggrYGYLVEFDRTEKIFNSPQQQATR 256
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-241 |
5.04e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.57 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTC-ARIIARLDKP--TGGRLFFRGQDLTARgeakdeHQYRR 91
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRRLTAL------PAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFssLNPAFTVSHHLARPLqlhRQSGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALA 171
Cdd:COG4136 77 RIGILFQDDL--LFPHLSVGENLAFAL---PPTIGRAQRRARVEQALEEAGLAGFADR--DPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAhvaeeivvmFAGQMVEWGDTD 241
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP---------AAGRVLDLGNWQ 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
33-240 |
7.53e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 107.25 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 33 SFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehqYRRAVQMVFQDpfSSLNPAFTVSH 112
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP------YQRPVSMLFQE--NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 113 HLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRK 192
Cdd:TIGR01277 90 NIG--LGLHPGLKLNAEQQEKVVDAAQQVGIADYLDR--LPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2006592715 193 DILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDT 240
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-247 |
1.14e-27 |
|
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: 107.24 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakDEHQYRRA- 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT------KLPMHKRAr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 --VQMVFQDP--FSSLnpafTVSHHLARPLQLHRQsgSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIAR 168
Cdd:cd03218 75 lgIGYLPQEAsiFRKL----TVEENILAVLEIRGL--SKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKrENDLAMLyIT-HDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVL-ITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-198 |
1.57e-27 |
|
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: 106.34 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtARGEAKDEHQYRRA 92
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSrtDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAV 172
Cdd:cd03292 80 IGVVFQD--FRLLPDRNVYENVAFALEVTGVPPR--EIRKRVPAALELVGLSH--KHRALPAELSGGEQQRVAIARAIVN 153
|
170 180
....*....|....*....|....*.
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLL 198
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLL 179
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-247 |
1.59e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.51 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQYRRAVQMVFQDP--FSSlnp 106
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL----VQYDHHYLHRQVALVGQEPvlFSG--- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 afTVSHHLARPLQlhrqsgsRTDLAEEIArllTSVGLEPDLTRQKFPH-----------ELSGGQRQRVNIARALAVAPS 175
Cdd:TIGR00958 570 --SVRENIAYGLT-------DTPDEEIMA---AAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 176 VLVADEPTSMLDVSIRkdilHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:TIGR00958 638 VLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-247 |
2.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.77 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNF-GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDltaRGEAKDEHQYRR 91
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID---TGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFSSLnPAFTVSHHLA-RPLQLHRQSgsrTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARAL 170
Cdd:PRK13644 78 LVGIVFQNPETQF-VGRTVEEDLAfGPENLCLPP---IEIRKRVDRALAEIGLEK--YRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIaTAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-233 |
2.24e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.16 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNF-GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgEAKDehqyr 90
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPAD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDpfSSLNPAFTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLTRQkfPHELSGGQRQRVNIARAL 170
Cdd:PRK11650 76 RDIAMVFQN--YALYPHMSVRENMAYGLKIRGMP--KAEIEERVAEAARILELEPLLDRK--PRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLD----VSIRKDILHL---LATVKrendlamLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDaklrVQMRLEIQRLhrrLKTTS-------LYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-246 |
2.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDPFSSLNpA 107
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLF-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 FTVSHHLARPLQlhrQSGSRTDLAEEIAR-LLTSVGLEPDLtRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSML 186
Cdd:PRK13649 101 ETVLKDVAFGPQ---NFGVSQEEAEALAReKLALVGISESL-FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 187 DVSIRKDILHLLATVkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13649 177 DPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-267 |
4.07e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.39 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLT--ARGE-AKdehq 88
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAElAR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 yRRAV--QmvfqdpFSSLNPAFTVSHHLArpLQLHRQSGSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNI 166
Cdd:PRK13548 77 -RRAVlpQ------HSSLSFPFTVEEVVA--MGRAPHGLSRAEDDALVAAALAQVDLAH--LAGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALA------VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDT 240
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
250 260 270
....*....|....*....|....*....|
gi 2006592715 241 DTVLSDP--RHPY-TRLLLSAVPDGSRPFV 267
Cdd:PRK13548 226 AEVLTPEtlRRVYgADVLVQPHPETGAPLV 255
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-248 |
4.21e-27 |
|
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: 105.83 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakdeHQYR 90
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL------PPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RA---VQMVFQDP--FSSLnpafTVSHHLARPLQLHRqsgSRTDLAEEIARLLTsvgLEPDL-TRQKFP-HELSGGQRQR 163
Cdd:COG0410 75 IArlgIGYVPEGRriFPSL----TVEENLLLGAYARR---DRAEVRADLERVYE---LFPRLkERRRQRaGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTV 243
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
....*
gi 2006592715 244 LSDPR 248
Cdd:COG0410 224 LADPE 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-247 |
4.51e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.81 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRAVQMVFQDP--- 100
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK----ENIREVRKFVGLVFQNPddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 101 -FSSlnpafTVSHHLA-RPLQLHRQSGSrtdLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLV 178
Cdd:PRK13652 91 iFSP-----TVEQDIAfGPINLGLDEET---VAHRVSSALHMLGLEELRDR--VPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 179 ADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-236 |
6.99e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFrgQDLTARGEAKDEH--QYRRAVQMVFQDPFSSLN 105
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYirPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPlqlhRQSGSRTDLAEEIA-RLLTSVGLEPDLTRQKfPHELSGGQRQRVNIARALAVAPSVLVADEPTS 184
Cdd:PRK13646 100 EDTVEREIIFGP----KNFKMNLDEVKNYAhRLLMDLGFSRDVMSQS-PFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 185 MLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVE 236
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-252 |
8.23e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 106.33 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 18 NIQRNFGPVHALKGVSFSlFPGRAL-ALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARG--EAKDEHQYRRAVQ 94
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMG-FPARAVtSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 95 MVFQDPfsslNP-AFTVSHHLARPLQLHRQSGSRTDLAEEIARLlTSVGLEpDLTRQKF---PHELSGGQRQRVNIARAL 170
Cdd:PRK14271 105 MLFQRP----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARL-TEVGLW-DAVKDRLsdsPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKreNDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPRHP 250
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
..
gi 2006592715 251 YT 252
Cdd:PRK14271 257 ET 258
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-234 |
2.06e-26 |
|
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: 102.29 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehQYRRAVQMVFQDpfsslnpaf 108
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN----ELGDHVGYLPQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 tvshhlarpLQLHrqSGSrtdLAEEIarlltsvglepdltrqkfpheLSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:cd03246 85 ---------DELF--SGS---IAENI---------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2006592715 189 SIRKDILHLLATVKRENDLAMLyITHDIATAAhVAEEIVVMFAGQM 234
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIV-IAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-247 |
2.14e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQ 88
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLhrqsGSRTDLAEEIA-RLLTSVGLEPDLTrQKFPHELSGGQRQRVNIA 167
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFGPKNF----GFSEDEAKEKAlKWLKKVGLSEDLI-SKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLyITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-247 |
5.32e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtaRGEAKDEHQYRRAVQMVFQDPFSSLNpA 107
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI--KYDKKSLLEVRKTVGIVFQNPDDQLF-A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 FTVSHHLA-RPLQLhrqSGSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSML 186
Cdd:PRK13639 94 PTVEEDVAfGPLNL---GLSKEEVEKRVKEALKAVGMEG--FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 187 DVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-247 |
1.01e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.28 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 27 HALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQYRRAVQMVFQDP----FS 102
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE----NEKWVRSKVGLVFQDPddqvFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 103 SlnpafTVSHHLA-RPLQLHRqsgSRTDLAEEIARLLTSVGLEpDLtRQKFPHELSGGQRQRVNIARALAVAPSVLVADE 181
Cdd:PRK13647 95 S-----TVWDDVAfGPVNMGL---DKDEVERRVEEALKAVRMW-DF-RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 182 PTSMLDVSIRKDILHLLATVKRENDLAMLyITHDIATAAHVAEEIVVMFAGQMVEWGDTdTVLSDP 247
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIV-ATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDE 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-304 |
1.01e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.65 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeakdEHQYR-- 90
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP------EDRRRig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 -----RavqmvfqdpfsSLNPAFTVSHHLARPLQLHrqsG-SRTDLAEEIARLLTSVGLEPdltRQKFP-HELSGGQRQR 163
Cdd:COG4152 75 ylpeeR-----------GLYPKMKVGEQLVYLARLK---GlSKAEAKRRADEWLERLGLGD---RANKKvEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLD---VSIRKDILHLLatvkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDT 240
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDpvnVELLKDVIREL----AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSV 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 241 DTVLSdpRHPYTRLLLsavpdgsrpfVTGGSARFLEQAEKVRSLSRPESTVI----EQVGSNHFMRAL 304
Cdd:COG4152 214 DEIRR--QFGRNTLRL----------EADGDAGWLRALPGVTVVEEDGDGAElkleDGADAQELLRAL 269
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-220 |
1.61e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.39 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDPFssLNPAF 108
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM--LIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQLHRQSGSRTdlAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:PRK10584 104 NALENVELPALLRGESSRQS--RNGAKALLEQLGLGKRLDH--LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190
....*....|....*....|....*....|..
gi 2006592715 189 SIRKDILHLLATVKRENDLAMLYITHDIATAA 220
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-290 |
2.33e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.68 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 16 LENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargEAKDEhqyrraVQM 95
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA---EARED------TRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 96 VFQDpfSSLNPAFTVSHHLARPLqlhrqSGSRTDLAEEIarlLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPS 175
Cdd:PRK11247 86 MFQD--ARLLPWKKVIDNVGLGL-----KGQWRDAALQA---LAAVGLAD--RANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 176 VLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMvewG-DTDTVLSDPRHPytrl 254
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GlDLTVDLPRPRRR---- 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 2006592715 255 llsavpdgsrpfvtgGSARFLEQAEKV--RSLSRPEST 290
Cdd:PRK11247 227 ---------------GSARLAELEAEVlqRVMSRGESE 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-246 |
3.17e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.09 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargEAKDEHQYRRAVQMVFQDPFSSL--- 104
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS---DEENLWDIRNKAGMVFQNPDNQIvat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 ----NPAFTVSHHLARPLQLHrqsgSRTDLAeeiarlLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSVLVAD 180
Cdd:PRK13633 102 iveeDVAFGPENLGIPPEEIR----ERVDES------LKKVGMYE--YRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 181 EPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-238 |
3.77e-25 |
|
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: 100.05 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgEAKDEHQY---R 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--AARNRIGYlpeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAvqmvfqdpfssLNPAFTVSHHLARPLQLHrqsG-SRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARA 169
Cdd:cd03269 79 RG-----------LYPKMKVIDQLVYLAQLK---GlKKEEARRRIDEWLERLELSE--YANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 170 LAVAPSVLVADEPTSMLD---VSIRKDILHLLatvkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03269 143 VIHDPELLILDEPFSGLDpvnVELLKDVIREL----ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
8-238 |
3.98e-25 |
|
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: 105.29 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 8 VVTDAVIRLENIQRNFGPVHA-LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDE 86
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD----VTQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 HQYRRAVQMVFQDP--F-SSL--NPAF---TVSH----HLARPLQLHrqsgsrtdlaEEIARL----LTSVGlEPDLtrq 150
Cdd:COG5265 428 ASLRAAIGIVPQDTvlFnDTIayNIAYgrpDASEeeveAAARAAQIH----------DFIESLpdgyDTRVG-ERGL--- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 151 kfphELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEEIVVMF 230
Cdd:COG5265 494 ----KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLE 566
|
....*...
gi 2006592715 231 AGQMVEWG 238
Cdd:COG5265 567 AGRIVERG 574
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
15-243 |
5.32e-25 |
|
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: 99.91 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 15 RLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeaKDEHQYRRAVQ 94
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL---PPHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 95 MVFQ--DPFSSLnpafTVSHHLarplqlhrQSGsrtdlAEEIARLLTSVglePDLTRQKFP--HE--------LSGGQRQ 162
Cdd:TIGR03410 79 YVPQgrEIFPRL----TVEENL--------LTG-----LAALPRRSRKI---PDEIYELFPvlKEmlgrrggdLSGGQQQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDT 242
Cdd:TIGR03410 139 QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
.
gi 2006592715 243 V 243
Cdd:TIGR03410 219 L 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-234 |
5.44e-25 |
|
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: 99.85 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 7 PVVTDAVIRLENIQ---RNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgea 83
Cdd:cd03248 5 PDHLKGIVKFQNVTfayPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 84 kdEHQY-RRAVQMVFQDPFSSlnpAFTVSHHLARPLQlhrqsGSRTDLAEEIAR------LLTSVGLEPDLTRQKFPHEL 156
Cdd:cd03248 82 --EHKYlHSKVSLVGQEPVLF---ARSLQDNIAYGLQ-----SCSFECVKEAAQkahahsFISELASGYDTEVGEKGSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEEIVVMFAGQM 234
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-248 |
6.06e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakdeHQ--Y 89
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT--------HLpmH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAvQM----VFQDP--FSSLnpafTVSHHLARPLQLHRQSgsRTDLAEEIARLLTSVGLEPdLTRQKfPHELSGGQRQR 163
Cdd:COG1137 74 KRA-RLgigyLPQEAsiFRKL----TVEDNILAVLELRKLS--KKEREERLEELLEEFGITH-LRKSK-AYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLD---VS-IRKDILHLlatvkRENDLAMLyIT-HdiataaHVAE--EIV----VMFAG 232
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVL-ITdH------NVREtlGICdrayIISEG 212
|
250
....*....|....*.
gi 2006592715 233 QMVEWGDTDTVLSDPR 248
Cdd:COG1137 213 KVLAEGTPEEILNNPL 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-229 |
6.54e-25 |
|
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: 99.82 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNF-----GPV--HALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ----DLTar 80
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 81 gEAkDEHQY----RRAVQMVFQdpFssLN-----PAFTVshhLARPLqlhRQSGSRTDLAEEIAR-LLTSVGLEPDLTrQ 150
Cdd:COG4778 81 -QA-SPREIlalrRRTIGYVSQ--F--LRviprvSALDV---VAEPL---LERGVDREEARARAReLLARLNLPERLW-D 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 151 KFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEIVVM 229
Cdd:COG4778 148 LPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-244 |
9.50e-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: 99.22 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQYRRA 92
Cdd:cd03254 3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI----SRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDP--FSSlnpafTVSHHLarplqlhRQSGSRTDlAEEIARLLTSVGLEpDLTRqKFP-----------HELSGG 159
Cdd:cd03254 79 IGVVLQDTflFSG-----TIMENI-------RLGRPNAT-DEEVIEAAKEAGAH-DFIM-KLPngydtvlgengGNLSQG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 160 QRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKreNDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGD 239
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
....*
gi 2006592715 240 TDTVL 244
Cdd:cd03254 221 HDELL 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-235 |
1.32e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 98.82 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 25 PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQYRRAVQMVFQDP---F 101
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL----DPADLRRNIGYVPQDVtlfY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSLNPAFTVSHHLArplqlhrqsgsrTDlaEEIARLLTSVGLEpDLTRqKFPH-----------ELSGGQRQRVNIARAL 170
Cdd:cd03245 92 GTLRDNITLGAPLA------------DD--ERILRAAELAGVT-DFVN-KHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAhVAEEIVVMFAGQMV 235
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-247 |
1.32e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 6 NPVVTDAVIRLENIQRNFG-----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRL----FFRGQD 76
Cdd:PRK13631 14 NPLSDDIILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 77 LTARGEA--------KDEHQYRRAVQMVFQDPFSSLNPAFTVSHHLARPLQLHRqsgSRTDLAEEIARLLTSVGL-EPDL 147
Cdd:PRK13631 94 KNNHELItnpyskkiKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGV---KKSEAKKLAKFYLNKMGLdDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 148 TRQkfPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIV 227
Cdd:PRK13631 171 ERS--PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVI 247
|
250 260
....*....|....*....|
gi 2006592715 228 VMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQ 267
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-247 |
1.83e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.10 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 43 ALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakDEHQ------YRRAVQMVFQDpfSSLNPAFTVSHHLar 116
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF------DAEKgiclppEKRRIGYVFQD--ARLFPHYKVRGNL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 117 plqlhrQSGSRTDLAEEIARLLTSVGLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILH 196
Cdd:PRK11144 98 ------RYGMAKSMVAQFDKIVALLGIEPLLDR--YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 197 LLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-235 |
1.90e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.39 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehq 88
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQM--VFQDPFSSLNPAFTVSHHLA--------RPLQLHRQSGSRTDLAEEIA--------RLLTSVGLepdltrq 150
Cdd:COG1101 76 YKRAKYIgrVFQDPMMGTAPSMTIEENLAlayrrgkrRGLRRGLTKKRRELFRELLAtlglglenRLDTKVGL------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 151 kfpheLSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMF 230
Cdd:COG1101 149 -----LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMH 223
|
....*
gi 2006592715 231 AGQMV 235
Cdd:COG1101 224 EGRII 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-238 |
2.53e-24 |
|
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: 97.82 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeAKDEHQY 89
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSR-TDLAEEIARLLtsvGLEPDLTRQKfpHELSGGQRQRVNIAR 168
Cdd:cd03266 77 RRRLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDElTARLEELADRL---GMEELLDRRV--GGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-245 |
2.54e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdeHQYRRAV 93
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS----RQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfssLNP---------AFTVSHHL-------ARPLQLHRQSGSRTDLAEEIARLLTsvglepdltrqkfphELS 157
Cdd:PRK11231 79 ALLPQHH---LTPegitvrelvAYGRSPWLslwgrlsAEDNARVNQAMEQTRINHLADRRLT---------------DLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 158 GGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAGQMVEW 237
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
....*...
gi 2006592715 238 GDTDTVLS 245
Cdd:PRK11231 220 GTPEEVMT 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-235 |
3.68e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNF----GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtARGEAKDEH 87
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-ATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRA-VQMVFQDpfSSLNPAFTVSHHLARPlQLHRQSGSRTDLAEEIArLLTSVGLEPDLTRQkfPHELSGGQRQRVNI 166
Cdd:PRK10535 82 QLRREhFGFIFQR--YHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQE-LLQRLGLEDRVEYQ--PSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVkRENDLAMLYITHDIATAAHvAEEIVVMFAGQMV 235
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
14-255 |
1.21e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 101.17 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHA--LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQYRR 91
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPR----EEIPREVLAN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQD-------------------PFSSLNPAftvshhlARPLQLHRQSGSRTDlaeeiarlltsvGLEPDLTrqkf 152
Cdd:TIGR03796 554 SVAMVDQDiflfegtvrdnltlwdptiPDADLVRA-------CKDAAIHDVITSRPG------------GYDAELA---- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 153 phE----LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLatvkRENDLAMLYITHDIATAAHvAEEIVV 228
Cdd:TIGR03796 611 --EgganLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLSTIRD-CDEIIV 683
|
250 260
....*....|....*....|....*..
gi 2006592715 229 MFAGQMVEWGdTDTVLSDPRHPYTRLL 255
Cdd:TIGR03796 684 LERGKVVQRG-THEELWAVGGAYARLI 709
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-212 |
1.60e-23 |
|
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: 96.19 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLD---KPTGGRLFFRGQDLTArgeakdeHQYRRAVQMVFQDPFssLN 105
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKP-------DQFQKCVAYVRQDDI--LL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHL--ARPLQLHRQSGSRTDLAEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPT 183
Cdd:cd03234 94 PGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRDLALTR--IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|....*....
gi 2006592715 184 SMLDVSIRKDILHLLATVKRENDLAMLYI 212
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-245 |
2.25e-23 |
|
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: 96.02 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP--VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRR 91
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL----ADPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFSsLNPAFTVSHHLARP-LQLHR--QSGSRTDLAEEIARLltSVGLEPDLTRQKFphELSGGQRQRVNIAR 168
Cdd:cd03252 77 QVGVVLQENVL-FNRSIRDNIALADPgMSMERviEAAKLAGAHDFISEL--PEGYDTIVGEQGA--GLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdlAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-236 |
3.70e-23 |
|
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: 94.59 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDltargeAKDEHQYRRAV 93
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS------YQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVSHHLARPLQLHRQSGSRTDlaeeiaRLLTSVGLEpDLTRQKFpHELSGGQRQRVNIARALAVA 173
Cdd:cd03268 75 GALIEAP--GFYPNLTARENLRLLARLLGIRKKRID------EVLDVVGLK-DSAKKKV-KGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLAtVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVE 236
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIL-SLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-245 |
7.43e-23 |
|
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: 94.53 E-value: 7.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 26 VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeaKDE--HQYRRAVQMVFQDP--F 101
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI------RDLnlRWLRSQIGLVSQEPvlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSlnpafTVSHHLA--RPlqlhrqsgSRTDlaEEIARLLTSVGLEPDLTrqKFPH-----------ELSGGQRQRVNIAR 168
Cdd:cd03249 90 DG-----TIAENIRygKP--------DATD--EEVEEAAKKANIHDFIM--SLPDgydtlvgergsQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLatvkrenDLAM-----LYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTV 243
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEAL-------DRAMkgrttIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
..
gi 2006592715 244 LS 245
Cdd:cd03249 225 MA 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-245 |
8.35e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 98.40 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNF--GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakdehQY-- 89
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR---------QIdp 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 ---RRAVQMVFQDP--FSSlnpafTVSHHLArplqlhrqSGSR--TDlaEEIARLLTSVGLEpDLTRQKfPH-------- 154
Cdd:TIGR03375 535 adlRRNIGYVPQDPrlFYG-----TLRDNIA--------LGAPyaDD--EEILRAAELAGVT-EFVRRH-PDgldmqige 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 ---ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdlAMLYITHDIATAAHVaEEIVVMFA 231
Cdd:TIGR03375 598 rgrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLV-DRIIVMDN 674
|
250
....*....|....
gi 2006592715 232 GQMVEWGDTDTVLS 245
Cdd:TIGR03375 675 GRIVADGPKDQVLE 688
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-246 |
1.11e-22 |
|
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: 94.38 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTggrlffRGQDLTARGEAK---DEH 87
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPT------YGNDVRLFGERRggeDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRA---VQMVFQDPFSSLNPAFTV-------SHHLARPLqlhrqsgsrTDLAEEIAR-LLTSVGLEpDLTRQKFpHEL 156
Cdd:COG1119 75 ELRKRiglVSPALQLRFPRDETVLDVvlsgffdSIGLYREP---------TDEQRERAReLLELLGLA-HLADRPF-GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHdiataaHVaEEI------VVMF 230
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HV-EEIppgithVLLL 216
|
250
....*....|....*..
gi 2006592715 231 -AGQMVEWGDTDTVLSD 246
Cdd:COG1119 217 kDGRVVAAGPKEEVLTS 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-238 |
1.32e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.67 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 9 VTDAVIRL--ENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDE 86
Cdd:PRK10253 1 MTESVARLrgEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI----QHYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 HQYRRAVQMVFQDpfsSLNPA-FTVSHHLARPLQLHRQ--SGSRTDLAEEIARLLTSVGLEpDLTRQKFpHELSGGQRQR 163
Cdd:PRK10253 77 KEVARRIGLLAQN---ATTPGdITVQELVARGRYPHQPlfTRWRKEDEEAVTKAMQATGIT-HLADQSV-DTLSGGQRQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-215 |
1.84e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 16 LENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ--------------DLTARG 81
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqepplddDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 82 EAKDEHQYRRAVQMVFQDpfsslnpaftVSHHLARPLQ-LHRQSGSRTDLAE--------EIARLLTSVGLEPDLTRQKF 152
Cdd:COG0488 81 TVLDGDAELRALEAELEE----------LEAKLAEPDEdLERLAELQEEFEAlggweaeaRAEEILSGLGFPEEDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 153 pHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV-SIRkdilhLLATVKRENDLAMLYITHD 215
Cdd:COG0488 151 -SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-246 |
1.97e-22 |
|
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: 93.45 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQYRRAVQMVFQDPFsslnpA 107
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV----RDYTLASLRRQIGLVSQDVF-----L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 F--TVSHHLArplqlhrqSGSRTDLAEEIARLLTSVGLEPDLTRqkFPH-----------ELSGGQRQRVNIARALAVAP 174
Cdd:cd03251 88 FndTVAENIA--------YGRPGATREEVEEAARAANAHEFIME--LPEgydtvigergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 175 SVLVADEPTSMLDVS----IRKDILHLLAtvkrenDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:cd03251 158 PILILDEATSALDTEserlVQAALERLMK------NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-215 |
9.70e-22 |
|
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: 95.12 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRAVQMVFQDP--FSSln 105
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS----LDQDEVRRRVSVCAQDAhlFDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 pafTVSHHL--ARPlqlhrqsgSRTDlaEEIARLLTSVGLEPDLtrQKFPH-----------ELSGGQRQRVNIARALAV 172
Cdd:TIGR02868 424 ---TVRENLrlARP--------DATD--EELWAALERVGLADWL--RALPDgldtvlgeggaRLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLATVKREndLAMLYITHD 215
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-254 |
2.18e-21 |
|
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: 94.01 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP--VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRG---QDLTARgeakdehQ 88
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLA-------S 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDPFsslnpAF--TVSHHLA--RPLQLHRqsgSRTDLAEEIARLLTSVGLEPDLTRQKFPHE---LSGGQR 161
Cdd:TIGR02203 404 LRRQVALVSQDVV-----LFndTIANNIAygRTEQADR---AEIERALAAAYAQDFVDKLPLGLDTPIGENgvlLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdlAMLYITHDIATAAHvAEEIVVMFAGQMVEWGdTD 241
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERG-TH 551
|
250
....*....|...
gi 2006592715 242 TVLSDPRHPYTRL 254
Cdd:TIGR02203 552 NELLARNGLYAQL 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
28-229 |
3.18e-21 |
|
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: 93.51 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEHQYRRAVQMVFQDPFsslnpa 107
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD----ADADSWRDQIAWVPQHPF------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 fTVSHHLARPLQLHRQSGSRTDLAEEIAR-----LLTSVGLEPDLTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEP 182
Cdd:TIGR02857 407 -LFAGTIAENIRLARPDASDAEIREALERagldeFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2006592715 183 TSMLDVSIRKDILHLLATVKRENdlAMLYITHDIATAAhVAEEIVVM 229
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAA-LADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
24-238 |
1.25e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 91.94 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVhALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQYRRAVQMVFQDpfSS 103
Cdd:TIGR03797 465 GPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL----AGLDVQAVRRQLGVVLQN--GR 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 104 LNPAFTVSHHL-ARPLQLhrqsgsrtDLAEEIARLltsVGLEPDLTRqkFP---H--------ELSGGQRQRVNIARALA 171
Cdd:TIGR03797 538 LMSGSIFENIAgGAPLTL--------DEAWEAARM---AGLAEDIRA--MPmgmHtvisegggTLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKrendLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-246 |
1.31e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 89.76 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP-----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRL--FFRGQDLTARGEAKDE 86
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 H------------------QYRRAVQMVFQdpFSSLnpaftvshhlarplQLHRQS------------GSRTDLAEEIAR 136
Cdd:PRK13651 83 VleklviqktrfkkikkikEIRRRVGVVFQ--FAEY--------------QLFEQTiekdiifgpvsmGVSKEEAKKRAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 137 -LLTSVGLePDLTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLyITHD 215
Cdd:PRK13651 147 kYIELVGL-DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHD 224
|
250 260 270
....*....|....*....|....*....|.
gi 2006592715 216 IATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13651 225 LDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-246 |
1.77e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeaKDEHQ--YRR 91
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-----KLDHKlaAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQ-----DPFSSLNPAFtVSHHLAR-----PLQLHRQSGSRTdlaeeiARLLTSVGLEPDLtrQKFPHELSGGQR 161
Cdd:PRK09700 81 GIGIIYQelsviDELTVLENLY-IGRHLTKkvcgvNIIDWREMRVRA------AMMLLRVGLKVDL--DEKVANLSISHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSMLdvsIRKDILHLLATVK--RENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGD 239
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
....*..
gi 2006592715 240 TDTVLSD 246
Cdd:PRK09700 229 VSDVSND 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-244 |
2.27e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargEAKDEhQYRRAV 93
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA---TTPSR-ELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDPfsSLNPAFTVS---------HHLARPlqlhrqsgSRTDLaEEIARLLTSVGLEPdlTRQKFPHELSGGQRQRV 164
Cdd:COG4604 78 AILRQEN--HINSRLTVRelvafgrfpYSKGRL--------TAEDR-EIIDEAIAYLDLED--LADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLD----VSIRKdILHLLAtvkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDT 240
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMK-LLRRLA---DELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
....
gi 2006592715 241 DTVL 244
Cdd:COG4604 221 EEII 224
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
5-245 |
2.81e-20 |
|
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: 90.96 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 5 ANPVVtDAVIRLENIQRNFGPVHA--LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArge 82
Cdd:TIGR01846 448 ALPEL-RGAITFENIRFRYAPDSPevLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI--- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 83 aKDEHQYRRAVQMVFQDPF----------SSLNPAFTVSH--HLARPLQLHrqsgsrtDLAEEIARlltsvGLEPDLTRQ 150
Cdd:TIGR01846 524 -ADPAWLRRQMGVVLQENVlfsrsirdniALCNPGAPFEHviHAAKLAGAH-------DFISELPQ-----GYNTEVGEK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 151 KfpHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLamLYITHDIATAAHvAEEIVVMF 230
Cdd:TIGR01846 591 G--ANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLE 665
|
250
....*....|....*
gi 2006592715 231 AGQMVEWGDTDTVLS 245
Cdd:TIGR01846 666 KGQIAESGRHEELLA 680
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-246 |
3.04e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.64 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGP-----VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEH 87
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRAVQMVFQDPFSSLNPAFTVSHHLARPlqlhRQSGSRTDLAEEIA-RLLTSVGLEPDLTrQKFPHELSGGQRQRVNI 166
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVAFGP----QNFGIPKEKAEKIAaEKLEMVGLADEFW-EKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLyITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-234 |
3.23e-20 |
|
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: 85.95 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNfgpvHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehQYR 90
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDPFSS-LNPAFTVSHHLArplqlhrqsgsrtdlaeeiarlltsvglepdltrqkFPHELSGGQRQRVNIARA 169
Cdd:cd03215 75 AGIAYVPEDRKREgLVLDLSVAENIA------------------------------------LSSLLSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 170 LAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-253 |
5.75e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLdKPTG---GRLFFRGQDLTARGEAKDE 86
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 87 hqyRRAVQMVFQDpfSSLNPAFTVSHHLARPLQLHRqsGSRTDLAEEIAR---LLTSVGLEPDltrqkfPH----ELSGG 159
Cdd:PRK13549 81 ---RAGIAIIHQE--LALVKELSVLENIFLGNEITP--GGIMDYDAMYLRaqkLLAQLKLDIN------PAtpvgNLGLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 160 QRQRVNIARALAVAPSVLVADEPTSMLdvsIRKDILHLLATVK--RENDLAMLYITHDIATAAHVAeeivvmfagqmvew 237
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASL---TESETAVLLDIIRdlKAHGIACIYISHKLNEVKAIS-------------- 210
|
250
....*....|....*.
gi 2006592715 238 gDTDTVLSDPRHPYTR 253
Cdd:PRK13549 211 -DTICVIRDGRHIGTR 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-248 |
7.04e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQY-RRA 92
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI----EGLPGHQIaRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDP--FSSLnpafTVSHHLARPLQLHRQSG-------------SRTDLAEEIARLLTSVGLEPDLTRQKfpHELS 157
Cdd:PRK11300 82 VVRTFQHVrlFREM----TVIENLLVAQHQQLKTGlfsgllktpafrrAESEALDRAATWLERVGLLEHANRQA--GNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 158 GGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEW 237
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
250
....*....|.
gi 2006592715 238 GDTDTVLSDPR 248
Cdd:PRK11300 236 GTPEEIRNNPD 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-238 |
7.94e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 8 VVTDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdeH 87
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRAVQMVFQdpFSSLNPAFTVSHHLarpLQLHRQSG-SRTDLAEEIARLLTSVGLEPDLTRQKfpHELSGGQRQRVNI 166
Cdd:PRK13537 77 HARQRVGVVPQ--FDNLDPDFTVRENL---LVFGRYFGlSAAAARALVPPLLEFAKLENKADAKV--GELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 167 ARALAVAPSVLVADEPTSMLDVSIRKDILH----LLATVKrendlAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWErlrsLLARGK-----TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-248 |
1.68e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQYRRAV 93
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV----EALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSH--HLARPLQLHRQSGS----RTDLAEEIARLLTSVGLEPDLTrqkfphELSGGQRQRVNIA 167
Cdd:PRK09536 80 ASVPQD--TSLSFEFDVRQvvEMGRTPHRSRFDTWtetdRAAVERAMERTGVAQFADRPVT------SLSGGERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYItHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
.
gi 2006592715 248 R 248
Cdd:PRK09536 231 T 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-200 |
3.22e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGqdltargeaKDEHQYRRAVQMVFQDPFSSLNPAF 108
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---------GDIDDPDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQLHRQSGSRtdlaeeIARLLTSVGLePDLTRQKFpHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELD------IAAALEAVGL-APLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|..
gi 2006592715 189 SIRKDILHLLAT 200
Cdd:PRK13539 161 AAVALFAELIRA 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-245 |
3.49e-19 |
|
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: 87.55 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLD--KPTGGRLFFR----------------GQ 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 76 DLTARGEA-------------KDEHQYRRAVQMVFQDPFSsLNPAFTVSHHLARPLQlhrQSGSRTDLAEEIA-RLLTSV 141
Cdd:TIGR03269 81 PCPVCGGTlepeevdfwnlsdKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALE---EIGYEGKEAVGRAvDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 142 GLEPDLTRqkFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDvSIRKDILH--LLATVKrENDLAMLYITHDIATA 219
Cdd:TIGR03269 157 QLSHRITH--IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVHnaLEEAVK-ASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*.
gi 2006592715 220 AHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-245 |
3.88e-19 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 87.50 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeakdeHQYRRAVQMVF-----QDPfsS 103
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL---------SQWDREELGRHigylpQDV--E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 104 LNPAfTVshhlarplqlhrqsgsrtdlAEEIARLltsvglePDLTRQK----------------FP-----------HEL 156
Cdd:COG4618 417 LFDG-TI--------------------AENIARF-------GDADPEKvvaaaklagvhemilrLPdgydtrigeggARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLyITHDIAtAAHVAEEIVVMFAGQMVE 236
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVV-ITHRPS-LLAAVDKLLVLRDGRVQA 546
|
....*....
gi 2006592715 237 WGDTDTVLS 245
Cdd:COG4618 547 FGPRDEVLA 555
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-235 |
3.92e-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: 87.19 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLdKPTG---GRLFFRGQDLTARGEAKDEhqy 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDTE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQDpfSSLNPAFTVSHH--LARPLQLhrqSGSRTDLAEEIAR---LLTSVGLePDLTRQKFPHELSGGQRQRV 164
Cdd:TIGR02633 77 RAGIVIIHQE--LTLVPELSVAENifLGNEITL---PGGRMAYNAMYLRaknLLRELQL-DADNVTRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-238 |
1.04e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 81.98 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP--VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargeAKDEHQYRR 91
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-----SDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFsslnpaftvshhlarplqlhrqsgsrtdlaeeiarlLTSVGLEPDLTRQkfpheLSGGQRQRVNIARALA 171
Cdd:cd03247 76 LISVLNQRPY------------------------------------LFDTTLRNNLGRR-----FSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLamLYITHDIATAAHVaEEIVVMFAGQMVEWG 238
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-234 |
1.58e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQ---Y---RRAVQMVFQDPFSSLN 105
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglvYlpeDRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 pAFTVSHHLaRPLQLHRQSGSRTdlaeeIARLLTSVGLepdltrqKFPHE------LSGGQRQRVNIARALAVAPSVLVA 179
Cdd:PRK15439 362 -VCALTHNR-RGFWIKPARENAV-----LERYRRALNI-------KFNHAeqaartLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 180 DEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-198 |
1.61e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 81.83 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIA--RLDKPTGGRLFFRGQDLtargeakDEHQYRRAVQMVFQDpfSSLNP 106
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL-------DKRSFRKIIGYVPQD--DILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFTVSHHLarplqlhrqsgsrtdlaeEIARLLTSvglepdltrqkfpheLSGGQRQRVNIARALAVAPSVLVADEPTSML 186
Cdd:cd03213 96 TLTVRETL------------------MFAAKLRG---------------LSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170
....*....|..
gi 2006592715 187 DVSIRKDILHLL 198
Cdd:cd03213 143 DSSSALQVMSLL 154
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
34-247 |
3.38e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 81.44 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 34 FSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGqdltargeaKDEHQYRRAVQMVFQ-DPFS---SLNPAFT 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---------ASPGKGWRHIGYVPQrHEFAwdfPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 110 VSHHLARPLQLHRQSGsRTDLAEeIARLLTSVGLEpDLTRQKFpHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVS 189
Cdd:TIGR03771 72 VMSGRTGHIGWLRRPC-VADFAA-VRDALRRVGLT-ELADRPV-GELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 190 IRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEiVVMFAGQMVEWGDTDTvLSDP 247
Cdd:TIGR03771 148 TQELLTELFIELAGA-GTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQ-LQDP 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-246 |
3.45e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 3 AEANPVVTDAVIRLENIqrNFG----PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLT 78
Cdd:PRK11160 328 TTSTAAADQVSLTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 79 ARGEAkdehQYRRAVQMVFQ--DPFsslnpaftvSHHLARPLQLhrQSGSRTDlaEEIARLLTSVGLEPDLT-------- 148
Cdd:PRK11160 406 DYSEA----ALRQAISVVSQrvHLF---------SATLRDNLLL--AAPNASD--EALIEVLQQVGLEKLLEddkglnaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 149 -----RQkfpheLSGGQRQRVNIARA-LAVAPSVLVaDEPTSMLDVSIRKDILHLLATVKRENDLAMlyITHDiATAAHV 222
Cdd:PRK11160 469 lgeggRQ-----LSGGEQRRLGIARAlLHDAPLLLL-DEPTEGLDAETERQILELLAEHAQNKTVLM--ITHR-LTGLEQ 539
|
250 260
....*....|....*....|....
gi 2006592715 223 AEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-214 |
3.64e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQdltargeakdehqy 89
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 rravQMVFQDPFSSLNPAFTVSH---HLARPL---------QLHRQSG--SRTDLAEEIARLLTSVGLEPD-LTRQKfph 154
Cdd:PRK11288 67 ----EMRFASTTAALAAGVAIIYqelHLVPEMtvaenlylgQLPHKGGivNRRLLNYEAREQLEHLGVDIDpDTPLK--- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 155 ELSGGQRQRVNIARALAVAPSVLVADEPTSMLdvSIRK-DILHLLATVKRENDLAMLYITH 214
Cdd:PRK11288 140 YLSIGQRQMVEIAKALARNARVIAFDEPTSSL--SAREiEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-271 |
5.21e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 6 NPVVTDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKD 85
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL----ESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 86 EHQYRRAVQMVFQdpfsSLNPA--FTVSHHLA---RPLQLHRQSGSRTDlAEEIARLLTSVGLEPdlTRQKFPHELSGGQ 160
Cdd:PRK10575 80 SKAFARKVAYLPQ----QLPAAegMTVRELVAigrYPWHGALGRFGAAD-REKVEEAISLVGLKP--LAHRLVDSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 161 RQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDT 240
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
250 260 270
....*....|....*....|....*....|.
gi 2006592715 241 DTVLSDPrhpyTRLLLSAVPDGSRPFVTGGS 271
Cdd:PRK10575 233 AELMRGE----TLEQIYGIPMGILPHPAGAA 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-246 |
6.33e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.98 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTAR-GEAKDEHQYRRAVQMVFQDPFSSLNP 106
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AfTVSHHLA-RPLQLhrqSGSRTDLAEEIARLLTSVGLEPDLTRQKfPHELSGGQRQRVNIARALAVAPSVLVADEPTSM 185
Cdd:PRK13645 106 E-TIEKDIAfGPVNL---GENKQEAYKKVPELLKLVQLPEDYVKRS-PFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 186 LDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-216 |
1.07e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLffrgqdltargeaKDEHQYRRA 92
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 V--QMVFQDPFSSLnpafTVShhlaRPLQLhRQSGSRTDLAEEIARLLTSVGLEPDLtrQKfpheLSGGQRQRVNIARAL 170
Cdd:PRK09544 71 YvpQKLYLDTTLPL----TVN----RFLRL-RPGTKKEDILPALKRVQAGHLIDAPM--QK----LSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDI 216
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
29-239 |
2.55e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDK--PTGGRLFFRGQDLTArgEAKDEhqyrRA---VQMVFQDPfss 103
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILE--LSPDE----RAragIFLAFQYP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 104 lnPAF---TVSHHLARPLQLHRQSG-SRTDLAEEIARLLTSVGLEPD-LTRqkfphEL----SGGQRQRVNIARALAVAP 174
Cdd:COG0396 87 --VEIpgvSVSNFLRTALNARRGEElSAREFLKLLKEKMKELGLDEDfLDR-----YVnegfSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 175 SVLVADEPTSMLDVsirkDILHLLA-TVK--RENDLAMLYITH-----DIATAAHVaeeiVVMFAGQMVEWGD 239
Cdd:COG0396 160 KLAILDETDSGLDI----DALRIVAeGVNklRSPDRGILIITHyqrilDYIKPDFV----HVLVDGRIVKSGG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-241 |
3.01e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehQYRRAVQMVFQDP--FS-SL 104
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA----SLRRNIAVVFQDAglFNrSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 NPAFTVSHHLARPLQLHRQSgSRTDLAEEIAR----LLTSVGlepDLTRQkfpheLSGGQRQRVNIARALAVAPSVLVAD 180
Cdd:PRK13657 426 EDNIRVGRPDATDEEMRAAA-ERAQAHDFIERkpdgYDTVVG---ERGRQ-----LSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 181 EPTSMLDVSIRkdilhllATVKRENDLAM-----LYITHDIATAAHvAEEIVVMFAGQMVEWGDTD 241
Cdd:PRK13657 497 EATSALDVETE-------AKVKAALDELMkgrttFIIAHRLSTVRN-ADRILVFDNGRVVESGSFD 554
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-238 |
3.22e-17 |
|
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: 78.61 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGP--VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeaKDEH 87
Cdd:cd03369 3 EHGEIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST----IPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRAVQMVFQDP--FSSlnpafTVSHHLARplqlhrqSGSRTDlaEEIARLL--TSVGLEpdltrqkfpheLSGGQRQR 163
Cdd:cd03369 79 DLRSSLTIIPQDPtlFSG-----TIRSNLDP-------FDEYSD--EEIYGALrvSEGGLN-----------LSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLDVSIRkdilHLLATVKRE--NDLAMLYITHDIATAAHVAeEIVVMFAGQMVEWG 238
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATD----ALIQKTIREefTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-245 |
4.32e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ--DLTARGEAKdehqYRRAVQMVFQDPfsslnp 106
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLA----LRQQVATVFQDP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 aftvshhlarplqlhRQSGSRTDLAEEIARLLTSVGL-EPDLTR-----------QKFPHE----LSGGQRQRVNIARAL 170
Cdd:PRK13638 87 ---------------EQQIFYTDIDSDIAFSLRNLGVpEAEITRrvdealtlvdaQHFRHQpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYiTHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-238 |
4.61e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.22 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMV--FQDpfssln 105
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVhlFND------ 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 pafTVSHHLARPLQLHRqsgSRTDLaEEIARLLTSVGLepdltRQKFPH-----------ELSGGQRQRVNIARALAVAP 174
Cdd:PRK11176 432 ---TIANNIAYARTEQY---SREQI-EEAARMAYAMDF-----INKMDNgldtvigengvLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 175 SVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-220 |
4.75e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.66 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGqdltargeakdehqyRRAVQMVFQDpfSSLNPA 107
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQR--SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 F------TVSHHLARPLQLHRQSgSRTDLAEeIARLLTSVGLEpDLTRQKFpHELSGGQRQRVNIARALAVAPSVLVADE 181
Cdd:NF040873 70 LpltvrdLVAMGRWARRGLWRRL-TRDDRAA-VDDALERVGLA-DLAGRQL-GELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 2006592715 182 PTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAA 220
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVR 183
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
29-245 |
8.56e-17 |
|
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: 80.47 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtargEAKDEHQYRRAVQMVFQDpfsslnpaf 108
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL----KQWDRETFGKHIGYLPQD--------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 tvshhlarpLQLHrqSGSrtdLAEEIARLltsvglEPDLTRQKF--------PHE-------------------LSGGQR 161
Cdd:TIGR01842 401 ---------VELF--PGT---VAENIARF------GENADPEKIieaaklagVHElilrlpdgydtvigpggatLSGGQR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSMLD----VSIRKDILHLLA---TVkrendlamLYITHDIAtAAHVAEEIVVMFAGQM 234
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDeegeQALANAIKALKArgiTV--------VVITHRPS-LLGCVDKILVLQDGRI 531
|
250
....*....|.
gi 2006592715 235 VEWGDTDTVLS 245
Cdd:TIGR01842 532 ARFGERDEVLA 542
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-234 |
1.25e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.13 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARL---DKPTGGRLFFRGQDLTARGE-AKDEHQ 88
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDpFSSLNPAFTVSHHLARPLqlhrqsGS----RTDLA-------EEIARLLTSVGLepdltrQKFPHE-- 155
Cdd:PRK09984 84 SRANTGYIFQQ-FNLVNRLSVLENVLIGAL------GStpfwRTCFSwftreqkQRALQALTRVGM------VHFAHQrv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 156 --LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:PRK09984 151 stLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
.
gi 2006592715 234 M 234
Cdd:PRK09984 231 V 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-259 |
1.26e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLdKPTGGRLFFRGQDLT-------ARgeakdehqyRRAvqMVFQDpf 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSdwsaaelAR---------HRA--YLSQQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSLNPAFTVSHHLArplqLHRQSGSRTDLAE-EIARLLTSVGLEPDLTRQKfpHELSGGQRQRVNIARA-LAVAPSV--- 176
Cdd:COG4138 78 QSPPFAMPVFQYLA----LHQPAGASSEAVEqLLAQLAEALGLEDKLSRPL--TQLSGGEWQRVRLAAVlLQVWPTInpe 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 177 ---LVADEPTSMLDVSirkdilHLLATVKRENDLAMLYIT-----HDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPr 248
Cdd:COG4138 152 gqlLLLDEPMNSLDVA------QQAALDRLLRELCQQGITvvmssHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPE- 224
|
250
....*....|.
gi 2006592715 249 hpytrlLLSAV 259
Cdd:COG4138 225 ------NLSEV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-235 |
2.90e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 2 KAEANPvvTDAVIRLENIQ-RNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTAR 80
Cdd:COG3845 248 KAPAEP--GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 81 GEAKdehqyRRAVQMVF--QDPFSS-LNPAFTVSHHLArpLQLHRQSG-SR---------TDLAEEI--------ARLLT 139
Cdd:COG3845 326 SPRE-----RRRLGVAYipEDRLGRgLVPDMSVAENLI--LGRYRRPPfSRggfldrkaiRAFAEELieefdvrtPGPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 140 SVGLepdltrqkfpheLSGGQRQRVNIARALAVAPSVLVADEPTSMLDVS----IRKDILHLlatvkRENDLAMLYITHD 215
Cdd:COG3845 399 PARS------------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaiefIHQRLLEL-----RDAGAAVLLISED 461
|
250 260
....*....|....*....|....*..
gi 2006592715 216 IataahvaEE-------IVVMFAGQMV 235
Cdd:COG3845 462 L-------DEilalsdrIAVMYEGRIV 481
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-238 |
3.03e-16 |
|
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: 75.99 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP--VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdeHQYRR 91
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGL----HDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDP--FSSlnpafTVSHHLArPLQLHrqsgsrTDlaEEIARLLTSVGLEPDLTRQKFPHE---------LSGGQ 160
Cdd:cd03244 79 RISIIPQDPvlFSG-----TIRSNLD-PFGEY------SD--EELWQALERVGLKEFVESLPGGLDtvveeggenLSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 161 RQRVNIARALAVAPSVLVADEPTSMLDVSIRKdilHLLATVKRE-NDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDA---LIQKTIREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-235 |
3.43e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 4 EANPVVTDAVIRLENIQRNfgpvHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGea 83
Cdd:COG1129 247 KRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS-- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 84 kdehqYRRAVQ----MVFQDPFSS-LNPAFTVSHHLARPLQLHRQSGSRTDLAEEIA---RLLTSVGLepdltrqKFPH- 154
Cdd:COG1129 321 -----PRDAIRagiaYVPEDRKGEgLVLDLSIRENITLASLDRLSRGGLLDRRRERAlaeEYIKRLRI-------KTPSp 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 -----ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVM 229
Cdd:COG1129 389 eqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGLSDRILVM 467
|
....*.
gi 2006592715 230 FAGQMV 235
Cdd:COG1129 468 REGRIV 473
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-238 |
3.63e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 2 KAEANPV--VTDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTA 79
Cdd:PRK13536 28 EAKASIPgsMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 80 RGEAKdehqyRRAVQMVFQdpFSSLNPAFTVSHHLarpLQLHRQSGSRT-DLAEEIARLLTSVGLEPDL-TRQKfphELS 157
Cdd:PRK13536 108 RARLA-----RARIGVVPQ--FDNLDLEFTVRENL---LVFGRYFGMSTrEIEAVIPSLLEFARLESKAdARVS---DLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 158 GGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILH----LLATVKrendlAMLYITHDIATAAHVAEEIVVMFAGQ 233
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWErlrsLLARGK-----TILLTTHFMEEAERLCDRLCVLEAGR 249
|
....*
gi 2006592715 234 MVEWG 238
Cdd:PRK13536 250 KIAEG 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-237 |
3.76e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRlFFRGQDltargeakdehqyrra 92
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGET---------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVF--QDpFSSLNPAFTVSHHLARplqlhrqsGSRTDLAEEIARLLTSVGLEPDltRQ-KFPHELSGGQRQRVNIARA 169
Cdd:COG0488 378 VKIGYfdQH-QEELDPDKTVLDELRD--------GAPGGTEQEVRGYLGRFLFSGD--DAfKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 170 LAVAPSVLVADEPTSMLDVsirkDILHLLatvkrENDL-----AMLYITHDIATAAHVAEEIVVMFAGQMVEW 237
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDI----ETLEAL-----EEALddfpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-247 |
4.22e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.60 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeAKDEHQYRRAVqmVFQDPFsslnpa 107
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL--QLDSWRSRLAV--VSQTPF------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 fTVSHHLARPLQLHRQSGSRTDLaEEIARLltsVGLEPDLTR--QKFPHE-------LSGGQRQRVNIARALAVAPSVLV 178
Cdd:PRK10789 400 -LFSDTVANNIALGRPDATQQEI-EHVARL---ASVHDDILRlpQGYDTEvgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 179 ADEPTSMLDVSIRKDILHLLATVKRENdlaMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGR---TVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-264 |
5.99e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP--VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehQYRR 91
Cdd:PLN03232 1235 IKFEDVHLRYRPglPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT----DLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDP--FSSlnpafTVSHHLaRPLQLHRQSG-----SRTDLAEEIARllTSVGLEPDLTRQKfpHELSGGQRQRV 164
Cdd:PLN03232 1311 VLSIIPQSPvlFSG-----TVRFNI-DPFSEHNDADlwealERAHIKDVIDR--NPFGLDAEVSEGG--ENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVsiRKDILhLLATVKRE-NDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTV 243
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDV--RTDSL-IQRTIREEfKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
250 260
....*....|....*....|.
gi 2006592715 244 LSDPRHPYTRLLLSAVPDGSR 264
Cdd:PLN03232 1457 LSRDTSAFFRMVHSTGPANAQ 1477
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-229 |
1.18e-15 |
|
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: 72.48 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLffrgqdltargeakdehqyrrav 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 qmvfqdpfsSLNPAFTVSHhlarplqlhrqsgsrtdlaeeiarlltsvglepdltrqkFPHeLSGGQRQRVNIARALAVA 173
Cdd:cd03221 58 ---------TWGSTVKIGY---------------------------------------FEQ-LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 174 PSVLVADEPTSMLDVsirKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVM 229
Cdd:cd03221 89 PNLLLLDEPTNHLDL---ESIEALEEALKEYPG-TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-266 |
1.29e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.19 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdEHQYRRAVQMVFQDP--FSSLNpaft 109
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR-LYTVRKRMSMLFQSGalFTDMN---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 110 VSHHLARPLQLHrqsgsrTDLAEEIARL-----LTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTS 184
Cdd:PRK11831 101 VFDNVAYPLREH------TQLPAPLLHStvmmkLEAVGLRG--AAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 185 MLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMfAGQMVEWGDTDTVLSDPRHPYTRLLLSAVPDGSR 264
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIV-ADKKIVAHGSAQALQANPDPRVRQFLDGIADGPV 251
|
..
gi 2006592715 265 PF 266
Cdd:PRK11831 252 PF 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-242 |
2.85e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdEHQYrrA 92
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQL--G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDPFssLNPAFTVSHHLARPLQLHRQSGSRtdlaeeIARLLTSVGLEPDLTRQKFPHELSggQRQRVNIARALAV 172
Cdd:PRK15439 88 IYLVPQEPL--LFPNLSVKENILFGLPKRQASMQK------MKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 173 APSVLVADEPTSMLDV----SIRKDILHLLATvkrenDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDT 242
Cdd:PRK15439 158 DSRILILDEPTASLTPaeteRLFSRIRELLAQ-----GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-255 |
3.32e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.65 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTCarIIARLdkptgGRLFFRGQdLTARG-EAK--DEHQYRRAVQMVFQDPF---SSLN 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSL--LNALL-----GFLPYQGS-LKINGiELRelDPESWRKHLSWVGQNPQlphGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPLQLHrQSGSRTDLAEEIARLltSVGLEPDLTRQKFphELSGGQRQRVNIARALAVAPSVLVADEPTSM 185
Cdd:PRK11174 441 DNVLLGNPDASDEQLQ-QALENAWVSEFLPLL--PQGLDTPIGDQAA--GLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 186 LDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHVaEEIVVMFAGQMVEWGDTDTvLSDPRHPYTRLL 255
Cdd:PRK11174 516 LDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE-LSQAGGLFATLL 581
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-235 |
1.06e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeAKDEHQy 89
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNG-PKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 rRAVQMVFQDpfssLN--PAFTVshhlARPLQLHRQSGSR------TDLAEEIARLLTSVGLEPDltRQKFPHELSGGQR 161
Cdd:PRK10762 79 -AGIGIIHQE----LNliPQLTI----AENIFLGREFVNRfgridwKKMYAEADKLLARLNLRFS--SDKLVGELSIGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 162 QRVNIARALAVAPSVLVADEPTSML-DV---SIRKDILHLlatvkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALtDTeteSLFRVIREL-----KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-187 |
1.09e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 27 HALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDkPTGGRlffRGQDLTARGEAKDEHQYRRAVQMVFQDPFssLNP 106
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS-PKGVK---GSGSVLLNGMPIDAKEMRAISAYVQQDDL--FIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFTVSHHL---ARpLQLHRQSGSRTDLaEEIARLLTSVGLEP-DLTRQKFPHE---LSGGQRQRVNIARALAVAPSVLVA 179
Cdd:TIGR00955 113 TLTVREHLmfqAH-LRMPRRVTKKEKR-ERVDEVLQALGLRKcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFC 190
|
....*...
gi 2006592715 180 DEPTSMLD 187
Cdd:TIGR00955 191 DEPTSGLD 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-246 |
1.27e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgeAKDEHQYRR 91
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL---LPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPfsSLNPAFTVSHHLARPLQLHRQ--SGSRTDLAEEIARLLTSVGLepdltRQKFPHELSGGQRQRVNIARA 169
Cdd:PRK10895 79 GIGYLPQEA--SIFRRLSVYDNLMAVLQIRDDlsAEQREDRANELMEEFHIEHL-----RDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 170 LAVAPSVLVADEPTSMLD----VSIRKDILHLlatvkRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLS 245
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDpisvIDIKRIIEHL-----RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
.
gi 2006592715 246 D 246
Cdd:PRK10895 227 D 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-241 |
1.87e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 19 IQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDltargEAKDEHQYRRAVQMVF- 97
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRRKEFARRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 98 -----------QDPFsslnpaftvshhlarplQLHRQ--SGSRTDLAEEIARLLTSVGLEPDLTRQKfpHELSGGQRQRV 164
Cdd:COG4586 103 qrsqlwwdlpaIDSF-----------------RLLKAiyRIPDAEYKKRLDELVELLDLGELLDTPV--RQLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 165 NIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTD 241
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLE 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-235 |
2.56e-14 |
|
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: 70.82 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 21 RNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDltaRGEAKDEHQYRRAVQMVFQDP 100
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRKKFLRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 101 FS-SLNPA--FTVSHHLARpLQLHRQSGSRTDLAE--EIARLLTSvglePdlTRQkfpheLSGGQRQRVNIARALAVAPS 175
Cdd:cd03267 106 LWwDLPVIdsFYLLAAIYD-LPPARFKKRLDELSEllDLEELLDT----P--VRQ-----LSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 176 VLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-289 |
3.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 1 MKAEANPVVTD----------AVIRLENI----QRNFGPVhaLKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPT 66
Cdd:PLN03130 1215 LPSEAPLVIENnrpppgwpssGSIKFEDVvlryRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 67 GGRLFFRGQDLTARGEAkdehQYRRAVQMVFQDP--FSSlnpafTVSHHLaRPLQLHR-----QSGSRTDLAEEIARllT 139
Cdd:PLN03130 1293 RGRILIDGCDISKFGLM----DLRKVLGIIPQAPvlFSG-----TVRFNL-DPFNEHNdadlwESLERAHLKDVIRR--N 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 140 SVGLEPDLTR--QKFphelSGGQRQRVNIARALAVAPSVLVADEPTSMLDVsiRKDILhLLATVKRE-NDLAMLYITHDI 216
Cdd:PLN03130 1361 SLGLDAEVSEagENF----SVGQRQLLSLARALLRRSKILVLDEATAAVDV--RTDAL-IQKTIREEfKSCTMLIIAHRL 1433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 217 ATAAHvAEEIVVMFAGQMVEWGDTDTVLSDPRHPYTRLLLSavpdgsrpfvTGGS-ARFLEQ---AEKVRSLSRPES 289
Cdd:PLN03130 1434 NTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS----------TGAAnAQYLRSlvfGGDEDRLAREES 1499
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-189 |
4.09e-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: 69.69 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeakdEHQYRRAVQMVFQDPFSSLNPA 107
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-------EQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 108 FTVSHHLARplqLHRQSGSRTDLAEEiarLLTSVGLEpDLTRQKFpHELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:TIGR01189 88 LSALENLHF---WAAIHGGAQRTIED---ALAAVGLT-GFEDLPA-AQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
..
gi 2006592715 188 VS 189
Cdd:TIGR01189 160 KA 161
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-214 |
5.46e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIArldkptggrlffrgqdltarGEAKDehqyrR 91
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA--------------------GALKG-----T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFSSLNPAFTVSHHLARplqlhrqsgsRTDLAEEIaRLLTSVGL-EPDLTRQKFpHELSGGQRQRVNIARAL 170
Cdd:COG2401 84 PVAGCVDVPDNQFGREASLIDAIGR----------KGDFKDAV-ELLNAVGLsDAVLWLRRF-KELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITH 214
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-244 |
7.76e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 20 QRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ-----DLTArgeakdehqyrravq 94
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELGA--------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 95 mvfqdpfsSLNPAFTvshhlARplqlhrqsgsrtDLAEEIARLLtsvGLEPDLTRQKFPH-----EL-----------SG 158
Cdd:COG1134 98 --------GFHPELT-----GR------------ENIYLNGRLL---GLSRKEIDEKFDEivefaELgdfidqpvktySS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 159 GQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
....*.
gi 2006592715 239 DTDTVL 244
Cdd:COG1134 229 DPEEVI 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-244 |
9.10e-14 |
|
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: 68.71 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLD--KPTGGRLFFRGQDLTargEAKDEHQYRRAVQMVFQDPfsslnP 106
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT---DLPPEERARLGIFLAFQYP-----P 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFtvshhlarplqlhrqSGSRtdlaeeIARLLTSVGLepdltrqkfphELSGGQRQRVNIARALAVAPSVLVADEPTSML 186
Cdd:cd03217 88 EI---------------PGVK------NADFLRYVNE-----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 187 DVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIV-VMFAGQMVEWGDTDTVL 244
Cdd:cd03217 136 DIDALRLVAEVINKLREEG-KSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSGDKELAL 193
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-214 |
1.12e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIA--------RLDKPTGGRLFFrgqdltargeakdehqyrravqmVFQDP 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLF-----------------------LPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 101 F---SSLNPAftvshhLARPlqlhRQSGSRTDlaEEIARLLTSVGLePDL-----TRQKFPHELSGGQRQRVNIARALAV 172
Cdd:COG4178 436 YlplGTLREA------LLYP----ATAEAFSD--AELREALEAVGL-GHLaerldEEADWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDILHLLAtvKRENDLAMLYITH 214
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-244 |
1.36e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIAR---LDKptgGRLFFRgQDLT---------- 78
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYE-QDLIvarlqqdppr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 79 ----------ARG-EAKDEH--QYRRAVQMVFQDPFSS-LNpaftvshHLARpLQ--LHRQSGSRTDlaEEIARLLTSVG 142
Cdd:PRK11147 78 nvegtvydfvAEGiEEQAEYlkRYHDISHLVETDPSEKnLN-------ELAK-LQeqLDHHNLWQLE--NRINEVLAQLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 143 LEPD--LTrqkfphELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVsirkDILHLLATVKRENDLAMLYITHDIATAA 220
Cdd:PRK11147 148 LDPDaaLS------SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
250 260
....*....|....*....|....*
gi 2006592715 221 HVAEEIVVMFAGQMVEW-GDTDTVL 244
Cdd:PRK11147 218 NMATRIVDLDRGKLVSYpGNYDQYL 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-233 |
1.40e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 33 SFSL-------FPGRALALVGESGCGKTTCARIIARLDKPTGGRLffrgqDLTARGEAKDehQY-RRAVQMVFQDPFSSL 104
Cdd:PRK13409 352 DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----DPELKISYKP--QYiKPDYDGTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 NPAFTVS---HHLARPLQLHRQsgsrtdlaeeiarlltsvgLEPDLTrqkfphELSGGQRQRVNIARALAVAPSVLVADE 181
Cdd:PRK13409 425 TDDLGSSyykSEIIKPLQLERL-------------------LDKNVK------DLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 182 PTSMLDVSIRkdilhLLAT--VKR---ENDLAMLYITHDIATAAHVAEEIVVmFAGQ 233
Cdd:PRK13409 480 PSAHLDVEQR-----LAVAkaIRRiaeEREATALVVDHDIYMIDYISDRLMV-FEGE 530
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-233 |
1.84e-13 |
|
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: 68.59 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 39 GRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdehQYRRA-VQMVFQDPFSSLNPAFTVSHH---- 113
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP------QYIKAdYEGTVRDLLSSITKDFYTHPYfkte 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 114 LARPLQLhrqsgsrtdlaEEIarlltsvgLEPDLTrqkfphELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRkd 193
Cdd:cd03237 99 IAKPLQI-----------EQI--------LDREVP------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2006592715 194 iLHLLATVKR---ENDLAMLYITHDIATAAHVAEEIVVmFAGQ 233
Cdd:cd03237 152 -LMASKVIRRfaeNNEKTAFVVEHDIIMIDYLADRLIV-FEGE 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-249 |
1.86e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARlDKPTGGR---LFFRGqDLTARGE---AKDEHQYRRAVQMVFQdpfs 102
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAprgARVTG-DVTLNGEplaAIDAPRLARLRAVLPQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 103 SLNPAFTVShhlARPLQL------HRQSGSRTDLAEEIA-RLLTSVGLEPDLTRQKfpHELSGGQRQRVNIARALA---- 171
Cdd:PRK13547 91 AAQPAFAFS---AREIVLlgryphARRAGALTHRDGEIAwQALALAGATALVGRDV--TTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 -----VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSd 246
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT- 244
|
...
gi 2006592715 247 PRH 249
Cdd:PRK13547 245 PAH 247
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
29-238 |
2.04e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLfPGRA-LALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdeHQ-YRRAVQMVFQDPFSsLNP 106
Cdd:PRK10790 357 LQNINLSV-PSRGfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-----HSvLRQGVAMVQQDPVV-LAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFTVSHHLARPLQLHR--QSGSRTDLAEeIARLLtSVGLEPDLTRQKfpHELSGGQRQRVNIARALAVAPSVLVADEPTS 184
Cdd:PRK10790 430 TFLANVTLGRDISEEQvwQALETVQLAE-LARSL-PDGLYTPLGEQG--NNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 185 MLDVSIRKDILHLLATVKRENDLamLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:PRK10790 506 NIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-233 |
4.37e-13 |
|
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: 69.43 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 35 SLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLffrgqDLTARGEAKD---EHQYRRAVQMVFqdpFSSLNPAFTVS 111
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKISYKPqyiSPDYDGTVEEFL---RSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 112 ---HHLARPLQLHRQsgsrtdlaeeiarlltsvgLEPDLTrqkfphELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:COG1245 434 yykTEIIKPLGLEKL-------------------LDKNVK------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2006592715 189 SIRKDILHLLATVKRENDLAMLYITHDIATAAHVAEEIVVmFAGQ 233
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV-FEGE 532
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-247 |
1.05e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGP---VHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFrgqdltargeaKDEHQ-- 88
Cdd:PTZ00265 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII-----------NDSHNlk 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 ------YRRAVQMVFQDP-----------------------------------FSSLNPAFTVSHHLARPLQLHRQSGSR 127
Cdd:PTZ00265 452 dinlkwWRSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDS 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 128 TDLAEEIARLLTSVGLEP-DLTRQKFPHE-------------------LSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:PTZ00265 532 NELIEMRKNYQTIKDSEVvDVSKKVLIHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 188 VSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWGDTDTVLSDP 247
Cdd:PTZ00265 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-188 |
2.26e-12 |
|
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: 67.27 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFrgqdltarGEAkdehqyr 90
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------GET------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 raVQMVFQDPF-SSLNPAFTVSHHLARPLQL----HRQSGSRTdlaeEIARLLTSVGlepdlTRQKFPHELSGGQRQRVN 165
Cdd:TIGR03719 385 --VKLAYVDQSrDALDPNKTVWEEISGGLDIiklgKREIPSRA----YVGRFNFKGS-----DQQKKVGQLSGGERNRVH 453
|
170 180
....*....|....*....|...
gi 2006592715 166 IARALAVAPSVLVADEPTSMLDV 188
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-189 |
2.31e-12 |
|
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: 64.82 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLtarGEAKDEhqYRRAVQMVFQDPfsSLNPAF 108
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDS--IARGLLYLGHAP--GIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLarplQLHRQSGSRTDLAEEIARL-LTSVGLEPdltrqkfPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:cd03231 89 SVLENL----RFWHADHSDEQVEEALARVgLNGFEDRP-------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
..
gi 2006592715 188 VS 189
Cdd:cd03231 158 KA 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-234 |
2.91e-12 |
|
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: 67.35 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 16 LENIQRNFGPVH--ALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdehqYRRAV 93
Cdd:TIGR01257 931 VKNLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-----VRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfSSLNPAFTVSHHLARPLQLHRQSGSRTDLaeEIARLLTSVGLEPdlTRQKFPHELSGGQRQRVNIARALAVA 173
Cdd:TIGR01257 1006 GMCPQH--NILFHHLTVAEHILFYAQLKGRSWEEAQL--EMEAMLEDTGLHH--KRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2006592715 174 PSVLVADEPTSMLDVSIRKDILHLLatVKRENDLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-187 |
4.25e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeaKDEHQYRRavQMVFQDPFSSLNPAF 108
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----KDLCTYQK--QLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLArpLQLHRQSGsrtdlAEEIARLLTSVGLEPDLtrqKFP-HELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:PRK13540 90 TLRENCL--YDIHFSPG-----AVGITELCRLFSLEHLI---DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-238 |
5.70e-12 |
|
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: 64.09 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQD--LTARGeakdehqyrravqmvfqdpf 101
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssLLGLG-------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSLNPAFTVSHHLARPLQLHRQsgSRTDLAEEIARLLTSVGLEPDLTRQ-KfphELSGGQRQRVNIARALAVAPSVLVAD 180
Cdd:cd03220 93 GGFNPELTGRENIYLNGRLLGL--SRKEIDEKIDEIIEFSELGDFIDLPvK---TYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 181 EPTSMLDVSIRKDILHLLATvKRENDLAMLYITHDIATAAHVAEEIVVMFAGQMVEWG 238
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-201 |
1.06e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIArldkptgGRLF---FRGQDLTARGeaKDEHQYRRAVQMVFQDPFssLN 105
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQgnnFTGTILANNR--KPTKQILKRTGFVTQDDI--LY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLA------RPLQLHRQSgsRTDLAEEIARLLTSVGLEPDLTRQKFPHELSGGQRQRVNIARALAVAPSVLVA 179
Cdd:PLN03211 153 PHLTVRETLVfcsllrLPKSLTKQE--KILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180
....*....|....*....|..
gi 2006592715 180 DEPTSMLDVSIRKDILHLLATV 201
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSL 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-235 |
1.24e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 12 AVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKdehQYRR 91
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK---IMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDP--FSSLnpafTVSHHLArplqLHRQSGSRTDLAEEIARLLtsvGLEPDL--TRQKFPHELSGGQRQRVNIA 167
Cdd:PRK11614 81 AVAIVPEGRrvFSRM----TVEENLA----MGGFFAERDQFQERIKWVY---ELFPRLheRRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 168 RALAVAPSVLVADEPTSMLDVSIrkdILHLLATVK--RENDLAMLYITHDIATAAHVAEEIVVMFAGQMV 235
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPII---IQQIFDTIEqlREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-199 |
2.36e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 31 GVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdehQYRRavQMVFQDPFSSLNPAFTV 110
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-----EYHQ--DLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 111 SHHLARPLQLHRQSGsrtdlAEEIARLLTSVGLEpdlTRQKFP-HELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVS 189
Cdd:PRK13538 92 LENLRFYQRLHGPGD-----DEALWEALAQVGLA---GFEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170
....*....|
gi 2006592715 190 IRKDILHLLA 199
Cdd:PRK13538 164 GVARLEALLA 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-308 |
3.04e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTT-CARIIARLDKpTGGRLFFRG-----------QDLTAR-----GEAKDEHQYRR 91
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDK-VEGHVHMKGsvayvpqqawiQNDSLRenilfGKALNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFSSLNPaftvshhlarplqlhrqSGSRTDLAEEiarlltsvGLEpdltrqkfpheLSGGQRQRVNIARALA 171
Cdd:TIGR00957 733 VLEACALLPDLEILP-----------------SGDRTEIGEK--------GVN-----------LSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDIL-HLLATVKRENDLAMLYITHDIATAAHVaEEIVVMFAGQMVEWGDTDTVLsDPRHP 250
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL-QRDGA 854
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 251 YTRLLLSAVPDgSRPFVTGGSARFLEQAEKVRSLSRPESTVIEQVGSNHFMRALGASS 308
Cdd:TIGR00957 855 FAEFLRTYAPD-EQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSASS 911
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-230 |
3.91e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.00 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 25 PVHALKGVSFSLF------PGRALALVGESGCGKTTCARIIARLDKPTGGRL-----------FFRGQDLTARGEAKDEH 87
Cdd:cd03236 6 PVHRYGPNSFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 88 QYRRAV--QMVFQDPfsslnPAFTvshhlARPLQLHRQSGSRTDLAEEIARLltsvGLEPDLTRQKfpHELSGGQRQRVN 165
Cdd:cd03236 86 DVKVIVkpQYVDLIP-----KAVK-----GKVGELLKKKDERGKLDELVDQL----ELRHVLDRNI--DQLSGGELQRVA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 166 IARALAVAPSVLVADEPTSMLDVSIRkdiLHLLATVKR--ENDLAMLYITHDIATAAHVAEEIVVMF 230
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQR---LNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-248 |
3.97e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTC-ARIIARLdkPTGGRLFFRGQDLTargeakdehQYRRAVQMVFQDPFS-SLNPAFT 109
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLlARMAGLL--PGSGSIQFAGQPLE---------AWSAAELARHRAYLSqQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 110 --VSHHLARPLQLHRQSGSRTDLAEEIARLLtsvGLEPDLTRQKfpHELSGGQRQRVNIARA-LAVAPSV------LVAD 180
Cdd:PRK03695 84 mpVFQYLTLHQPDKTRTEAVASALNEVAEAL---GLDDKLGRSV--NQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 181 EPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSDPR 248
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-230 |
1.07e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 25 PVHALKGVSFSLF------PGRALALVGESGCGKTTCARIIARLDKPTGGRL-----------FFRGQDL------TARG 81
Cdd:COG1245 79 PVHRYGENGFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELqdyfkkLANG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 82 EAKDEH--QYRRAVQMVFQDpfsslnpafTVSHHLarplqlhrqsgSRTD---LAEEIARLLtsvGLEPDLTRQKfpHEL 156
Cdd:COG1245 159 EIKVAHkpQYVDLIPKVFKG---------TVRELL-----------EKVDergKLDELAEKL---GLENILDRDI--SEL 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIR---KDILHLLAtvkrENDLAMLYITHDIATAAHVAEEIVVMF 230
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlnvARLIRELA----EEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-230 |
1.22e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 25 PVHALKGVSFSLF------PGRALALVGESGCGKTTCARIIARLDKPTGGRL-----------FFRGQDL------TARG 81
Cdd:PRK13409 79 PVHRYGVNGFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELqnyfkkLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 82 EAKDEH--QYRRAVQMVFQDpfsslnpafTVSHHLarplqlhrqsgSRTD---LAEEIARLLtsvGLEPDLTRQKfpHEL 156
Cdd:PRK13409 159 EIKVVHkpQYVDLIPKVFKG---------KVRELL-----------KKVDergKLDEVVERL---GLENILDRDI--SEL 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDIlhllATVKRE--NDLAMLYITHDIATAAHVAEEIVVMF 230
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV----ARLIRElaEGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-187 |
1.32e-10 |
|
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: 61.87 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 27 HALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGgrlffrgqdltarGEAKDEHQYRraVQMVFQDPfsSLNP 106
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFN-------------GEARPQPGIK--VGYLPQEP--QLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFTVSHHLARPLQLHRQSGSRTD---------------LAEEIARL---LTSVGLEpDLTRQ--------KFP------H 154
Cdd:TIGR03719 82 TKTVRENVEEGVAEIKDALDRFNeisakyaepdadfdkLAAEQAELqeiIDAADAW-DLDSQleiamdalRCPpwdadvT 160
|
170 180 190
....*....|....*....|....*....|...
gi 2006592715 155 ELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-239 |
1.59e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLD--KPTGGRLFFRGQDLTargEAKDEHQYRRAVQMVFQDPFSSlnP 106
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLL---ELSPEDRAGEGIFMAFQYPVEI--P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFTVSHHLARPLQLHRQSGSR--------TDLAEEIARLLTsvgLEPDLTRQKFPHELSGGQRQRVNIARALAVAPSVLV 178
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRGQepldrfdfQDLMEEKIALLK---MPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 179 ADEPTSMLDVSIRKDILHLLATVkRENDLAMLYITHDIATAAHVAEEIV-VMFAGQMVEWGD 239
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-236 |
1.67e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 1 MKAEANPVVTDAVIRLENI-QRNFGPVhalKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTA 79
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVtSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 80 RGE---AKDEHQY----RRAvqmvfqdpfSSLNPAFTVSHHLA--RPLQLHRQSGS--------RTDLAEEIARLLT--S 140
Cdd:PRK09700 330 RSPldaVKKGMAYitesRRD---------NGFFPNFSIAQNMAisRSLKDGGYKGAmglfhevdEQRTAENQRELLAlkC 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 141 VGLEPDLTrqkfphELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAA 220
Cdd:PRK09700 401 HSVNQNIT------ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEII 473
|
250
....*....|....*.
gi 2006592715 221 HVAEEIVVMFAGQMVE 236
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-243 |
1.75e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 16 LENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQ--DLTARGEAKDEhqyrrAV 93
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALEN-----GI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 94 QMVFQDpfssLNPAFTVShhLARPLQLHR--QSGSRTD---LAEEIARLLTSVGLEPDlTRQKFPhELSGGQRQRVNIAR 168
Cdd:PRK10982 76 SMVHQE----LNLVLQRS--VMDNMWLGRypTKGMFVDqdkMYRDTKAIFDELDIDID-PRAKVA-TLSVSQMQMIEIAK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 169 ALAVAPSVLVADEPTSMLDvsiRKDILHLLATVK--RENDLAMLYITHDIATAAHVAEEIVVMFAGQmveWGDTDTV 243
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLT---EKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQ---WIATQPL 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-241 |
1.82e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 10 TDAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIArlDKP----TGGRLFFRGQDLTargEAKD 85
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESIL---DLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 86 EHQYRRAVQMVFQDPFSSlnPAFTVSHHLARPLQLHRQSGSRTDLA-----EEIARLLTSVGLEPDLTRQKFPHELSGGQ 160
Cdd:CHL00131 79 EERAHLGIFLAFQYPIEI--PGVSNADFLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPSFLSRNVNEGFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 161 RQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIV-VMFAGQMVEWGD 239
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKPDYVhVMQNGKIIKTGD 235
|
..
gi 2006592715 240 TD 241
Cdd:CHL00131 236 AE 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
8-214 |
2.16e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 8 VVTDAVIRLENIqrnfgPVHALKG------VSFSLFPGRALALVGESGCGKTTCARIIA--------RLDKPTGGRLFFR 73
Cdd:TIGR00954 446 EYQDNGIKFENI-----PLVTPNGdvliesLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 74 GQD-LTARGEAKDehqyrravQMVFQDpfsslnpaftvshhlaRPLQLHRQSGSRTDLAEeiarLLTSVGLEPDLTR--- 149
Cdd:TIGR00954 521 PQRpYMTLGTLRD--------QIIYPD----------------SSEDMKRRGLSDKDLEQ----ILDNVQLTHILERegg 572
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 150 ----QKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLatvkRENDLAMLYITH 214
Cdd:TIGR00954 573 wsavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-241 |
2.25e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCArIIARLDKPTGGRLFFRGQDLTARGEA-KDEHQYRRA 92
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRAlRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQDPFSSLNPAFTVshhlARPLQLHRQSG-SRTDLAEEIARLLTSVGlepdltrqKFPHELSGGQRQRVNIARALA 171
Cdd:NF000106 93 VR*GRRESFSGRENLYMI----GR*LDLSRKDArARADELLERFSLTEAAG--------RAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLyITHDIATAAHVAEEIVVMFAGQMVEWGDTD 241
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLL-TTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-232 |
5.91e-10 |
|
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: 58.11 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAKDEHQYRRAVQMVFQDPFSsLNPAF 108
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQLHRQSGsrtdlaeeiarLLTSVGLEPDLTRQKFPHE---------LSGGQRQRVNIARALAVAPSVLVA 179
Cdd:cd03290 96 EENITFGSPFNKQRYKA-----------VTDACSLQPDIDLLPFGDQteigerginLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 180 DEPTSMLDVSI-----RKDILHLLATVKRendlAMLYITHDIATAAHvAEEIVVMFAG 232
Cdd:cd03290 165 DDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
235-261 |
1.25e-09 |
|
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: 53.56 E-value: 1.25e-09
10 20
....*....|....*....|....*..
gi 2006592715 235 VEWGDTDTVLSDPRHPYTRLLLSAVPD 261
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPR 27
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-228 |
1.44e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 30 KGVSFSLFPGRALALVGESGCGKTTCARIIARL-DKPTGGRLFFRGQDltaRGEAKDEHQYR----RAVQMVFQDPFSSL 104
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEH---TNDMTNEQDYQgdeeQNVGMKNVNEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 NPA---------------------------------FTV--------SHHLARPLQLHRQSGSRTDLAE-----EIARLL 138
Cdd:PTZ00265 1262 KEGgsgedstvfknsgkilldgvdicdynlkdlrnlFSIvsqepmlfNMSIYENIKFGKEDATREDVKRackfaAIDEFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 139 TSVGLEPDLTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIAT 218
Cdd:PTZ00265 1342 ESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIAS 1421
|
250
....*....|
gi 2006592715 219 AAHvAEEIVV 228
Cdd:PTZ00265 1422 IKR-SDKIVV 1430
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-238 |
1.58e-09 |
|
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: 56.50 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 18 NIQRNFGPVHA----LKGVSFSLFPGRALALVGESGCGKTTCARIIArldKPTGGRLFFRGqDLTARGEAKDE--HQYRR 91
Cdd:cd03233 8 NISFTTGKGRSkipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEG-DIHYNGIPYKEfaEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 92 AVQMVFQDPFSslNPAFTVSHHLARPLQLhrqsgsrtdLAEEIARlltsvglepdltrqkfphELSGGQRQRVNIARALA 171
Cdd:cd03233 84 EIIYVSEEDVH--FPTLTVRETLDFALRC---------KGNEFVR------------------GISGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 172 VAPSVLVADEPTSMLDVSIRKDI---LHLLATVKRENDLAMLYITHDIATaaHVAEEIVVMFAGQMVEWG 238
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEIlkcIRTMADVLKTTTFVSLYQASDEIY--DLFDKVLVLYEGRQIYYG 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-188 |
2.66e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFrgqdltarGEAkdehqyr 90
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------GET------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 raVQMVFQDPF-SSLNPAFTVshhlarplqlhrqsgsrtdlAEEIarlltSVGLE----------------------PDl 147
Cdd:PRK11819 387 --VKLAYVDQSrDALDPNKTV--------------------WEEI-----SGGLDiikvgnreipsrayvgrfnfkgGD- 438
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2006592715 148 tRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:PRK11819 439 -QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
28-233 |
3.81e-09 |
|
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: 55.55 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 28 ALKGVSFSLFPGRALALVGESGCGKTT-CARIIARLDKpTGGRLFFRGQdltargeakdehqyrraVQMVFQDPFssLNP 106
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSlLSALLGELEK-LSGSVSVPGS-----------------IAYVSQEPW--IQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AfTVshhlarplqlhRQS---GSRTDlAEEIARLLTSVGLEPDLtrQKFPH-------E----LSGGQRQRVNIARALAV 172
Cdd:cd03250 80 G-TI-----------RENilfGKPFD-EERYEKVIKACALEPDL--EILPDgdlteigEkginLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 173 APSVLVADEPTSMLDVSIRKDIL-HLLATVKRENDLAMLyITHDIATAAHvAEEIVVMFAGQ 233
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-235 |
3.90e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQrnfGPvhALKG-VSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEAkdeHQY 89
Cdd:PRK11288 255 EVRLRLDGLK---GP--GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR---DAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 90 RRAVQMVFQD-------PFSSLNPAFTVS---HHLarPLQLHRQSGSRTDLAEE-IARLltsvglepdltRQKFPH---- 154
Cdd:PRK11288 327 RAGIMLCPEDrkaegiiPVHSVADNINISarrHHL--RAGCLINNRWEAENADRfIRSL-----------NIKTPSreql 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 --ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHL---LAtvkrENDLAMLYITHDIATAAHVAEEIVVM 229
Cdd:PRK11288 394 imNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNViyeLA----AQGVAVLFVSSDLPEVLGVADRIVVM 469
|
....*.
gi 2006592715 230 FAGQMV 235
Cdd:PRK11288 470 REGRIA 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
156-234 |
5.90e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 5.90e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 156 LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-198 |
8.89e-09 |
|
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: 53.70 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIA--------RLDKPTGGRLFFrgqdltargeakdehqyrravqmVFQDP 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLF-----------------------LPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 101 FsslnpaFTVshhlarplqlhrqsGSrtdLAEEIArlltsvglepdltrqkFP--HELSGGQRQRVNIARALAVAPSVLV 178
Cdd:cd03223 74 Y------LPL--------------GT---LREQLI----------------YPwdDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180
....*....|....*....|
gi 2006592715 179 ADEPTSMLDVSIRKDILHLL 198
Cdd:cd03223 115 LDEATSALDEESEDRLYQLL 134
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-234 |
1.39e-08 |
|
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: 55.60 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKT-TCARIIARLDKPTGGRLFFRGQDLTARGEAKdehQYRRAVQMVFQD-PFSSLNPAFT 109
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAQ---AIRAGIAMVPEDrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 110 VSHHLARPLqLHRQSG-SRTDLAEEIARLLTSV------GLEPDLTRQKfpheLSGGQRQRVNIARALAVAPSVLVADEP 182
Cdd:TIGR02633 356 VGKNITLSV-LKSFCFkMRIDAAAELQIIGSAIqrlkvkTASPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2006592715 183 TSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-187 |
1.75e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.40 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIArlDKPTGGrlfFRGQDLTARGEAKDEhQYRRAVQMVFQDPFssLNPAF 108
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAG---VITGEILINGRPLDK-NFQRSTGYVEQQDV--HSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 109 TVshhlarplqlhRQSgsrtdlaeeiarLLTSVGLEpdltrqkfphELSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:cd03232 95 TV-----------REA------------LRFSALLR----------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-238 |
2.67e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGEakdeHQYRRAVQMVFQDP--FS---- 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL----HDLRFKITIIPQDPvlFSgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 103 -SLNPaftvshhlarplqLHRQSGSRTDLAEEIARLLTSVGLEPDltrqKFPHE-------LSGGQRQRVNIARALAVAP 174
Cdd:TIGR00957 1378 mNLDP-------------FSQYSDEEVWWALELAHLKTFVSALPD----KLDHEcaeggenLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006592715 175 SVLVADEPTSMLDvsIRKDILhLLATVKRE-NDLAMLYITHDIATAAHVAeEIVVMFAGQMVEWG 238
Cdd:TIGR00957 1441 KILVLDEATAAVD--LETDNL-IQSTIRTQfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-232 |
3.41e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 38 PGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTArgEAKDEHQyrravQMVFQDPFSSLNPAFTVSHHLARP 117
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--NISDVHQ-----NMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 118 LQLhrqsgsRTDLAEEIARL----LTSVGLEpdLTRQKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKD 193
Cdd:TIGR01257 2037 ARL------RGVPAEEIEKVanwsIQSLGLS--LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190
....*....|....*....|....*....|....*....
gi 2006592715 194 ILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAG 232
Cdd:TIGR01257 2109 LWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-255 |
4.03e-08 |
|
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: 53.37 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 9 VTDAVIRLENiqrNFGPVhaLKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARgeakDEHQ 88
Cdd:cd03288 22 IHDLCVRYEN---NLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL----PLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQDP--FS-----SLNPAFTVSHhlarplqlhrqsgSRTDLAEEIARLLTSVGLEP---DLTRQKFPHELSG 158
Cdd:cd03288 93 LRSRLSIILQDPilFSgsirfNLDPECKCTD-------------DRLWEALEIAQLKNMVKSLPgglDAVVTEGGENFSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 159 GQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRenDLAMLYITHDIATAAHvAEEIVVMFAGQMVEWG 238
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAHRVSTILD-ADLVLVLSRGILVECD 236
|
250
....*....|....*..
gi 2006592715 239 DTDTVLSDPRHPYTRLL 255
Cdd:cd03288 237 TPENLLAQEDGVFASLV 253
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
155-245 |
6.51e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAeEIVVMFAGQM 234
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFC-DYTVMVKGTV 219
|
90
....*....|.
gi 2006592715 235 VEWGDTDTVLS 245
Cdd:PRK15056 220 LASGPTETTFT 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-187 |
7.15e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIArlDKPTGGrlFFRGqDLTARGEAKDEHQYRRAVQMVFQDPFSSlnPAF 108
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTGG--YIEG-DIRISGFPKKQETFARISGYCEQNDIHS--PQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TV------SHHLARPLQLHRQSGSRtdLAEEIARLL-------TSVGLePDLTrqkfphELSGGQRQRVNIARALAVAPS 175
Cdd:PLN03140 969 TVresliySAFLRLPKEVSKEEKMM--FVDEVMELVeldnlkdAIVGL-PGVT------GLSTEQRKRLTIAVELVANPS 1039
|
170
....*....|..
gi 2006592715 176 VLVADEPTSMLD 187
Cdd:PLN03140 1040 IIFMDEPTSGLD 1051
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-187 |
1.34e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 23 FGPVHalkgvsFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTaRGEakdehqyrRAVQMVFQDPFS 102
Cdd:PRK13543 27 FGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGD--------RSRFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 103 SLNPAFTVSHHLARPLQLHRQSGSRTDlaeeiARLLTSVGL---EPDLTRQkfpheLSGGQRQRVNIARA-LAVAPSVLV 178
Cdd:PRK13543 92 GLKADLSTLENLHFLCGLHGRRAKQMP-----GSALAIVGLagyEDTLVRQ-----LSAGQKKRLALARLwLSPAPLWLL 161
|
....*....
gi 2006592715 179 aDEPTSMLD 187
Cdd:PRK13543 162 -DEPYANLD 169
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-236 |
1.90e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 14 IRLENIQRNFG-PVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeAKDEHQYRRA 92
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT----AEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQMVFQD--PFSS-LNPAFTVSHHLARPLQLHR-QSGSRTDLAEEiaRLLTSvglepdltrqkfphELSGGQRQRVNIAR 168
Cdd:PRK10522 399 FSAVFTDfhLFDQlLGPEGKPANPALVEKWLERlKMAHKLELEDG--RISNL--------------KLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 169 ALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITHDIATAAHvAEEIVVMFAGQMVE 236
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-187 |
3.74e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIArlDKPTGGrlFFRGQDLTARGEAKDEHQYRRA--VQMvfQD---PFSS 103
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG--VITGGDRLVNGRPLDSSFQRSIgyVQQ--QDlhlPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 104 LNPAFTVSHHLARPLQLHRQsgSRTDLAEEIARLL-------TSVGLepdltrqkfPHE-LSGGQRQRVNIARALAVAPS 175
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKS--EKMEYVEEVIKLLemesyadAVVGV---------PGEgLNVEQRKRLTIGVELVAKPK 921
|
170
....*....|...
gi 2006592715 176 VLV-ADEPTSMLD 187
Cdd:TIGR00956 922 LLLfLDEPTSGLD 934
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-218 |
4.22e-07 |
|
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: 48.52 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 38 PGRALALVGESGCGKTTCARIIAR-LDKPTGGRLFFRGQDLTARGEAKDEHQYRRavqmvfqdpfsslnpaftvshhlar 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 117 plqlhrqsgsrtdlaeeiarlltsvglepdltrqKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDIL- 195
Cdd:smart00382 56 ----------------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLl 101
|
170 180
....*....|....*....|....*..
gi 2006592715 196 ----HLLATVKRENDLAMLYITHDIAT 218
Cdd:smart00382 102 leelRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-233 |
6.66e-07 |
|
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: 48.72 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 155 ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRkdiLHLLATVKR---ENDLAMLYITHDIATAAHVAEEIVVmFA 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR---LNAARAIRRlseEGKKTALVVEHDLAVLDYLSDRIHV-FE 146
|
..
gi 2006592715 232 GQ 233
Cdd:cd03222 147 GE 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-187 |
1.01e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGgrlffrgqdltarGEAKDEHQYRraVQMVFQDPfsSLNPAF 108
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFE-------------GEARPAPGIK--VGYLPQEP--QLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 109 TVSHHLARPLQLHRQSGSRTD---------------LAEEIARL---LTSVGLEpDLTRQ--------KFPH------EL 156
Cdd:PRK11819 86 TVRENVEEGVAEVKAALDRFNeiyaayaepdadfdaLAAEQGELqeiIDAADAW-DLDSQleiamdalRCPPwdakvtKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-265 |
1.13e-06 |
|
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: 45.82 E-value: 1.13e-06
10 20 30
....*....|....*....|....*....|...
gi 2006592715 233 QMVEWGDTDTVLSDPRHPYTRLLLSAVPDGSRP 265
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKR 33
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-204 |
1.65e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGG--RLFfrGQDLTARGeakdeHQ 88
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWLF--GQPVDAGD-----IA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 89 YRRAVQMVFQdPFSsLNPAFTVSHHL---ARPLQLhrqsgSRTDLAEEIARLLTSVGLEPDLtrQKFPHELSGGQRQRVn 165
Cdd:NF033858 337 TRRRVGYMSQ-AFS-LYGELTVRQNLelhARLFHL-----PAAEIAARVAEMLERFDLADVA--DALPDSLPLGIRQRL- 406
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2006592715 166 iarALAVA----PSVLVADEPTSMLDVSIRKDILHLLATVKRE 204
Cdd:NF033858 407 ---SLAVAvihkPELLILDEPTSGVDPVARDMFWRLLIELSRE 446
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-236 |
2.03e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTcariiarLDK------PTG---GRLFFRGQDLTARGEA 83
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST-------LMKvlsgvyPHGsyeGEILFDGEVCRFKDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 84 KDEHqyrRAVQMVFQDpfSSLNPAFTVSHHLArpLQLHRQSGSRTDLAEEIAR---LLTSVGLE--PDlTRQKfphELSG 158
Cdd:NF040905 74 DSEA---LGIVIIHQE--LALIPYLSIAENIF--LGNERAKRGVIDWNETNRRareLLAKVGLDesPD-TLVT---DIGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 159 GQRQRVNIARALAVAPSVLVADEPTSMLDvsiRKDILHLLATVK--RENDLAMLYITHDIATAAHVAEEIVVMFAGQMVE 236
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALN---EEDSAALLDLLLelKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-244 |
2.40e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 3 AEANPVVTDAVIR-LENIQRNFGPVHA------LKGVSFSLFPGRALALVGESGCGKTTCARIIA-RLDKptggrlFFRG 74
Cdd:TIGR00956 44 SDYQPTFPNALLKiLTRGFRKLKKFRDtktfdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDG------FHIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 75 QD--LTARGEAKDE--HQYRRAVQmvfqdpFSSLN----PAFTVSHHL-----ARPLQLHRQSGSRTDLAEEIARL-LTS 140
Cdd:TIGR00956 118 VEgvITYDGITPEEikKHYRGDVV------YNAETdvhfPHLTVGETLdfaarCKTPQNRPDGVSREEYAKHIADVyMAT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 141 VGLepDLTR-----QKFPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRE-NDLAMLYITH 214
Cdd:TIGR00956 192 YGL--SHTRntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIlDTTPLVAIYQ 269
|
250 260 270
....*....|....*....|....*....|
gi 2006592715 215 DIATAAHVAEEIVVMFAGQMVEWGDTDTVL 244
Cdd:TIGR00956 270 CSQDAYELFDKVIVLYEGYQIYFGPADKAK 299
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-238 |
3.37e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdEHQYRRAVQMVFQDPF------- 101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG----LRELRRQFSMIPQDPVlfdgtvr 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 102 SSLNPAFTVShhlarplqlhrqsgsrtdlAEEIARLLTSVGLepdltRQKFPHELSG--------------GQRQRVNIA 167
Cdd:PTZ00243 1402 QNVDPFLEAS-------------------SAEVWAALELVGL-----RERVASESEGidsrvleggsnysvGQRQLMCMA 1457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006592715 168 RALAVAPS-VLVADEPTSMLDVSIRKDIlhlLATVKRE-NDLAMLYITHDIATAAHVaEEIVVMFAGQMVEWG 238
Cdd:PTZ00243 1458 RALLKKGSgFILMDEATANIDPALDRQI---QATVMSAfSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMG 1526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-195 |
3.95e-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: 48.37 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVhaLKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLffrgqdltargeakdehqyR 90
Cdd:TIGR01271 426 DDGLFFSNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------------K 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDPFSSLNPA-------FTVSHHLARplqlHRQSGSRTDLAEEIARLL---TSVGLEPDLTrqkfpheLSGGQ 160
Cdd:TIGR01271 485 HSGRISFSPQTSWIMPGtikdniiFGLSYDEYR----YTSVIKACQLEEDIALFPekdKTVLGEGGIT-------LSGGQ 553
|
170 180 190
....*....|....*....|....*....|....*
gi 2006592715 161 RQRVNIARALAVAPSVLVADEPTSMLDVSIRKDIL 195
Cdd:TIGR01271 554 RARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-215 |
5.94e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.06 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 21 RNFGPVHALKGVSFslFPGRALaLVGESGCGKTTcarIIARL------DKPTGGRLFFRGQDLTARGE------------ 82
Cdd:cd03240 7 RNIRSFHERSEIEF--FSPLTL-IVGQNGAGKTT---IIEALkyaltgELPPNSKGGAHDPKLIREGEvraqvklafena 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 83 AKDEHQYRRAVQMVfqdpfssLNPAFTvshhlarplqlhRQSGSRTDLAEEIARLltsvglepdltrqkfphelSGGQRQ 162
Cdd:cd03240 81 NGKKYTITRSLAIL-------ENVIFC------------HQGESNWPLLDMRGRC-------------------SGGEKV 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 163 RVNIARALAVAP------SVLVADEPTSMLDV-SIRKDILHLLATVKRENDLAMLYITHD 215
Cdd:cd03240 123 LASLIIRLALAEtfgsncGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-215 |
8.22e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLfFRGQDLtargEAKDEHQYRRA 92
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKL----EVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 vqmvfqdpfssLNPAFTVSHHLA----------RP------LQlhrqsgsrtDLAEEIARLLTSVglepdltrqkfpHEL 156
Cdd:PRK11147 394 -----------LDPEKTVMDNLAegkqevmvngRPrhvlgyLQ---------DFLFHPKRAMTPV------------KAL 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 157 SGGQRQRVNIARALAVAPSVLVADEPTSMLDVsirkDILHLLATVKRENDLAMLYITHD 215
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
156-234 |
1.11e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006592715 156 LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKREnDLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-183 |
1.35e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 13 VIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTARGeakdehqYRRA 92
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR-------HRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 93 VQ-----MVfQDPFSSLNPAFTVSHHL---ARplqLHRQSgsRTDLAEEIARLLTSVGLEPDLTRQ--KfpheLSGGQRQ 162
Cdd:NF033858 74 VCpriayMP-QGLGKNLYPTLSVFENLdffGR---LFGQD--AAERRRRIDELLRATGLAPFADRPagK----LSGGMKQ 143
|
170 180
....*....|....*....|.
gi 2006592715 163 RVNIARALAVAPSVLVADEPT 183
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPT 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-187 |
1.54e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 29 LKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGgrlffrgqDLTARGEAKDE---HQYRRAVQMVFQDpfssln 105
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG--------EIQIDGVSWNSvtlQTWRKAFGVIPQK------ 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 pAFTVSHHLARPLQLHRQSGSrtdlaEEIARLLTSVGLEPDLtrQKFPHE-----------LSGGQRQRVNIARALAVAP 174
Cdd:TIGR01271 1301 -VFIFSGTFRKNLDPYEQWSD-----EEIWKVAEEVGLKSVI--EQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKA 1372
|
170
....*....|...
gi 2006592715 175 SVLVADEPTSMLD 187
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-218 |
1.59e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 26 VHALKGVSFSlFPGRALALV-GESGCGKTTCARIIarldkptggrLFFRGQDLTARGEAKDEHQyrravQMVFQDpfssl 104
Cdd:cd03238 8 VHNLQNLDVS-IPLNVLVVVtGVSGSGKSTLVNEG----------LYASGKARLISFLPKFSRN-----KLIFID----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 105 npaftvshhlarplQLhrqsgsrtdlaeeiaRLLTSVGLEPDLTRQKFPhELSGGQRQRVNIARALAVAP--SVLVADEP 182
Cdd:cd03238 67 --------------QL---------------QFLIDVGLGYLTLGQKLS-TLSGGELQRVKLASELFSEPpgTLFILDEP 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 2006592715 183 TSMLDVSirkDILHLLATVKRENDL--AMLYITHDIAT 218
Cdd:cd03238 117 STGLHQQ---DINQLLEVIKGLIDLgnTVILIEHNLDV 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-188 |
2.36e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 7 PVVTDavIRLENIQRNFGPVHALKGVSFSLFPGRALALVGESGCGKTTCARIIA--RLDK-PTGGRLF-----FRGQDLT 78
Cdd:PLN03073 173 PAIKD--IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGiPKNCQILhveqeVVGDDTT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 79 A----------RGEAKDE----HQYRRAVQM--VFQDPFSSLNPAFTVSHHLARPLQLH-RQSGSRTDLAE-EIARLLTS 140
Cdd:PLN03073 251 AlqcvlntdieRTQLLEEeaqlVAQQRELEFetETGKGKGANKDGVDKDAVSQRLEEIYkRLELIDAYTAEaRAASILAG 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2006592715 141 VGLEPDLTRQKfPHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV 188
Cdd:PLN03073 331 LSFTPEMQVKA-TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-236 |
3.12e-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: 45.17 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFFRGQDLTargeAKDEHQYRRAVQMVFQDpfsslnpaftvs 111
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT----ADNREAYRQLFSAVFSD------------ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 112 HHL-ARPLQLHrqsgsRTDLAEEIARLLTSVGLE--PDLTRQKF-PHELSGGQRQRVniarALAVA-----PsVLVADEP 182
Cdd:COG4615 415 FHLfDRLLGLD-----GEADPARARELLERLELDhkVSVEDGRFsTTDLSQGQRKRL----ALLVAlledrP-ILVFDEW 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 183 TSMLDVSIRK----DILHLLatvkRENDLAMLYITHDIAtAAHVAEEIVVMFAGQMVE 236
Cdd:COG4615 485 AADQDPEFRRvfytELLPEL----KARGKTVIAISHDDR-YFDLADRVLKMDYGKLVE 537
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-246 |
3.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 33 SFSLFPGRALALVGESGCGKTTCARIIArldkptggrlffrGQDLTARGEAkdEHQYRRAVQMVFQ-------DPFSSLN 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALA-------------GELPLLSGER--QSQFSHITRLSFEqlqklvsDEWQRNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 -----PAFTVSHHLARplQLHRQSGSRTDLAEEIARLLtsvGLEPDLTRqKFPHeLSGGQRQRVNIARALAVAPSVLVAD 180
Cdd:PRK10938 88 tdmlsPGEDDTGRTTA--EIIQDEVKDPARCEQLAQQF---GITALLDR-RFKY-LSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006592715 181 EPTSMLDVSIRKDILHLLATVKRENDLAMLYIT--HDIATAahvAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVLVLNrfDEIPDF---VQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-234 |
9.83e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 32 VSFSLFPGRALALVGESGCGKTTCARII-----ARLDkptgGRLFFRGQDLTARGEAkdeHQYRRAVQMVFQD-PFSSLN 105
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGRWE----GEIFIDGKPVKIRNPQ---QAIAQGIAMVPEDrKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 106 PAFTVSHHLARPLqLHRQS-GSRTDLAEEIARLLTSVglepDLTRQKFPH------ELSGGQRQRVNIARALAVAPSVLV 178
Cdd:PRK13549 354 PVMGVGKNITLAA-LDRFTgGSRIDDAAELKTILESI----QRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 179 ADEPTSMLDVSIRKDILHLLATVKRENdLAMLYITHDIATAAHVAEEIVVMFAGQM 234
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-194 |
1.36e-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: 42.92 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 11 DAVIRLENIQRNFGPVhaLKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLffrgqdltargeakdehqyR 90
Cdd:cd03291 37 DNNLFFSNLCLVGAPV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------------K 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 91 RAVQMVFQDPFSSLNPA-------FTVSHHLARPLQLHRQSGSRTDLAEEIARLLTSVGlEPDLTrqkfpheLSGGQRQR 163
Cdd:cd03291 96 HSGRISFSSQFSWIMPGtikeniiFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLG-EGGIT-------LSGGQRAR 167
|
170 180 190
....*....|....*....|....*....|.
gi 2006592715 164 VNIARALAVAPSVLVADEPTSMLDVSIRKDI 194
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
138-214 |
2.00e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 2.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006592715 138 LTSVGLEPDLTRQKFpHELSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDLAMLYITH 214
Cdd:PRK10938 385 LDILGIDKRTADAPF-HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
156-226 |
2.73e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 156 LSGGQRQRVNIARALAVAP------SVLVADEPTSMLDVSIRKDILHLLA-TVKRENDL-AMLYITH--DIATAAHVAEE 225
Cdd:PRK01156 802 LSGGEKTAVAFALRVAVAQflnndkSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIpQVIMISHhrELLSVADVAYE 881
|
.
gi 2006592715 226 I 226
Cdd:PRK01156 882 V 882
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-246 |
6.85e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 27 HALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGrlffrgqDLTARGEakdehqyrraVQMVfqdpfsSLNP 106
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNGE----------VSVI------AISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 107 AFtvshhlarplqlhrqSGSRTDLaEEIARLLTSVGLEPDLTRQKFPH-----EL-----------SGGQRQRVNIARAL 170
Cdd:PRK13546 95 GL---------------SGQLTGI-ENIEFKMLCMGFKRKEIKAMTPKiiefsELgefiyqpvkkySSGMRAKLGFSINI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006592715 171 AVAPSVLVADEPTSMLDVSIRKDILHLLATVKRENDlAMLYITHDIATAAHVAEEIVVMFAGQMVEWGDTDTVLSD 246
Cdd:PRK13546 159 TVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
156-187 |
1.12e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|..
gi 2006592715 156 LSGGQRQRVNIARALAVAPSVLVADEPTSMLD 187
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
137-215 |
1.64e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 137 LLTSVGLEPDLtrqkfpH-----ELSGGQRQRVNIARALAVAPSVLVADEPTSMLDV-SIRkdilhLLATVKRENDLAML 210
Cdd:PRK15064 138 LLLGVGIPEEQ------HyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDVLNERNSTMI 206
|
....*
gi 2006592715 211 YITHD 215
Cdd:PRK15064 207 IISHD 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-248 |
1.80e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 130 LAEEIARL--LTSVGLePDLTRQKFPHELSGGQRQRVNIARALAVAPS-VL-VADEPtsmldvSI---RKDILHLLATVK 202
Cdd:TIGR00630 462 LKEIRERLgfLIDVGL-DYLSLSRAAGTLSGGEAQRIRLATQIGSGLTgVLyVLDEP------SIglhQRDNRRLINTLK 534
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2006592715 203 RENDL--AMLYITHDIATAAHvAEEIVVM------FAGQMVEWGDTDTVLSDPR 248
Cdd:TIGR00630 535 RLRDLgnTLIVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANPD 587
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-188 |
2.34e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 24 GPVhALKGVSFSLFPGRALALVGESGCGKTTCARIIARLDKPTGGRLFfrgqdltargeakDEHQYRRAVqmvfqdpFSS 103
Cdd:PLN03073 521 GPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------------RSAKVRMAV-------FSQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 104 lnpaftvsHHL------ARPLqLHRQSGSRTDLAEEIARLLTSVGLEPDLTRQKFpHELSGGQRQRVNIARALAVAPSVL 177
Cdd:PLN03073 580 --------HHVdgldlsSNPL-LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPM-YTLSGGQKSRVAFAKITFKKPHIL 649
|
170
....*....|.
gi 2006592715 178 VADEPTSMLDV 188
Cdd:PLN03073 650 LLDEPSNHLDL 660
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
34-61 |
6.38e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 37.97 E-value: 6.38e-03
10 20
....*....|....*....|....*...
gi 2006592715 34 FSLFPGRALALVGESGCGKTTCARIIAR 61
Cdd:COG0464 186 YGLPPPRGLLLYGPPGTGKTLLARALAG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
156-195 |
6.52e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 38.42 E-value: 6.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2006592715 156 LSGGQRQRVNIARALAVAPSVLVADEPTSMLDVSIRKDIL 195
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| PRK14964 |
PRK14964 |
DNA polymerase III subunits gamma and tau; Provisional |
44-60 |
8.26e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237870 [Multi-domain] Cd Length: 491 Bit Score: 37.84 E-value: 8.26e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-222 |
8.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006592715 136 RLLTSVGLE------PDLTrqkfpheLSGGQRQRVNIARAL---AVAPSVLVADEPTSMLDVSirkDILHLLATVKREND 206
Cdd:TIGR00630 811 QTLCDVGLGyirlgqPATT-------LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFD---DIKKLLEVLQRLVD 880
|
90 100
....*....|....*....|.
gi 2006592715 207 L--AMLYITHD---IATAAHV 222
Cdd:TIGR00630 881 KgnTVVVIEHNldvIKTADYI 901
|
|
| |
