|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-243 |
1.02e-140 |
|
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: 393.96 E-value: 1.02e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIA 90
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGA-SLDNQQYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLGAyARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-235 |
1.11e-122 |
|
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: 347.88 E-value: 1.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQS 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 173 LGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-245 |
7.92e-97 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 282.92 E-value: 7.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRIFPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYLEG 245
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-241 |
1.95e-82 |
|
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: 245.90 E-value: 1.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQS 92
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGASL--DNQQYFDEDVklmFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAAlpRRSRKIPDEI---YELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRElLSDPEVRAA 241
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE-LDEDKVRRY 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-248 |
1.29e-68 |
|
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: 211.82 E-value: 1.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 A---QSPegrRIFPRMTVLENLQMGASLDNQQYFDEDVkLMFDLFPR-----------------LKERINQRGGTLSGGE 149
Cdd:COG0411 82 ArtfQNP---RLFPELTVLENVLVAAHARLGRGLLAAL-LRLPRARReereareraeellervgLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 150 QQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSG 229
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250
....*....|....*....
gi 492862668 230 RELLSDPEVRAAYLeGGRH 248
Cdd:COG0411 238 AEVRADPRVIEAYL-GEEA 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-238 |
7.58e-64 |
|
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: 198.82 E-value: 7.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIA-- 90
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 -QSPegrRIFPRMTVLENLQMGASLDNQQYF---------DEDVKLMFDL--FPRLKERINQRGGTLSGGEQQMLAIARA 158
Cdd:cd03219 81 fQIP---RLFPELTVLENVMVAAQARTGSGLllararreeREARERAEELleRVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-243 |
5.84e-56 |
|
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: 178.89 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQS 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGASL--DNQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIrgLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 171 PSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-244 |
6.64e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.71 E-value: 6.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiAKLRIAQS 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE--VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGASL--DNQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLygLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELlsdpevRAAYLE 244
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL------KARLLE 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-243 |
1.18e-49 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 162.83 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQS 92
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLEN----LQMGASLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:TIGR04406 82 PQEASIFRKLTVEENimavLEIRKDLDRAEREERLEALLEEF--QISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYL 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-243 |
2.17e-49 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 162.12 E-value: 2.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI- 89
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 --AQSPEgrrIFPRMTVLEN----LQMgASLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARP 163
Cdd:COG1137 82 ylPQEAS---IFRKLTVEDNilavLEL-RKLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYL 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-242 |
9.65e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 158.30 E-value: 9.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR- 88
Cdd:COG3638 1 PMLELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 ----IAQSPegrRIFPRMTVLENLQMGA--------SLdNQQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLA 154
Cdd:COG3638 81 rigmIFQQF---NLVPRLSVLTNVLAGRlgrtstwrSL-LGLFPPEDRERALEALERvgLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 155 IARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFL----VEQnafgALKLADRGYVMVNGSITMSGSGR 230
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVnlhqVDL----ARRYADRIIGLRDGRVVFDGPPA 232
|
250
....*....|..
gi 492862668 231 ElLSDPEVRAAY 242
Cdd:COG3638 233 E-LTDAVLREIY 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-224 |
1.57e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.74 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIA 85
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 86 KLR------IAQSPEgrrIFPRMTVLENLQMGASLDNQQYFD--EDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIAR 157
Cdd:COG1136 82 RLRrrhigfVFQFFN---LLPELTALENVALPLLLAGVSRKErrERARELLERV-GLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 158 ALMARPKLLLLDEP--SL----GlaplivKQIFEAIKELNRTQGLTVFLVEQNAFgALKLADRGYVMVNGSIT 224
Cdd:COG1136 158 ALVNRPKLILADEPtgNLdsktG------EEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIV 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-237 |
9.69e-46 |
|
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: 152.49 E-value: 9.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA- 90
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRR-KVGl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 --QSPEgRRIFpRMTVLENLQMGasLDNQQYFDEDVKL-------MFDLFPRLKERINQrggtLSGGEQQMLAIARALMA 161
Cdd:COG1122 80 vfQNPD-DQLF-APTVEEDVAFG--PENLGLPREEIRErveealeLVGLEHLADRPPHE----LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-236 |
1.46e-45 |
|
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: 158.91 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 2 QAETMQKKQPLLSVEKVETYY-----GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDI 76
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 77 TSMPPHEIAKLR-----IAQSPEGrRIFPRMTVLENLQMGasLDNQQYFDED------VKLM--FDLFPRLKERinqRGG 143
Cdd:COG1123 330 TKLSRRSLRELRrrvqmVFQDPYS-SLNPRMTVGDIIAEP--LRLHGLLSRAerrervAELLerVGLPPDLADR---YPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 144 TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLT-VF------LVEQnafgalkLADRGY 216
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFishdlaVVRY-------IADRVA 476
|
250 260
....*....|....*....|
gi 492862668 217 VMVNGSITMSGSGRELLSDP 236
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANP 496
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-244 |
1.47e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 152.32 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiAKLRIAQ 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRIFPRMTVLENLQMGASLdnQQYFDEDVKLMFD-LFPRLK--ERINQRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAEL--YGLFDEELKKRIEeLIELLGleEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSG---RELLSDPEVRAAYLE 244
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLdelREEIGEENLEDAFVA 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-223 |
3.05e-45 |
|
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: 149.47 E-value: 3.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPphEIAKLRIAQS 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQmgasldnqqyfdedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:cd03230 79 PEEPSLYENLTVRENLK-----------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492862668 173 LGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:cd03230 124 SGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-223 |
3.86e-45 |
|
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: 150.72 E-value: 3.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR 88
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 iaqspegRR----IF------PRMTVLENLQMGASLDNQQYFDEDVKLMfDLFPR--LKERINQRGGTLSGGEQQMLAIA 156
Cdd:cd03255 81 -------RRhigfVFqsfnllPDLTALENVELPLLLAGVPKKERRERAE-ELLERvgLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 157 RALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGAlKLADRGYVMVNGSI 223
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-242 |
5.24e-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: 151.35 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA- 90
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR-RIAy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 --QSPEGRriFPrMTVLENLQMG--ASLDN-QQYFDEDVKL------MFDLFPrLKERinqRGGTLSGGEQQMLAIARAL 159
Cdd:COG1120 80 vpQEPPAP--FG-LTVRELVALGryPHLGLfGRPSAEDREAveealeRTGLEH-LADR---PVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 160 MARPKLLLLDEPslgLAPLIVK---QIFEAIKELNRTQGLTVFLV----EQnafgALKLADRGYVMVNGSITMSGSGREL 232
Cdd:COG1120 153 AQEPPLLLLDEP---TSHLDLAhqlEVLELLRRLARERGRTVVMVlhdlNL----AARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|
gi 492862668 233 LSDPEVRAAY 242
Cdd:COG1120 226 LTPELLEEVY 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-242 |
9.35e-45 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 150.41 E-value: 9.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNI-CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR--- 88
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 --IAQSPegrRIFPRMTVLENLQMGAsLDN--------QQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIA 156
Cdd:cd03256 81 gmIFQQF---NLIERLSVLENVLSGR-LGRrstwrslfGLFPKEEKQRALAALERvgLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 157 RALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRElLSDP 236
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDE 235
|
....*.
gi 492862668 237 EVRAAY 242
Cdd:cd03256 236 VLDEIY 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-223 |
1.06e-44 |
|
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: 149.21 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiaKLRIAQS 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGasLDNQQYFDEDVK-------LMFDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKL 165
Cdd:cd03259 78 FQDYALFPHLTVAENIAFG--LKLRGVPKAEIRarvrellELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-221 |
2.84e-44 |
|
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: 148.00 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 23 GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA---QSPEgRRIF 99
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR-KVGlvfQNPD-DQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 pRMTV-------LENLQMGASLDNQQyfDEDVKLMFDLFPRLKERINqrggTLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:cd03225 90 -GPTVeeevafgLENLGLPEEEIEER--VEEALELVGLEGLRDRSPF----TLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492862668 173 LGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNG 221
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-240 |
5.59e-43 |
|
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: 145.51 E-value: 5.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRi 89
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 aqspegRRI---------FPRMTVLEN----LQMGASLDNQQYFD------EDVKL--MFDLFPrlkerinqrgGTLSGG 148
Cdd:COG1127 82 ------RRIgmlfqggalFDSLTVFENvafpLREHTDLSEAEIRElvleklELVGLpgAADKMP----------SELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 149 EQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGS 228
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
250
....*....|....
gi 492862668 229 GRELL--SDPEVRA 240
Cdd:COG1127 226 PEELLasDDPWVRQ 239
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-171 |
6.38e-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: 142.79 E-value: 6.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsMPPHEIAKLRIAQSPEGRRIFPRMTVLEN 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 108 LQMGASLDNQQYFDEDVKL-----MFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAeealeKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-243 |
9.21e-43 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 145.52 E-value: 9.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRIFPRMTVLENL------QMGA------------------SLDNQQYFDEDVKlmfdlfprLKERINQRGGTL 145
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLlvaqhqQLKTglfsgllktpafrraeseALDRAATWLERVG--------LLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 146 SGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITM 225
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
250
....*....|....*...
gi 492862668 226 SGSGRELLSDPEVRAAYL 243
Cdd:PRK11300 235 NGTPEEIRNNPDVIKAYL 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-241 |
2.40e-42 |
|
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: 150.44 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYY--GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG---SPRARTGRILFNGKDITSMPPHEI 84
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 85 AKLR--IAQSPEGRriFPRMTVLEnlQMGASLDNQQY----FDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARA 158
Cdd:COG1123 82 GRRIgmVFQDPMTQ--LNPVTVGD--QIAEALENLGLsraeARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
...
gi 492862668 239 RAA 241
Cdd:COG1123 237 LAA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-236 |
1.05e-41 |
|
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: 142.09 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNIcALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiaKLRIAQS 92
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMG--ASLDNQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGlkKRKVDKKEIERKVLEIAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-236 |
1.10e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 145.24 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 9 KQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTI--FGSPRArtGRILFNGKDITSMPPHEiak 86
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFETPDS--GRILLDGRDVTGLPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 87 lriaqspegRRI---------FPRMTVLEN----LQM-GASLDNQqyfDEDVKLMFDLFpRLKERINQRGGTLSGGEQQM 152
Cdd:COG3842 77 ---------RNVgmvfqdyalFPHLTVAENvafgLRMrGVPKAEI---RARVAELLELV-GLEGLADRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 153 LAIARALMARPKLLLLDEPSLGL-APLIVKQIFEaIKELNRTQGLTVFLV-----EqnafgALKLADRGYVMVNGSITMS 226
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALdAKLREEMREE-LRRLQRELGITFIYVthdqeE-----ALALADRIAVMNDGRIEQV 217
|
250
....*....|
gi 492862668 227 GSGRELLSDP 236
Cdd:COG3842 218 GTPEEIYERP 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-239 |
1.66e-41 |
|
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: 141.61 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQS 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegRRIFPRMTVLENLQMGASLD--NQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03300 81 ---YALFPHLTVFENIAFGLRLKklPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVR 239
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-198 |
3.45e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.57 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRiaqspegRRI- 98
Cdd:COG2884 10 RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-------RRIg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 --------FPRMTVLENLQ-----MGASLDNQQyfdEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKL 165
Cdd:COG2884 83 vvfqdfrlLPDRTVYENVAlplrvTGKSRKEIR---RRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190
....*....|....*....|....*....|...
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELNRTqGLTV 198
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRR-GTTV 190
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-232 |
1.08e-40 |
|
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: 139.24 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG----SPRART-GRILFNGKDITSMPPHEIA-K 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlIPGAPDeGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 87 LRIA---QSPegrriFP-RMTVLENLQMGASL---DNQQYFDEDVK---LMFDLFPRLKERINQRGgtLSGGEQQMLAIA 156
Cdd:cd03260 81 RRVGmvfQKP-----NPfPGSIYDNVAYGLRLhgiKLKEELDERVEealRKAALWDEVKDRLHALG--LSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 157 RALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTqgLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGREL 232
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-239 |
1.62e-40 |
|
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: 139.17 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRiaqs 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegRRI---------FPRMTVLENLQMGASldnqQYFDEDVKLMFDL------FPRLKERINQRGGTLSGGEQQMLAIAR 157
Cdd:cd03261 77 ---RRMgmlfqsgalFDSLTVFENVAFPLR----EHTRLSEEEIREIvlekleAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 158 ALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLS--D 235
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdD 229
|
....
gi 492862668 236 PEVR 239
Cdd:cd03261 230 PLVR 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-242 |
4.29e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 4.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 8 KKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmppheiAKL 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 RIA---QSPEGRRIFPrMTVLENLQMGasldnqqyFDEDVKLMFDLFPRLKERI-------------NQRGGTLSGGEQQ 151
Cdd:COG1121 76 RIGyvpQRAEVDWDFP-ITVRDVVLMG--------RYGRRGLFRRPSRADREAVdealervgledlaDRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 152 MLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRgYVMVNGSITMSGSGRE 231
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
250
....*....|.
gi 492862668 232 LLSDPEVRAAY 242
Cdd:COG1121 225 VLTPENLSRAY 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-223 |
7.41e-40 |
|
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: 136.89 E-value: 7.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmPPHEIAKLRiaqs 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegRRI---------FPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARALMA 161
Cdd:cd03262 76 ---QKVgmvfqqfnlFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTqGLTVFLV-EQNAFgALKLADRGYVMVNGSI 223
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVtHEMGF-AREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-221 |
7.81e-40 |
|
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: 135.78 E-value: 7.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsmppheiaKLRIAQS 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--------DLEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRI---------FPRMTVLENLQMGasldnqqyfdedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARP 163
Cdd:cd03229 73 PLRRRIgmvfqdfalFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNG 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-237 |
9.13e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.43 E-value: 9.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsMPPHEIAKLRiaq 91
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 spegRRI---------FPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARALM 160
Cdd:COG1126 77 ----RKVgmvfqqfnlFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLV--EQnAFgALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVthEM-GF-AREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-221 |
2.47e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG--SPRArtGRILFNGKDITSMPPHEiakLR-- 88
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADldPPTS--GEIYLDGKPLSAMPPPE---WRrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 ---IAQSPegrRIFPrMTVLENLQMGASLDNQQYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKL 165
Cdd:COG4619 76 vayVPQEP---ALWG-GTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNG 221
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-223 |
2.89e-39 |
|
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: 135.71 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKL 87
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 R-----IAQSPeGRRIFPRMTV----LENLQMGASLDNQQYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARA 158
Cdd:cd03257 81 RkeiqmVFQDP-MSSLNPRMTIgeqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNaFGALK-LADRGYVMVNGSI 223
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVAkIADRVAVMYAGKI 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-231 |
5.97e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.98 E-value: 5.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 26 CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLrIAqspegrRIF------ 99
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IG------RVFqdpmmg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 --PRMTVLENLQM----------GASLDNQQ--YFDEDVKLMfDLfpRLKERINQRGGTLSGGEQQMLAIARALMARPKL 165
Cdd:COG1101 93 taPSMTIEENLALayrrgkrrglRRGLTKKRreLFRELLATL-GL--GLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRE 231
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEE 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-236 |
7.59e-39 |
|
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: 137.11 E-value: 7.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYY----GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG--SPRART-GRILFNGKDITSMPPHEI 84
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllPPPGITsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 85 AKLRiaqspeGRR---IF--------PRMTVLEnlQMGASLDNQQYFDED-----VKLMFDL--FPRLKERINQRGGTLS 146
Cdd:COG0444 81 RKIR------GREiqmIFqdpmtslnPVMTVGD--QIAEPLRIHGGLSKAearerAIELLERvgLPDPERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 147 GGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFL-------VEQnafgalkLADRGYVMV 219
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFithdlgvVAE-------IADRVAVMY 225
|
250
....*....|....*..
gi 492862668 220 NGSITMSGSGRELLSDP 236
Cdd:COG0444 226 AGRIVEEGPVEELFENP 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-227 |
9.53e-39 |
|
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: 132.94 E-value: 9.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 14 SVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSP 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR-KIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 94 egrrifprmTVLENLQMgASLDNQQYfdedvklmfdlfprlkerinqrgGTLSGGEQQMLAIARALMARPKLLLLDEPsl 173
Cdd:cd03214 80 ---------QALELLGL-AHLADRPF-----------------------NELSGGERQRVLLARALAQEPPILLLDEP-- 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 174 gLAPLIVK---QIFEAIKELNRTQGLTVFLV--EQNAfgALKLADRGYVMVNGSITMSG 227
Cdd:cd03214 125 -TSHLDIAhqiELLELLRRLARERGKTVVMVlhDLNL--AARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-221 |
1.81e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 131.60 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 14 SVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSP 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 94 EgrrifprmtvlenlqmgasldnqqyfdedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492862668 174 GLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNG 221
Cdd:cd00267 110 GLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-237 |
1.82e-38 |
|
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: 134.16 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYG----NICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKl 87
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 RIA---QSPEGRrIFPRMTVLENLQMGASLDNQQYFDEDVKLMFD---LFPRLKERinqRGGTLSGGEQQMLAIARALMA 161
Cdd:COG1124 80 RVQmvfQDPYAS-LHPRHTVDRILAEPLRIHGLPDREERIAELLEqvgLPPSFLDR---YPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-232 |
5.07e-38 |
|
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: 132.24 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNIC--ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiAKLRIA 90
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGASLD--NQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKglPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGREL 232
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-232 |
6.21e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 138.23 E-value: 6.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 A---QSPEgrrIFPRMTVLENLQMGASLDNQQYFDEdvKLMF----DLFPRLKERIN--QRGGTLSGGEQQMLAIARALM 160
Cdd:COG1129 82 AiihQELN---LVPNLSVAENIFLGREPRRGGLIDW--RAMRrrarELLARLGLDIDpdTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTV-----FLVEqnafgALKLADRGYVMVNGSITMSGSGREL 232
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIiyishRLDE-----VFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-243 |
1.82e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 131.55 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQ 91
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRIFPRMTVLEN----LQMGASLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLL 167
Cdd:PRK10895 83 LPQEASIFRRLSVYDNlmavLQIRDDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 168 LDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-227 |
5.69e-37 |
|
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: 129.19 E-value: 5.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 14 SVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsMPPHEIAKLriAQSP 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-KERKRIGYV--PQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 94 EGRRIFPrMTVLENLQMGA--------SLDNQQYFDEDVKL----MFDLfprlkerINQRGGTLSGGEQQMLAIARALMA 161
Cdd:cd03235 78 SIDRDFP-ISVRDVVLMGLyghkglfrRLSKADKAKVDEALervgLSEL-------ADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRgYVMVNGSITMSG 227
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-226 |
6.08e-37 |
|
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: 127.54 E-value: 6.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAqs 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegrrifprmtvlenlqmgasldnqqyfdedvklmfdlfprlkeRINQrggtLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:cd03216 79 --------------------------------------------MVYQ----LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492862668 173 LGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMS 226
Cdd:cd03216 111 AALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-227 |
2.23e-36 |
|
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: 127.87 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 23 GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiAKLRIAQSPEGRRIFPRM 102
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLENLQMGASLD--NQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIV 180
Cdd:cd03266 94 TARENLEYFAGLYglKGDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492862668 181 KQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03266 173 RALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-234 |
2.68e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 134.50 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlR 88
Cdd:COG4988 334 PPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-Q 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 IA---QSPegrRIFPrMTVLENLQMG---ASLDNQQYFDEDVKLMfDLFPRLKE----RINQRGGTLSGGEQQMLAIARA 158
Cdd:COG4988 413 IAwvpQNP---YLFA-GTIRENLRLGrpdASDEELEAALEAAGLD-EFVAALPDgldtPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNAfGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-236 |
1.02e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.07 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 1 MQAETMQKKqPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMP 80
Cdd:PRK09452 4 LNKQPSSLS-PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 81 pheiaklriaqsPEGRRI---------FPRMTVLENLQMGasLDNQQYFDEDVK-LMFDLFP--RLKERINQRGGTLSGG 148
Cdd:PRK09452 83 ------------AENRHVntvfqsyalFPHMTVFENVAFG--LRMQKTPAAEITpRVMEALRmvQLEEFAQRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 149 EQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGS 228
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
....*...
gi 492862668 229 GRELLSDP 236
Cdd:PRK09452 229 PREIYEEP 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-236 |
1.32e-35 |
|
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: 126.65 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPheiAKLRiaqspegRRI- 98
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELR-------RKIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 --------FPRMTVLENLQMGASLDN------QQYFDEDVKLMfDLFPrlKERINQRGGTLSGGEQQMLAIARALMARPK 164
Cdd:cd03295 79 yviqqiglFPHMTVEENIALVPKLLKwpkekiRERADELLALV-GLDP--AEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 165 LLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-242 |
2.19e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDI-TSMPPHEiaklriaq 91
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 spegRRI---------FPRMTVLENLQMGAS---LDNQQyFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARAL 159
Cdd:COG1118 75 ----RRVgfvfqhyalFPHMTVAENIAFGLRvrpPSKAE-IRARVEELLELV-QLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 160 MARPKLLLLDEPsLG-----LAPLIVKQIFEAIKELNRTqglTVF----LVEqnafgALKLADRGYVMVNGSITMSGSGR 230
Cdd:COG1118 149 AVEPEVLLLDEP-FGaldakVRKELRRWLRRLHDELGGT---TVFvthdQEE-----ALELADRVVVMNQGRIEQVGTPD 219
|
250
....*....|..
gi 492862668 231 ELLSDPEVRAAY 242
Cdd:COG1118 220 EVYDRPATPFVA 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
27-234 |
3.15e-35 |
|
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: 132.65 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSPEGRRIFPRmTVLE 106
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR-QIGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGA-SLDNQQY--------FDEDVKLM---FDLfprlkeRINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLG 174
Cdd:COG2274 568 NITLGDpDATDEEIieaarlagLHDFIEALpmgYDT------VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 175 LAPLIVKQIFEAIKELnrTQGLTVFLVeqnafgA-----LKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:COG2274 642 LDAETEAIILENLRRL--LKGRTVIII------AhrlstIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-199 |
6.62e-35 |
|
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: 123.74 E-value: 6.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiAKLRIA 90
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180
....*....|....*....|....*....
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRTQGLTVF 199
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-223 |
8.37e-35 |
|
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: 122.93 E-value: 8.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYgnicALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIA 90
Cdd:cd03215 3 PVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRR---IFPRMTVLENLQMGASldnqqyfdedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLL 167
Cdd:cd03215 79 YVPEDRKregLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 168 LDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLV-----EqnafgALKLADRGYVMVNGSI 223
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLIsseldE-----LLGLCDRILVMYEGRI 182
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-237 |
1.32e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 129.89 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 9 KQPLLSVEKVE-TYYGNI-CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAK 86
Cdd:COG4987 330 GGPSLELEDVSfRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 87 lRIA---QSPEgrrIFpRMTVLENLQMG---ASldnqqyfDEDVKLMF------DLFPRLKE----RINQRGGTLSGGEQ 150
Cdd:COG4987 410 -RIAvvpQRPH---LF-DTTLRENLRLArpdAT-------DEELWAALervglgDWLAALPDgldtWLGEGGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 151 QMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNAFGaLKLADRGYVMVNGSITMSGSGR 230
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA--LAGRTVLLITHRLAG-LERMDRILVLEDGRIVEQGTHE 554
|
....*..
gi 492862668 231 ELLSDPE 237
Cdd:COG4987 555 ELLAQNG 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-221 |
1.39e-34 |
|
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: 121.72 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA---QSPEgrrIFPrMT 103
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK-NIAyvpQDPF---LFS-GT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 VLENLqmgasldnqqyfdedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQI 183
Cdd:cd03228 92 IRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 492862668 184 FEAIKELnrTQGLTVFLVEQNaFGALKLADRGYVMVNG 221
Cdd:cd03228 136 LEALRAL--AKGKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-235 |
1.85e-34 |
|
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: 122.64 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRART--GRILFNGKDITSMPPHEIAKLRIA---QSP---EGRRIf 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEERARLGIFlafQYPpeiPGVKN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 prMTVLENLQMGasldnqqyfdedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLI 179
Cdd:cd03217 95 --ADFLRYVNEG---------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 180 VKQIFEAIKELnRTQGLTVFLVE--QNAFGALKlADRGYVMVNGSITMSGsGRELLSD 235
Cdd:cd03217 140 LRLVAEVINKL-REEGKSVLIIThyQRLLDYIK-PDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-232 |
1.90e-34 |
|
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: 123.25 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 15 VEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmPPHEIAKlRIAQSPE 94
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRR-RIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 95 GRRIFPRMTVLENLQMGASLDN------QQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGvpgaerRERIDELLDFV-----GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGREL 232
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-237 |
3.12e-34 |
|
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: 122.69 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKL 87
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 RiaqspegRRI---------FPRMTVLENLQMGASLDN--QQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIA 156
Cdd:cd03258 81 R-------RRIgmifqhfnlLSSRTVFENVALPLEIAGvpKAEIEERVLELLELV-GLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 157 RALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
.
gi 492862668 237 E 237
Cdd:cd03258 233 Q 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-232 |
4.03e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.07 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLriaqs 92
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLqmgasldnqQYF-----------DEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMA 161
Cdd:COG4152 77 PEERGLYPKMKVGEQL---------VYLarlkglskaeaKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTV-F------LVEqnafgalKLADRGYVMVNGSITMSGSGREL 232
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTViFsshqmeLVE-------ELCDRIVIINKGRKVLSGSVDEI 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-218 |
4.73e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.89 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYY----GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmPP 81
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 82 HEIAKlrIAQSPegrRIFPRMTVLENLQMGASLD--NQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARAL 159
Cdd:COG1116 80 PDRGV--VFQEP---ALLPWLTVLDNVALGLELRgvPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 160 MARPKLLLLDEPslglaplivkqiFEA------------IKELNRTQGLTVFLV-----EqnafgALKLADRGYVM 218
Cdd:COG1116 154 ANDPEVLLMDEP------------FGAldaltrerlqdeLLRLWQETGKTVLFVthdvdE-----AVFLADRVVVL 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-243 |
4.75e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.17 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNicALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiaklriaqs 92
Cdd:COG3840 2 LRLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegRRI---------FPRMTVLENLQMGASlDNQQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARAL-M 160
Cdd:COG3840 71 ---RPVsmlfqennlFPHLTVAQNIGLGLR-PGLKLTAEQRAQVEQALERvgLAGLLDRLPGQLSGGQRQRVALARCLvR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 161 ARPkLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLS--DPEV 238
Cdd:COG3840 147 KRP-ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDgePPPA 225
|
....*
gi 492862668 239 RAAYL 243
Cdd:COG3840 226 LAAYL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-201 |
5.95e-34 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 122.16 E-value: 5.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYY----GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIA 85
Cdd:COG4181 6 APIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 86 KLRiaqspeGRRI------F---PRMTVLENLQMGASLDNQQyfdedvklmfDLFPR---------LKERINQRGGTLSG 147
Cdd:COG4181 86 RLR------ARHVgfvfqsFqllPTLTALENVMLPLELAGRR----------DARARarallervgLGHRLDHYPAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492862668 148 GEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLV 201
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLV 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-236 |
6.40e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.80 E-value: 6.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiaklR-IA- 90
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----RnIAm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 --QSPEgrrIFPRMTVLENLQMG---ASLDNQQYfDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKL 165
Cdd:COG3839 80 vfQSYA---LYPHMTVYENIAFPlklRKVPKAEI-DRRVREAAELL-GLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 166 LLLDEPslgLAPLIVK---QIFEAIKELNRTQGLTVFLV-----EqnafgALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:COG3839 155 FLLDEP---LSNLDAKlrvEMRAEIKRLHRRLGTTTIYVthdqvE-----AMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-236 |
7.86e-34 |
|
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: 122.06 E-value: 7.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 15 VEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiaklriaqspe 94
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 95 gRRI---------FPRMTVLENLQMG------ASLDNQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARAL 159
Cdd:cd03296 74 -RNVgfvfqhyalFRHMTVFDNVAFGlrvkprSERPPEAEIRAKVHELLKLV-QLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 160 MARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-218 |
8.16e-34 |
|
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: 121.42 E-value: 8.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmPPHEIAklR 88
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRG--Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 IAQSPegrRIFPRMTVLENLQMGASLDNQQYFD--EDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLL 166
Cdd:cd03293 78 VFQQD---ALLPWLTVLDNVALGLELQGVPKAEarERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492862668 167 LLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVM 218
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-223 |
3.97e-33 |
|
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: 119.28 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiaklR-IAQ 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----RdIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRIFPRMTVLENLQMGASLDN--QQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKvpKDEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-221 |
5.52e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.75 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGK--DITSmpPHEIAKL 87
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS--PRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 RIA---QSPegrRIFPRMTVLENLQMGAsldnqqyfdEDVKLMFDLFPRLKERI-------------NQRGGTLSGGEQQ 151
Cdd:COG3845 81 GIGmvhQHF---MLVPNLTVAENIVLGL---------EPTKGGRLDRKAARARIrelserygldvdpDAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 152 MLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLV-----EqnafgALKLADRGYVMVNG 221
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFIthklrE-----VMAIADRVTVLRRG 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-201 |
1.62e-32 |
|
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: 117.73 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR--IAQSPEGRR 97
Cdd:TIGR02673 10 AYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRrrIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IFPRMTVLEN--LQMGASLDNQQYFDEDVKLMFDLFPrLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:TIGR02673 90 LLPDRTVYENvaLPLEVRGKKEREIQRRVGAALRQVG-LEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNL 168
|
170 180
....*....|....*....|....*.
gi 492862668 176 APLIVKQIFEAIKELNRtQGLTVFLV 201
Cdd:TIGR02673 169 DPDLSERILDLLKRLNK-RGTTVIVA 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-227 |
3.90e-32 |
|
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: 116.55 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmpPHEIAKlRIAQS 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALR-RIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGASLdnQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARL--LGIRKKRIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 173 LGLAPLIVKQIFEAIKELnRTQGLTVFL-------VEQnafgalkLADRGYVMVNGSITMSG 227
Cdd:cd03268 155 NGLDPDGIKELRELILSL-RDQGITVLIsshllseIQK-------VADRIGIINKGKLIEEG 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-245 |
1.24e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.67 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 3 AETMQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG----SPRAR-TGRILFNGKDI- 76
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndlIPGARvEGEILLDGEDIy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 77 -TSMPPHEiakLRiaqspegRRI---------FPrMTVLENLQMGASL---DNQQYFDEDV-----KLMfdLFPRLKERI 138
Cdd:COG1117 82 dPDVDVVE---LR-------RRVgmvfqkpnpFP-KSIYDNVAYGLRLhgiKSKSELDEIVeeslrKAA--LWDEVKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 139 NQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQgLTVFLVEQNAFGALKLADRGYVM 218
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKD-YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|....*....
gi 492862668 219 VNGSITMSGSGRELLSDPEVR--AAYLEG 245
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKrtEDYITG 255
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-227 |
1.28e-31 |
|
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: 115.46 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLriaqs 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPRMTVLENLQMGASLD--NQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKglKKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-233 |
1.62e-31 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 115.93 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSP--RARTGRILFNGKDITSMPPHEIAKLRIA---QSPEgrRIfPRM 102
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAGIFlafQYPV--EI-PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLENLQ--MGASLDNQQYFDEDVKLMFDLFPRLK------ER-INqrgGTLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:COG0396 93 SVSNFLRtaLNARRGEELSAREFLKLLKEKMKELGldedflDRyVN---EGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 174 GL---ApliVKQIFEAIKELnRTQGLTVFLV-EQNAFGALKLADRGYVMVNGSITMSGsGRELL 233
Cdd:COG0396 170 GLdidA---LRIVAEGVNKL-RSPDRGILIItHYQRILDYIKPDFVHVLVDGRIVKSG-GKELA 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-237 |
2.24e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 117.87 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 23 GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRiaqspegRRI---- 98
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-------RKIgmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 -----FPRMTVLEN----LQMgASLDNQQyFDEDVKLMFDLFPrLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:COG1135 89 qhfnlLSSRTVAENvalpLEI-AGVPKAE-IRKRVAELLELVG-LSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELNRTQGLTVFL-------VEQnafgalkLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:COG1135 166 EATSALDPETTRSILDLLKDINRELGLTIVLithemdvVRR-------ICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-237 |
3.37e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.64 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 9 KQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTI-----FGSPRARTGRILFNGKDITSmPPHE 83
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYS-PRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 84 IAKLR-----IAQSPEGrriFPrMTVLENLQMG---ASLDNQQYFDEDVKLMF---DLFPRLKERINQRGGTLSGGEQQM 152
Cdd:PRK14239 81 TVDLRkeigmVFQQPNP---FP-MSIYENVVYGlrlKGIKDKQVLDEAVEKSLkgaSIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 153 LAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNrtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGREL 232
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
....*
gi 492862668 233 LSDPE 237
Cdd:PRK14239 235 FMNPK 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-236 |
3.59e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 17 KVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmpPHeiAKLRIAQSPEGR 96
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND--PK--VDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 97 -----RIFPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:PRK09493 82 vfqqfYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-227 |
4.24e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.11 E-value: 4.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMT--IFGSPRARTGRILFNGKDITSMP-PHEIAKLR- 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnLLEMPRSGTLNIAGNHFDFSKTPsDKAIRELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 -IAQSPEGRRIFPRMTVLENLQMG----ASLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARP 163
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQALARAEKLLERL--RLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELNRTqGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-224 |
7.75e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 7.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGnicaLKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIA 90
Cdd:COG1129 255 VVLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRR---IFPRMTVLENLQMgASLD--------NQQYFDEDVKLMFDLFpRLK-ERINQRGGTLSGGEQQMLAIARA 158
Cdd:COG1129 331 YVPEDRKgegLVLDLSIRENITL-ASLDrlsrggllDRRRERALAEEYIKRL-RIKtPSPEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 159 LMARPKLLLLDEPSLGlapliV-----KQIFEAIKELNRtQGLTVFLV-----EqnafgALKLADRGYVMVNGSIT 224
Cdd:COG1129 409 LATDPKVLILDEPTRG-----IdvgakAEIYRLIRELAA-EGKAVIVIsselpE-----LLGLSDRILVMREGRIV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-241 |
1.15e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 118.61 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIA 90
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGasLDNQQyfdEDVKLMFDLFPRLKERIN--QRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFG--LPKRQ---ASMQKMKQLLAALGCQLDldSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRElLSDPEVRAA 241
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD-LSTDDIIQA 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-233 |
1.40e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.73 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIfgsPR---ARTGRILFNGKDITSMPPHEIAKlRIA---QSP 93
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL---LRfydPTSGRILIDGVDIRDLTLESLRR-QIGvvpQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 94 EgrrIFpRMTVLENLQMG---ASLD------NQQYFDEDVKlmfdlfpRLKE----RINQRGGTLSGGEQQMLAIARALM 160
Cdd:COG1132 424 F---LF-SGTIRENIRYGrpdATDEeveeaaKAAQAHEFIE-------ALPDgydtVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNaFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHR-LSTIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-242 |
1.98e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.71 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR-- 88
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 IAQSPegRRIFPrMTVLENLQMGASlDNQQYFDEDVKLMF------DLFPrLKERINQrggTLSGGEQQMLAIARALM-- 160
Cdd:PRK13548 81 LPQHS--SLSFP-FTVEEVVAMGRA-PHGLSRAEDDALVAaalaqvDLAH-LAGRDYP---QLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 161 ----ARPKLLLLDEP--SLGLAPLIvkQIFEAIKELNRTQGLTVFLVEQNafgaLKLA----DRGYVMVNGSITMSGSGR 230
Cdd:PRK13548 153 wepdGPPRWLLLDEPtsALDLAHQH--HVLRLARQLAHERGLAVIVVLHD----LNLAaryaDRIVLLHQGRLVADGTPA 226
|
250
....*....|..
gi 492862668 231 ELLSDPEVRAAY 242
Cdd:PRK13548 227 EVLTPETLRRVY 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-227 |
1.19e-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: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 32 DMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQSpegRRIFPRMTVLENLQMG 111
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE---NNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 112 ASlDNQQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKE 189
Cdd:cd03298 95 LS-PGLKLTAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 492862668 190 LNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-177 |
8.43e-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: 108.05 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGeIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPpheiAKLR--IA 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP----QKLRrrIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGASL------DNQQYFDEDVKLMfDLFPRLKERInqrgGTLSGGEQQMLAIARALMARPK 164
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLkgipskEVKARVDEVLELV-NLGDRAKKKI----GSLSGGMRRRVGIAQALVGDPS 150
|
170
....*....|...
gi 492862668 165 LLLLDEPSLGLAP 177
Cdd:cd03264 151 ILIVDEPTAGLDP 163
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-242 |
8.51e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 8.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRiAQ 91
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR-AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRI-FPrMTVLENLQMGAsLDNQQYFDEDVKL------MFDLfPRLKERINQrggTLSGGEQQMLAIARAL----- 159
Cdd:COG4559 80 LPQHSSLaFP-FTVEEVVALGR-APHGSSAAQDRQIvrealaLVGL-AHLAGRSYQ---TLSGGEQQRVQLARVLaqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 160 --MARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLV--EQNAfgALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVlhDLNL--AAQYADRILLLHQGRLVAQGTPEEVLTD 230
|
....*..
gi 492862668 236 PEVRAAY 242
Cdd:COG4559 231 ELLERVY 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-239 |
8.90e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.85 E-value: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 2 QAETMQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPP 81
Cdd:PRK11607 9 QAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 82 HEIAKLRIAQSpegRRIFPRMTVLENLQMGASLDN--QQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARAL 159
Cdd:PRK11607 89 YQRPINMMFQS---YALFPHMTVEQNIAFGLKQDKlpKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 160 MARPKLLLLDEPSLGL-APLIVKQIFEAIKELNRTqGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK11607 165 AKRPKLLLLDEPMGALdKKLRDRMQLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
.
gi 492862668 239 R 239
Cdd:PRK11607 244 R 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-241 |
9.27e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 111.35 E-value: 9.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 31 IDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKD------ITSMPPHeiaKLRIA---QSPegrRIFPR 101
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPH---RRRIGyvfQEA---RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGAS----LDNQQYFDEDVKLMfDLFPRLKERInqrgGTLSGGEQQMLAIARALMARPKLLLLDEPslgLAP 177
Cdd:COG4148 92 LSVRGNLLYGRKraprAERRISFDEVVELL-GIGHLLDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEP---LAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 178 LIVK---QIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAA 241
Cdd:COG4148 164 LDLArkaEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-233 |
2.11e-28 |
|
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: 107.70 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 21 YYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSPEGRRIFP 100
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-MIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RmTVLENLQMGaSLDNQqyfDEDVKLM-----FDLFPR-----LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03254 91 G-TIMENIRLG-RPNAT---DEEVIEAakeagAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNrtQGLTVFLVEQNaFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLM--KGRTSIIIAHR-LSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
28-232 |
2.83e-28 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 107.73 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRAR--TGRILFNGKDITSMPPHEIAKLRI---AQSPEGrriFPRM 102
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLELEPDERARAGLflaFQYPEE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLENLQMGASLDNQQYFDEDVKlMFDLFPRLKERIN---------QRG---GtLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:TIGR01978 93 SNLEFLRSALNARRSARGEEPLD-LLDFEKLLKEKLAlldmdeeflNRSvneG-FSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 171 PSLGLAPLIVKQIFEAIKELnRTQGLTVFLVE--QNAFGALKlADRGYVMVNGSITMSGsGREL 232
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRL-REPDRSFLIIThyQRLLNYIK-PDYVHVLLDGRIVKSG-DVEL 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-201 |
3.06e-28 |
|
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: 107.48 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG-SPRARTGRI-LFnGKDITSMPPHEIaKL 87
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVrLF-GERRGGEDVWEL-RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 RIAQ-SPE-GRRIFPRMTVLENLQMG--ASLD-NQQYFDEDVKLMFDL--FPRLKERINQRGGTLSGGEQQMLAIARALM 160
Cdd:COG1119 79 RIGLvSPAlQLRFPRDETVLDVVLSGffDSIGlYREPTDEQRERARELleLLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLV 201
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLV 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-224 |
4.18e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 106.19 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 14 SVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItsmppHEIAKLR---- 88
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKsigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 IAQSPEgrRIFPRMTVLENLQMG---ASLDNQQYfdEDVKLMFDLFpRLKERINQrggTLSGGEQQMLAIARALMARPKL 165
Cdd:cd03226 76 VMQDVD--YQLFTDSVREELLLGlkeLDAGNEQA--ETVLKDLDLY-ALKERHPL---SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSIT 224
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
27-244 |
4.52e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.86 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItSMPPHEIAKLR-----IAQSPEGRRIFPr 101
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRktvgiVFQNPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 mTVLENLQMGASldNQQYFDEDVKlmfdlfPRLKERINQRGGT---------LSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:PRK13639 95 -TVEEDVAFGPL--NLGLSKEEVE------KRVKEALKAVGMEgfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 173 LGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE-VRAAYLE 244
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEtIRKANLR 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-245 |
5.15e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLM------MTIFGSPRARtGRILFNGKDITSMPPHEIAKlRIAQSPEG 95
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlIELYPEARVS-GEVYLDGQDIFKMDVIELRR-RVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 96 RRIFPRMTVLENLQMGASLD----NQQYFDEDVKLMFD---LFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNrlvkSKKELQERVRWALEkaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELNRTqgLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP--EVRAAYLEG 245
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhELTEKYVTG 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-237 |
8.70e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.46 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMT----IFGSPRART-GRILFNGKDITS--MPPHEIA 85
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARVeGEVRLFGRNIYSpdVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 86 KlRIAQSPEGRRIFPRMTVLENLQMGASLDN----QQYFDEDVKLMFD---LFPRLKERINQRGGTLSGGEQQMLAIARA 158
Cdd:PRK14267 85 R-EVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvksKKELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTqgLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-198 |
9.41e-28 |
|
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: 105.57 E-value: 9.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 18 VETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR--IAQSPEG 95
Cdd:cd03292 7 TKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRrkIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 96 RRIFPRMTVLEN--LQMGASLDNQQYFDEDVKLMFDLFPrLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:cd03292 87 FRLLPDRNVYENvaFALEVTGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*
gi 492862668 174 GLAPLIVKQIFEAIKELNRtQGLTV 198
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINK-AGTTV 189
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-227 |
2.64e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.09 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTL--MMTIFGSPRARTGRILFNGKDITSMPPH-EIAKLR- 88
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLlrVLNLLETPDSGQLNIAGHQFDFSQKPSEkAIRLLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 -IAQSPEGRRIFPRMTVLENLQMG----ASLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARP 163
Cdd:COG4161 83 kVGMVFQQYNLWPHLTVMENLIEApckvLGLSKEQAREKAMKLLARL--RLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELNRTqGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-236 |
4.42e-27 |
|
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: 105.03 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRiaqspeGRRI-------- 98
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELR------RKKIsmvfqsfa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 -FPRMTVLENLQMGASLDN------QQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:cd03294 113 lLPHRTVLENVAFGLEVQGvpraerEERAAEALELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 172 SLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-245 |
4.85e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.89 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 32 DMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPheiaklriAQSP-----EGRRIFPRMTVLE 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP--------SRRPvsmlfQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGAS----LDNQQY--FDEDVKLMF--DLFPRLKerinqrgGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL 178
Cdd:PRK10771 91 NIGLGLNpglkLNAAQRekLHAIARQMGieDLLARLP-------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 179 IVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDpEVRAAYLEG 245
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSG-KASASALLG 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-239 |
6.55e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 15 VEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiaklriaqspe 94
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 95 gRRI---------FPRMTVLENLQMGASL------DNQQYFDEDVKLMFDL--FPRLKERINQRggtLSGGEQQMLAIAR 157
Cdd:PRK10851 74 -RKVgfvfqhyalFRHMTVFDNIAFGLTVlprrerPNAAAIKAKVTQLLEMvqLAHLADRYPAQ---LSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 158 ALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
..
gi 492862668 238 VR 239
Cdd:PRK10851 230 TR 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
27-173 |
7.20e-27 |
|
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: 103.28 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGK----DITSMPPHEIAKLRiaqspegR------ 96
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREILALR-------Rrtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 97 ----RIFPRMTVLEN-----LQMGASLDNQQyfdEDVKLMFDLFpRLKERINQRG-GTLSGGEQQMLAIARALMARPKLL 166
Cdd:COG4778 99 sqflRVIPRVSALDVvaeplLERGVDREEAR---ARARELLARL-NLPERLWDLPpATFSGGEQQRVNIARGFIADPPLL 174
|
....*....
gi 492862668 167 LLDEP--SL 173
Cdd:COG4778 175 LLDEPtaSL 183
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-236 |
8.86e-27 |
|
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: 105.96 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 31 IDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITS------MPPHeiaKLRIAQSPEGRRIFPRMTV 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE---KRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMG---ASLDNQQYFDEDVKLMFDLFPRLkerinQRG-GTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIV 180
Cdd:TIGR02142 93 RGNLRYGmkrARPSERRISFERVIELLGIGHLL-----GRLpGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 181 KQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-237 |
1.12e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.36 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmpphEIAKLR--------IAQSPEgRRI 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD----KKVKLSdirkkvglVFQYPE-YQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 FPRmTVLENLQMGASldNQQYFDEDVKlmfdlfPRLKERINQRGGT-----------LSGGEQQMLAIARALMARPKLLL 167
Cdd:PRK13637 97 FEE-TIEKDIAFGPI--NLGLSEEEIE------NRVKRAMNIVGLDyedykdkspfeLSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 168 LDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-213 |
1.34e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.71 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 3 AETMQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTL------MMTIFGSPRARtGRILFNGKDI 76
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrLNDLIPGFRVE-GKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 77 --TSMPPHEIAKlRIAQSPEGRRIFPRmTVLENLQMGASLDNQQY-FDEDVKLMFD---LFPRLKERINQRGGTLSGGEQ 150
Cdd:PRK14243 80 yaPDVDPVEVRR-RIGMVFQKPNPFPK-SIYDNIAYGARINGYKGdMDELVERSLRqaaLWDEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 151 QMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTqgLTVFLVEQNAFGALKLAD 213
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
1.45e-26 |
|
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: 107.45 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 2 QAETMQKKQPLLSVEKVETYY-GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMP 80
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 81 PHEIAKlRIAQSPEGRRIFPrMTVLENLQMG---ASLDNQQYFDEDVKLMfDLFPRLKE----RINQRGGTLSGGEQQML 153
Cdd:TIGR02868 404 QDEVRR-RVSVCAQDAHLFD-TTVRENLRLArpdATDEELWAALERVGLA-DWLRALPDgldtVLGEGGARLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492862668 154 AIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIkeLNRTQGLTVFLV 201
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLI 526
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-242 |
1.90e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.69 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA 90
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR-RVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGASlDNQQYFDEdvklMFDLFPRLKERINQRGG----------TLSGGEQQMLAIARALM 160
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRT-PHRSRFDT----WTETDRAAVERAMERTGvaqfadrpvtSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 161 ARPKLLLLDEPSLGLAplIVKQIfeaikelnRTQGLTVFLVEQN-----AFGALKLADRgY-----VMVNGSITMSGSGR 230
Cdd:PRK09536 156 QATPVLLLDEPTASLD--INHQV--------RTLELVRRLVDDGktavaAIHDLDLAAR-YcdelvLLADGRVRAAGPPA 224
|
250
....*....|..
gi 492862668 231 ELLSDPEVRAAY 242
Cdd:PRK09536 225 DVLTADTLRAAF 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-227 |
1.90e-26 |
|
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: 101.99 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVD---EGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNG-------KDItSMPPHeiaKLRIAQSPEGRR 97
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI-NLPPQ---QRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IFPRMTVLENLQMG----ASLDNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:cd03297 86 LFPHLNVRENLAFGlkrkRNREDRISVDELLDLL-----GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492862668 174 GLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-238 |
3.26e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.96 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKL--RIAQSPEGRR 97
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFvgLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IFPrmTVLENLQMGA---SLDNQ---QYFDEDVKLMFdlFPRLKERINQRggtLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13652 92 FSP--TVEQDIAFGPinlGLDEEtvaHRVSSALHMLG--LEELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 172 SLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-221 |
3.99e-26 |
|
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: 101.77 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLriaqspEGRRIFPRMTVLEN 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF------QNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASL--------DNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLI 179
Cdd:TIGR01184 75 IALAVDRvlpdlsksERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492862668 180 VKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNG 221
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-236 |
5.04e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 103.73 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKV-ETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiakLRIA 90
Cdd:PRK11153 4 LKNISKVfPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE---LRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 qspegRR----IF------PRMTVLENLQMGASLDNQQyfdedvklmfdlfprlKERINQR--------GGT-------- 144
Cdd:PRK11153 81 -----RRqigmIFqhfnllSSRTVFDNVALPLELAGTP----------------KAEIKARvtellelvGLSdkadrypa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 145 -LSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFL-------VEQnafgalkLADRGY 216
Cdd:PRK11153 140 qLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLithemdvVKR-------ICDRVA 212
|
250 260
....*....|....*....|
gi 492862668 217 VMVNGSITMSGSGRELLSDP 236
Cdd:PRK11153 213 VIDAGRLVEQGTVSEVFSHP 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-237 |
6.70e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.37 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIF-----GSPRARTGRILFNGKDITSMPPHEIAKLR--IAQSPEGRRIFP 100
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpEAGTIRVGDITIDTARSLSQQKGLIRQLRqhVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RMTVLENLQMGASLDNQQYFDEDVKLMFDLFPRL----KERINQRggTLSGGEQQMLAIARALMARPKLLLLDEPSLGLA 176
Cdd:PRK11264 99 HRTVLENIIEGPVIVKGEPKEEATARARELLAKVglagKETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 177 PLIVKQIFEAIKELNRTQGLTVFLVEQNAFgALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSF-ARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-227 |
9.05e-26 |
|
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: 100.36 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSPEGRRIFpRMTVLE 106
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASLDNQQYFDEDVKL-----MFDLFPR-LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIV 180
Cdd:cd03245 97 NITLGAPLADDERILRAAELagvtdFVNKHPNgLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492862668 181 KQIFEAIKELNRTQglTVFLVEQNAfGALKLADRGYVMVNGSITMSG 227
Cdd:cd03245 177 ERLKERLRQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-238 |
1.18e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItSMPPHEIAKLR-----IAQSPEgRRIFpR 101
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLResvgmVFQDPD-NQLF-S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGASldnqqyfdeDVKLMFDLFPRLKERINQRGGT----------LSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13636 98 ASVYQDVSFGAV---------NLKLPEDEVRKRVDNALKRTGIehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 172 SLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-236 |
1.45e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.09 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 5 TMQKKQPLLSVEKVETYYG-------------NICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILF 71
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 72 NGKDITSMPPHEIAKLR-----IAQSPEGRrIFPRMTV----LENLQMGASLDNQQYFDEDVKLMFD---LFPRLkerIN 139
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRsdiqmIFQDPLAS-LNPRMTIgeiiAEPLRTYHPKLSRQEVKDRVKAMMLkvgLLPNL---IN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 140 QRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMV 219
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 236
|
250
....*....|....*..
gi 492862668 220 NGSITMSGSGRELLSDP 236
Cdd:PRK15079 237 LGHAVELGTYDEVYHNP 253
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-236 |
1.84e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.11 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 1 MQAETMQKKQPLLSVEKV----ETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSpRARTGRI----LFN 72
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLrvtfSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 73 GKDITSMPPHEIAKLR------IAQSPEgRRIFPRMTV----LENLQMGASLDNQQYFDEDVKlMFDL--FPRLKERINQ 140
Cdd:PRK09473 80 GREILNLPEKELNKLRaeqismIFQDPM-TSLNPYMRVgeqlMEVLMLHKGMSKAEAFEESVR-MLDAvkMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 141 RGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVN 220
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 237
|
250
....*....|....*.
gi 492862668 221 GSITMSGSGRELLSDP 236
Cdd:PRK09473 238 GRTMEYGNARDVFYQP 253
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-201 |
3.62e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 98.71 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG--SPRART-GRILFNGKDITSMPPHEiaklri 89
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlSPAFSAsGEVLLNGRRLTALPAEQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 aqspegRRI---------FPRMTVLENLQMG--ASLDNQQYFD------EDVKL--MFDLFPrlkerinqrgGTLSGGEQ 150
Cdd:COG4136 76 ------RRIgilfqddllFPHLSVGENLAFAlpPTIGRAQRRArveqalEEAGLagFADRDP----------ATLSGGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 151 QMLAIARALMARPKLLLLDEPSLGL-APL---IVKQIFEAIkelnRTQGLTVFLV 201
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLdAALraqFREFVFEQI----RQRGIPALLV 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-235 |
4.11e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.70 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG------SPRARTgRILFNGKDITSMPPHE 83
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdkSAGSHI-ELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 84 IAKLRiAQSP---EGRRIFPRMTVLENLQMGAsLDNQQYFdedvKLMFDLFPRLKER--------------INQRGGTLS 146
Cdd:PRK09984 81 IRKSR-ANTGyifQQFNLVNRLSVLENVLIGA-LGSTPFW----RTCFSWFTREQKQralqaltrvgmvhfAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 147 GGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMS 226
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*....
gi 492862668 227 GSGRELLSD 235
Cdd:PRK09984 235 GSSQQFDNE 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-224 |
7.32e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETY-YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:COG3845 256 VVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRR---IFPRMTVLENLQMGasldnqQYFDE--------DVKLMFDLFPRLKER-------INQRGGTLSGGEQQ 151
Cdd:COG3845 336 AYIPEDRLgrgLVPDMSVAENLILG------RYRRPpfsrggflDRKAIRAFAEELIEEfdvrtpgPDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 152 MLAIARALMARPKLLLLDEPSLGL---ApliVKQIFEAIKELnRTQGLTVFLV-----EqnafgALKLADRGYVMVNGSI 223
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLdvgA---IEFIHQRLLEL-RDAGAAVLLIsedldE-----ILALSDRIAVMYEGRI 480
|
.
gi 492862668 224 T 224
Cdd:COG3845 481 V 481
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-244 |
9.99e-25 |
|
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: 98.00 E-value: 9.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTI--FGSPRArtGRILFNGKDITSMPPHEiakLR-----IAQSPEgrrIFP 100
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerFYDPTS--GEILLDGVDIRDLNLRW---LRsqiglVSQEPV---LFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 rMTVLENLQMGASLDNQQYFDEDVKLMF------DLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLG 174
Cdd:cd03249 91 -GTIAENIRYGKPDATDEEVEEAAKKANihdfimSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 175 LAPLIVKQIFEAIKELNRtqGLTVfLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYLE 244
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTT-IVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-237 |
1.21e-24 |
|
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: 101.68 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG----SPRARTGRILFNGKDITSMPP 81
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 82 HEIAKLRiaqspeGRRI---F--PrMTVLENL-----QMGASLDNQQYFD------------EDVKLmfdlfPRLKERIN 139
Cdd:COG4172 84 RELRRIR------GNRIamiFqeP-MTSLNPLhtigkQIAEVLRLHRGLSgaaararalellERVGI-----PDPERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 140 QRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFL-------VEqnafgalKLA 212
Cdd:COG4172 152 AYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLithdlgvVR-------RFA 224
|
250 260
....*....|....*....|....*
gi 492862668 213 DRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-239 |
4.04e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.24 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIA 90
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQ---------MGASLDNQQYFDEDVKLMFDLFPrLKERINQRGGTLSGGEQQMLAIARALMA 161
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYigrhltkkvCGVNIIDWREMRVRAAMMLLRVG-LKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVR 239
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-201 |
4.19e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.05 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQ 91
Cdd:TIGR02857 322 LEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRIFPRmTVLENLQMG------ASLDN---QQYFDEDVKlmfDLFPRLKERINQRGGTLSGGEQQMLAIARALMAR 162
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLArpdasdAEIREaleRAGLDEFVA---ALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190
....*....|....*....|....*....|....*....
gi 492862668 163 PKLLLLDEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLV 201
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLV 513
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-242 |
6.63e-24 |
|
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: 99.76 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYY-----------GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARtGRILFNGKDITSM 79
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 80 PPHEIAKLRiaqspegRRI---F--------PRMTVLENLQMG-----ASLDNQQYFD------EDVKL---MFDLFPRl 134
Cdd:COG4172 353 SRRALRPLR-------RRMqvvFqdpfgslsPRMTVGQIIAEGlrvhgPGLSAAERRArvaealEEVGLdpaARHRYPH- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 135 kErinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLT-VF------LVEQnafg 207
Cdd:COG4172 425 -E--------FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAyLFishdlaVVRA---- 491
|
250 260 270
....*....|....*....|....*....|....*
gi 492862668 208 alkLADRGYVMVNGSITMSGSGRELLSDPevRAAY 242
Cdd:COG4172 492 ---LAHRVMVMKDGKVVEQGPTEQVFDAP--QHPY 521
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-214 |
9.82e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 95.27 E-value: 9.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYY--GNICA--LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIA 85
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 86 KLR------IAQSpegRRIFPRMTVLENLQMGASLDNQQYfDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIAR 157
Cdd:PRK11629 83 ELRnqklgfIYQF---HHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 158 ALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGlTVFLVEQNafgALKLADR 214
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQG-TAFLVVTH---DLQLAKR 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-234 |
1.06e-23 |
|
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: 99.05 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLrI---AQSPEgrrIFPRmTV 104
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IgylPQDVE---LFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMGASLDnqqyfDEDV----KL--MFDLFPRLKE----RINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLG 174
Cdd:COG4618 423 AENIARFGDAD-----PEKVvaaaKLagVHEMILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 175 LAPLIVKQIFEAIKELnRTQGLTVFLVEQNAfGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:COG4618 498 LDDEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-222 |
4.25e-23 |
|
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: 92.92 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGkditsmppheiaklRIA---QSPegrRIFPrMT 103
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAyvsQEP---WIQN-GT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 VLENLQMGASLDNQQY--------FDEDVKLMFDlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:cd03250 82 IRENILFGKPFDEERYekvikacaLEPDLEILPD---GDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492862668 176 APLIVKQIFE-AIKEL---NRtqglTVFLVEQNaFGALKLADRGYVMVNGS 222
Cdd:cd03250 159 DAHVGRHIFEnCILGLllnNK----TRILVTHQ-LQLLPHADQIVVLDNGR 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-213 |
4.39e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLM-----MTIFGSPRARTGRILFNGKDITSMP 80
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrMNELESEVRVEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 81 PHeIAKLR--IAQSPEGRRIFPrMTVLENLQMGASL---DNQQYFDEDVKLMF---DLFPRLKERINQRGGTLSGGEQQM 152
Cdd:PRK14258 81 VN-LNRLRrqVSMVHPKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDIVESALkdaDLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 153 LAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLAD 213
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-233 |
6.32e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiAKLRIA 90
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGAsldnqQYF-------DEDVKLMFDlFPRLKERINQRGGTLSGGEQQMLAIARALMARP 163
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFG-----RYFglsaaaaRALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
27-227 |
6.76e-23 |
|
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: 91.61 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKditsmPPHEIAKLRIAQspegrrifprMTVLe 106
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-----PVSDLEKALSSL----------ISVL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 nlqmgasldNQQYFDEDVKLMfdlfprlkeriNQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEA 186
Cdd:cd03247 81 ---------NQRPYLFDTTLR-----------NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492862668 187 IKELnrTQGLTVFLVEQNAFGaLKLADRGYVMVNGSITMSG 227
Cdd:cd03247 141 IFEV--LKDKTLIWITHHLTG-IEHMDKILFLENGKIIMQG 178
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-201 |
1.21e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.53 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRiAQSP----EGRRIFPRMT 103
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR-AKHVgfvfQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 VLENLQMGASL---DNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIV 180
Cdd:PRK10584 105 ALENVELPALLrgeSSRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180
....*....|....*....|.
gi 492862668 181 KQIFEAIKELNRTQGLTVFLV 201
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILV 203
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-214 |
1.78e-22 |
|
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: 91.14 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKD---ITSMPPHEIAKLRIAQSPEGRRI 98
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKFRREKLGYLFQNFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 FPRMTVLENLQMGASLDNQQYFDEDVKLMFDL-FPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:TIGR03608 88 IENETVEENLDLGLKYKKLSKKEKREKKKEALeKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDP 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 492862668 178 LIVKQIFEAIKELNRtQGLTVFLVEQNAFGAlKLADR 214
Cdd:TIGR03608 168 KNRDEVLDLLLELND-EGKTIIIVTHDPEVA-KQADR 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-245 |
2.39e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEI- 84
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 85 -AKLRIAQSPEGRRIFPRMTVLENLQMgaSLDNQQYFDEDV---KLMFDLfprlkERINQRGGT------LSGGEQQMLA 154
Cdd:PRK11831 81 tVRKRMSMLFQSGALFTDMNVFDNVAY--PLREHTQLPAPLlhsTVMMKL-----EAVGLRGAAklmpseLSGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 155 IARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELL- 233
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQa 233
|
250
....*....|...
gi 492862668 234 -SDPEVRaAYLEG 245
Cdd:PRK11831 234 nPDPRVR-QFLDG 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-235 |
2.92e-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: 91.52 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIfgsPR---ARTGRILFNGKDITSMpphEIAKLR--IAQSPEGRRIFPR 101
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRfydVDSGRILIDGHDVRDY---TLASLRrqIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 mTVLENLQMG------------ASLDNQQYFDEDVKLMFDlfprlkERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:cd03251 91 -TVAENIAYGrpgatreeveeaARAANAHEFIMELPEGYD------TVIGERGVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNaFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:cd03251 164 EATSALDTESERLVQAALERL--MKNRTTFVIAHR-LSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-233 |
3.96e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 25 ICALKGIDMTVDEGEIVALIGANGAGKSTL--MMT--IFGSprarTGRILFNGKDitsmpPHeiaKLRIAQSpegRRI-- 98
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTikMLTgiLVPT----SGEVRVLGYV-----PF---KRRKEFA---RRIgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 --------FPRMTVLENLQMGA---SLDNQQYfDEDVKLMFDLFpRLKERINQRGGTLSGGeQQMLA-IARALMARPKLL 166
Cdd:COG4586 100 vfgqrsqlWWDLPAIDSFRLLKaiyRIPDAEY-KKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 167 LLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFL-------VEQnafgalkLADRGYVMVNGSITMSGSGRELL 233
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEELK 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-242 |
4.78e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.06 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARtGRILFNGKDITSMPPHEIAKLRiA-----QSPEgrrifPRM 102
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHR-AylsqqQSPP-----FAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLENLQMGASLDNQQYFDEDVKLM----FDLFPRLKERINQrggtLSGGEQQMLAIARALM-------ARPKLLLLDEP 171
Cdd:COG4138 85 PVFQYLALHQPAGASSEAVEQLLAQlaeaLGLEDKLSRPLTQ----LSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 172 slgLAPLIVKQifEA-----IKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAY 242
Cdd:COG4138 161 ---MNSLDVAQ--QAaldrlLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-243 |
4.89e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 29 KGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRR---IFPRMTVL 105
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGASL---------------DNQQYFDEDVKLMfdlfpRLK-ERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:PRK09700 360 QNMAISRSLkdggykgamglfhevDEQRTAENQRELL-----ALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 170 EPSLGLAPLIVKQIFEAIKELNrTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWAL 507
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-224 |
6.06e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.91 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRR---IFPRMTV 104
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENL---------QMGASLDNQ--QYFDEDVKLMFDL-FPRLKERInqrgGTLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:PRK10762 348 KENMsltalryfsRAGGSLKHAdeQQAVSDFIRLFNIkTPSMEQAI----GLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492862668 173 LGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSIT 224
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-236 |
7.18e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.10 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYY-----------GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGK 74
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 75 DITSMPPHEIAKLRiaqspegRR---IF--------PRMTVLENLqmGASLDNQQYFDED-----VKLMFDLFPRLKERI 138
Cdd:COG4608 81 DITGLSGRELRPLR-------RRmqmVFqdpyaslnPRMTVGDII--AEPLRIHGLASKAerrerVAELLELVGLRPEHA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 139 NQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLT-VF------LVEQnafgalkL 211
Cdd:COG4608 152 DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTyLFishdlsVVRH-------I 224
|
250 260
....*....|....*....|....*
gi 492862668 212 ADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:COG4608 225 SDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-237 |
9.20e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 9.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 4 ETMQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLM------MTIFGSPRARTGRILFNGKDIT 77
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 78 SMpphEIAKLR-----IAQSPEGrriFPRMTVLENLQMGASLDNQQYFDEDVKLMFD------LFPRLKERINQRGGTLS 146
Cdd:PRK14246 82 QI---DAIKLRkevgmVFQQPNP---FPHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 147 GGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTqgLTVFLVEQNAFGALKLADRGYVMVNGSITMS 226
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
250
....*....|.
gi 492862668 227 GSGRELLSDPE 237
Cdd:PRK14246 234 GSSNEIFTSPK 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-236 |
9.56e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.76 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsmpPHEIAKLri 89
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ---LRDLYAL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 aQSPEGRRI------FPRMTVLENLQMGAS-----------LDNQQYFD---------EDVKLMFDlfprlkeRINQRGG 143
Cdd:PRK11701 79 -SEAERRRLlrtewgFVHQHPRDGLRMQVSaggnigerlmaVGARHYGDiratagdwlERVEIDAA-------RIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 144 TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|...
gi 492862668 224 TMSGSGRELLSDP 236
Cdd:PRK11701 231 VESGLTDQVLDDP 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
28-223 |
1.08e-21 |
|
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: 90.63 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR-----IAQSPEGRrIFPRM 102
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRrdvqlVFQDSPSA-VNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLENLqmGASLDNQQYFDEDVKL-----MFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKariaeLLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492862668 178 LIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-227 |
1.16e-21 |
|
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: 89.64 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG---SPRARTGRILFNGKDITsmpPHEIAKlRIAQSPEGRRIFPRMTV 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRK---PDQFQK-CVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMGASLDNQQYFDEDVKLMFDLFPRLKE----RI-NQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLI 179
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492862668 180 VKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-239 |
1.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPP-HEIAKLR- 88
Cdd:PRK13644 1 MIRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 -IAQSPEGRriFPRMTVLENLQMGAslDNQQYFDEDVKLMFDLF---PRLKERINQRGGTLSGGEQQMLAIARALMARPK 164
Cdd:PRK13644 81 iVFQNPETQ--FVGRTVEEDLAFGP--ENLCLPPIEIRKRVDRAlaeIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 165 LLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNaFGALKLADRGYVMVNGSITMSGSGRELLSDPEVR 239
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-240 |
1.87e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.47 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 40 IVALIGANGAGKSTLMMTIFGSPRARTGRILFNGK---DI---TSMPPHeiaKLRIAQSPEGRRIFPRMTVLENLQMGAS 113
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekgICLPPE---KRRIGYVFQDARLFPHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 114 LDNQQYFDEDVKLM-----FDLFPrlkerinqrgGTLSGGEQQMLAIARALMARPKLLLLDEPslgLAPLIV---KQIFE 185
Cdd:PRK11144 103 KSMVAQFDKIVALLgieplLDRYP----------GSLSGGEKQRVAIGRALLTAPELLLMDEP---LASLDLprkRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 186 AIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRA 240
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRP 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-197 |
2.08e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTI-----FGSpraRTGRILFNGKDITSMPPHEI 84
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGT---YEGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 85 AKLRIAQSPEGRRIFPRMTVLENLQMGASLDNQQYFDEDvkLMF----DLFPRLKERIN--QRGGTLSGGEQQMLAIARA 158
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYD--AMYlraqKLLAQLKLDINpaTPVGNLGLGQQQLVEIAKA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLT 197
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIA 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-235 |
2.32e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 2 QAETMQKKQPLLSVEKVETYY--GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSM 79
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 80 PPheiAKLRIAQSPEGRR--IFPRmTVLENLQMGA-SLDNQQYFD--EDVKL--MFDLFPRLKERINQRGGTLSGGEQQM 152
Cdd:PRK11160 408 SE---AALRQAISVVSQRvhLFSA-TLRDNLLLAApNASDEALIEvlQQVGLekLLEDDKGLNAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 153 LAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNAFGaLKLADRGYVMVNGSITMSGSGREL 232
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTG-LEQFDRICVMDNGQIIEQGTHQEL 560
|
...
gi 492862668 233 LSD 235
Cdd:PRK11160 561 LAQ 563
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-223 |
2.52e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLsVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNgkditSMPPHEiAKLRIA 90
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAE-AREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRMTVLENLQMGASLDNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492862668 171 PSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-237 |
2.78e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.08 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITS-MPPHEIAKLR-----IAQSPEgRRIFP 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRkkvgiVFQFPE-HQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RmTVLENLQMGASldNQQYFDEDVKL----MFDLFPrLKERINQRGG-TLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK13634 101 E-TVEKDICFGPM--NFGVSEEDAKQkareMIELVG-LPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 176 APLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-235 |
4.23e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 18 VETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPphEIAKLRIAQSPEGRR 97
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARARIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IFPRMTVLENLqmgasLDNQQYFD------EDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13536 125 LDLEFTVRENL-----LVFGRYFGmstreiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 172 SLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-195 |
7.72e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRIFPRMTVLENLQMG-------ASLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMAR 162
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGrefvnrfGRIDWKKMYAEADKLLARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190
....*....|....*....|....*....|...
gi 492862668 163 PKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQG 195
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIREL-KSQG 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-238 |
8.08e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 14 SVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA--- 90
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK-RLAilr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEgrrIFPRMTVLENLQMG--------ASLDNQQYFDEDVKLMfDLFPrLKER-INQrggtLSGGEQQMLAIARALMA 161
Cdd:COG4604 82 QENH---INSRLTVRELVAFGrfpyskgrLTAEDREIIDEAIAYL-DLED-LADRyLDE----LSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 162 RPKLLLLDEPslgLAPLIVK---QIFEAIKELNRTQGLTVFLV--EQNAfgALKLADRGYVMVNGSITMSGSGRELLsDP 236
Cdd:COG4604 153 DTDYVLLDEP---LNNLDMKhsvQMMKLLRRLADELGKTVVIVlhDINF--ASCYADHIVAMKDGRVVAQGTPEEII-TP 226
|
..
gi 492862668 237 EV 238
Cdd:COG4604 227 EV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-200 |
1.11e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 19 ETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR--IAQSPEGR 96
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRrqIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 97 RIFPRMTVLENLQM-----GASLDNqqyFDEDVKLMFD---LFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLLL 168
Cdd:PRK10908 89 HLLMDRTVYDNVAIpliiaGASGDD---IRRRVSAALDkvgLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|..
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELNRTqGLTVFL 200
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRV-GVTVLM 192
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-234 |
1.17e-20 |
|
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: 87.29 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMpphEIAKLR--IAQSPEGRRIFpRMTVL 105
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRraIGVVPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMG---ASlDNQQYFDEDVKLMFDLFPRLKE----RINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL 178
Cdd:cd03253 93 YNIRYGrpdAT-DEEVIEAAKAAQIHDKIMRFPDgydtIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 179 IVKQIFEAIKEL--NRTqglTVFLveqnafgALKL-----ADRGYVMVNGSITMSGSGRELLS 234
Cdd:cd03253 172 TEREIQAALRDVskGRT---TIVI-------AHRLstivnADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-234 |
1.82e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 9 KQPLLSVEKVETYYGNIC--ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAK 86
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 87 lRIA---QSPEGRriFPRMTVLENLQMGasLDNQQYFDEDvklmfdLFPRLKERINQRGGT---------LSGGEQQMLA 154
Cdd:PRK13635 82 -QVGmvfQNPDNQ--FVGATVQDDVAFG--LENIGVPREE------MVERVDQALRQVGMEdflnrephrLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 155 IARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKlADRGYVMVNGSITMSGSGRELLS 234
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-236 |
2.48e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.24 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmppHEIAKLRIAQSPEGRRIFPR 101
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRDICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGASLDN------QQYFDEDVKLMfDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK11432 93 MSLGENVGYGLKMLGvpkeerKQRVKEALELV-DLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 176 APLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-247 |
2.69e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVeTYYGnicaLKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI 89
Cdd:PRK15439 266 APVLTVEDL-TGEG----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRifprmtvlenlQMGASLD------------NQQYFDEDVKLMFDLFPRLKERIN-------QRGGTLSGGEQ 150
Cdd:PRK15439 341 VYLPEDRQ-----------SSGLYLDaplawnvcalthNRRGFWIKPARENAVLERYRRALNikfnhaeQAARTLSGGNQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 151 QMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGR 230
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGA 488
|
250
....*....|....*..
gi 492862668 231 ELLSDPEVRAAYLEGGR 247
Cdd:PRK15439 489 AINVDTIMRLAFGEHQA 505
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-218 |
3.22e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.45 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNIC----ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmppheiak 86
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 87 lriaqsPEGRR--------IFPRMTVLENLQMGASL------DNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQM 152
Cdd:COG4525 74 ------PGADRgvvfqkdaLLPWLNVLDNVAFGLRLrgvpkaERRARAEELLALV-----GLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 153 LAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVM 218
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-171 |
3.29e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNgkditsmppheiAKLRI- 89
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------------ETVKIg 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 --AQSPEGrrIFPRMTVLENLQMGASLDNQQY-------FdedvklmfdLFPRlkERINQRGGTLSGGEQQMLAIARALM 160
Cdd:COG0488 382 yfDQHQEE--LDPDKTVLDELRDGAPGGTEQEvrgylgrF---------LFSG--DDAFKPVGVLSGGEKARLALAKLLL 448
|
170
....*....|.
gi 492862668 161 ARPKLLLLDEP 171
Cdd:COG0488 449 SPPNVLLLDEP 459
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-233 |
3.46e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 89.03 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYG-NICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLrIAQ 91
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRIFPRmTVLENLQMGASLDNQQyfdEDVKLMFDL---------FPR-LKERINQRGGTLSGGEQQMLAIARALMA 161
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGAKENVSQ---DEIWAACEIaeikddienMPLgYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 162 RPKLLLLDEPSLGLAPLIVKQIFEAIkeLNRTQGLTVFLVEQnaFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHR--LSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-189 |
3.72e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 85.62 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiaKLR-----IAQSP---EGrri 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH---DLRsrisiIPQDPvlfSG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 fprmTVLENLqmgaslD-NQQYFDEDV----------KLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLL 167
Cdd:cd03244 93 ----TIRSNL------DpFGEYSDEELwqalervglkEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180
....*....|....*....|..
gi 492862668 168 LDEPSLGLAPLIVKQIFEAIKE 189
Cdd:cd03244 163 LDEATASVDPETDALIQKTIRE 184
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-170 |
3.94e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 85.16 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHeiaKLR-----IAQSPegrrifpr 101
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE---DLRssltiIPQDP-------- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 102 mtvleNLQMGASLDNQQYFDE--DVKLMFDLfprlkeRINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03369 92 -----TLFSGTIRSNLDPFDEysDEEIYGAL------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-239 |
5.17e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPheiAKLRIAQSPEGRRIFPR 101
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGASLD--NQQYFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL-APL 178
Cdd:PRK11000 90 LSVAENMSFGLKLAgaKKEEINQRVNQVAEVL-QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLdAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 179 IVKQIFEaIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVR 239
Cdd:PRK11000 169 RVQMRIE-ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
13-236 |
9.44e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.01 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR---I 89
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrkkI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRIFPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLL 168
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-242 |
1.58e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 34 TVDEGEIVALIGANGAGKSTLMMTIFGSPRArTGRILFNGKDITSMPPHEIAKLR--IAQSpegRRIFPRMTVLENLQM- 110
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRayLSQQ---QTPPFAMPVFQYLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 111 ---GASLDNQQYFDEDVKLMFDLFPRLKERINQrggtLSGGEQQ-------MLAIARALMARPKLLLLDEPSlglAPLIV 180
Cdd:PRK03695 94 qpdKTRTEAVASALNEVAEALGLDDKLGRSVNQ----LSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPM---NSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 181 KQ---IFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAY 242
Cdd:PRK03695 167 AQqaaLDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-227 |
2.16e-19 |
|
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: 83.92 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRI--AQSPEGRRIF 99
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 PRMTVLENLQMGASLDNQQY---FDEDVKLMfDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLA 176
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFkkrLDELSELL-DLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492862668 177 PLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-224 |
2.50e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGID---MTVDEGEIVALIGANGAGKSTLMMTIFGS-PRARTGRILFNGKDITSMPPHEIAKLR 88
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDdvsFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 IAQSPEGRR---IFPRMTVLENLQMgASLDN------------QQYFDEDVKlmfdlfpRLKERIN---QRGGTLSGGEQ 150
Cdd:PRK13549 340 IAMVPEDRKrdgIVPVMGVGKNITL-AALDRftggsriddaaeLKTILESIQ-------RLKVKTAspeLAIARLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 151 QMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSIT 224
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-238 |
3.05e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYYGNI--CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmppHE 83
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---EN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 84 IAKLR-----IAQSPEGRriFPRMTVLENLQMGasLDNQQYFDEDVKLMFDLFPR---LKERINQRGGTLSGGEQQMLAI 155
Cdd:PRK13632 78 LKEIRkkigiIFQNPDNQ--FIGATVEDDIAFG--LENKKVPPKKMKDIIDDLAKkvgMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 156 ARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALkLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
...
gi 492862668 236 PEV 238
Cdd:PRK13632 233 KEI 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-204 |
3.81e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYY----GNICALKGIDMTVDEGEIVALIGANGAGKSTLMmTIFG---SPRARTGRILfnGKDITSMPPHE 83
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGcldKPTSGTYRVA--GQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 84 IAKLR------IAQSpegRRIFPRMTVLENLQMGA---SLDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLA 154
Cdd:PRK10535 80 LAQLRrehfgfIFQR---YHLLSHLTAAQNVEVPAvyaGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492862668 155 IARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQN 204
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-192 |
5.97e-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: 85.26 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG-SPRAR-TGRILFNGKDITSMPPHEIAKLRI 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRIFPRMTVLENLQMGASLD---NQQYFDEDVKLMFDLFPRLK---ERINQRGGTLSGGEQQMLAIARALMARP 163
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITlpgGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180
....*....|....*....|....*....
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELNR 192
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKA 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-234 |
6.40e-19 |
|
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: 85.54 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYG--NICALKGIDMTVDEGEIVALIGANGAGKSTL--MMTIFGSPRArtGRILFNGKDITSMpphEIAKL 87
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYEPDS--GQILLDGHDLADY---TLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 R--IAQSPEGRRIFPRmTVLENLQMGASldnQQYFDEDV---------KLMFDLFPR-LKERINQRGGTLSGGEQQMLAI 155
Cdd:TIGR02203 405 RrqVALVSQDVVLFND-TIANNIAYGRT---EQADRAEIeralaaayaQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 156 ARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKEL--NRTQgltvfLVEQNAFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTT-----LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
.
gi 492862668 234 S 234
Cdd:TIGR02203 556 A 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-221 |
9.85e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 81.06 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG--SPRARTGRILFNGKDItsmPPHEIAKlRIAQSPEGRRIFPRMTVL 105
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL---DKRSFRK-IIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGASLdnqqyfdedvklmfdlfprlkerinqRGgtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFE 185
Cdd:cd03213 101 ETLMFAAKL--------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 492862668 186 AIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNG 221
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQG 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-228 |
1.04e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.38 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRAR--TGRILFNGKDITSMPPHE 83
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 84 IAKLRI---AQSP----------------EGRRIFPRMTVLENLQMgasldnQQYFDEDVKLMfDLFPRLKERINQRGgt 144
Cdd:CHL00131 81 RAHLGIflaFQYPieipgvsnadflrlayNSKRKFQGLPELDPLEF------LEIINEKLKLV-GMDPSFLSRNVNEG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 145 LSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVE--QNAFGALKlADRGYVMVNGS 222
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILIThyQRLLDYIK-PDYVHVMQNGK 229
|
....*.
gi 492862668 223 ITMSGS 228
Cdd:CHL00131 230 IIKTGD 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-235 |
1.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITS-MPPHEIAKLR-----IAQSPEGRrIFP 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRPVRkrigmVFQFPESQ-LFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RmTVLENLQMGA---SLDNQQYFDEDVKLMFDL-FPRlkERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLA 176
Cdd:PRK13646 101 D-TVEREIIFGPknfKMNLDEVKNYAHRLLMDLgFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 177 PLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-171 |
1.43e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditSMPPHE-IAKLriAQSPEgrrIFPRMTVLE 106
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLrIGYL--PQEPP---LDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGAS--LDNQQYFDEDVKLMFDLFP------RLKERINQRGG--------------------------TLSGGEQQM 152
Cdd:COG0488 81 TVLDGDAelRALEAELEELEAKLAEPDEdlerlaELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRR 160
|
170
....*....|....*....
gi 492862668 153 LAIARALMARPKLLLLDEP 171
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-223 |
2.69e-18 |
|
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: 79.18 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIaklriaqspeGRRIfprmtvlen 107
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----------GDHV--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 lqmgasldnqQYFDEDVKLmfdlFP-RLKERInqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEA 186
Cdd:cd03246 79 ----------GYLPQDDEL----FSgSIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 492862668 187 IKELnRTQGLTVFLVEQNAfGALKLADRGYVMVNGSI 223
Cdd:cd03246 139 IAAL-KAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-233 |
3.65e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.09 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMpphEIAKLR--IAQSPEGRRIFPRmTV 104
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRrnIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMG---ASldnqqyfDEDVKLM------FDLFPR----LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13657 426 EDNIRVGrpdAT-------DEEMRAAaeraqaHDFIERkpdgYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 172 SLGLAPLIVKQIFEAIKELnrTQGLTVFLVeqnafgALKL-----ADRGYVMVNGSITMSGSGRELL 233
Cdd:PRK13657 499 TSALDVETEAKVKAALDEL--MKGRTTFII------AHRLstvrnADRILVFDNGRVVESGSFDELV 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-235 |
3.76e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.93 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 2 QAETMQKKQPLLSVEKVETYY-----GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILF----N 72
Cdd:TIGR03269 269 KECEVEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 73 GKDITSMPPHEI--AKLRIAQSPEGRRIFPRMTVLENLQMGASLD--------------NQQYFDEDvklmfdlfpRLKE 136
Cdd:TIGR03269 349 WVDMTKPGPDGRgrAKRYIGILHQEYDLYPHRTVLDNLTEAIGLElpdelarmkavitlKMVGFDEE---------KAEE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 137 RINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL----IVKQIFEAIKELNRtqglTVFLVEQNAFGALKLA 212
Cdd:TIGR03269 420 ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPItkvdVTHSILKAREEMEQ----TFIIVSHDMDFVLDVC 495
|
250 260
....*....|....*....|...
gi 492862668 213 DRGYVMVNGSITMSGSGRELLSD 235
Cdd:TIGR03269 496 DRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-237 |
3.83e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.41 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHE-IAKLR-----IAQSPEGRrIFPR 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLRkkvslVFQFPEAQ-LFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 mTVLENLQMGASldNQQYFDEDVKLMFDLFPR---LKER-INQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:PRK13641 102 -TVLKDVEFGPK--NFGFSEDEAKEKALKWLKkvgLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 178 LIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK13641 179 EGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-237 |
4.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.30 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 3 AETMQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTI-----------FGSPRARTGRILF 71
Cdd:PRK14271 12 AADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrYSGDVLLGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 72 NGKDITSMppheiaKLRIAQSPEGRRIFPrMTVLENLQMGA---SLDNQQYFDEDVKLMFD---LFPRLKERINQRGGTL 145
Cdd:PRK14271 92 NYRDVLEF------RRRVGMLFQRPNPFP-MSIMDNVLAGVrahKLVPRKEFRGVAQARLTevgLWDAVKDRLSDSPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 146 SGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnrTQGLTVFLVEQNAFGALKLADRGYVMVNGSITM 225
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
250
....*....|..
gi 492862668 226 SGSGRELLSDPE 237
Cdd:PRK14271 243 EGPTEQLFSSPK 254
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-236 |
4.71e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.49 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEkVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSP----RARTGRILFNGKDITSMPPHEIAKL- 87
Cdd:COG4170 9 LTIE-IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERRKIi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 88 -----RIAQSPEgRRIFPRMTVLENLqmgasldNQQYFDEDVKLMFdlFPRLKERINQ------RGGT------------ 144
Cdd:COG4170 88 greiaMIFQEPS-SCLDPSAKIGDQL-------IEAIPSWTFKGKW--WQRFKWRKKRaiellhRVGIkdhkdimnsyph 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 145 -LSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:COG4170 158 eLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250
....*....|...
gi 492862668 224 TMSGSGRELLSDP 236
Cdd:COG4170 238 VESGPTEQILKSP 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-237 |
6.73e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.40 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsMPPHEIAKLRIAQS 92
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN-LVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEGRRIFPR-------------MTVLENLqMGA-----SLDNQQYFDEDVKLMFDLfpRLKERINQRGGT-LSGGEQQML 153
Cdd:PRK10619 85 NQLRLLRTRltmvfqhfnlwshMTVLENV-MEApiqvlGLSKQEARERAVKYLAKV--GIDERAQGKYPVhLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 154 AIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
....
gi 492862668 234 SDPE 237
Cdd:PRK10619 241 GNPQ 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-227 |
1.23e-17 |
|
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: 78.46 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRAR---TGRILFNGKDITSMppHEIAKLRIAQSPEGRRIFPRMTV 104
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF--AEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMGASLDNQQYFdedvklmfdlfprlkerinqRGgtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIF 184
Cdd:cd03233 101 RETLDFALRCKGNEFV--------------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492862668 185 EAIKELNRTQGLTVFL-VEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03233 159 KCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-232 |
1.37e-17 |
|
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: 81.88 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGkditsmppheiaklRIAQSPEGRRIFPRmTVLEN 107
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDNQQY--------FDEDVKlmfdLFPRLKERINQRGG-TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL 178
Cdd:TIGR01271 507 IIFGLSYDEYRYtsvikacqLEEDIA----LFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 179 IVKQIFEA--IKEL-NRTQGLTVFLVEQnafgaLKLADRGYVMVNGSITMSGSGREL 232
Cdd:TIGR01271 583 TEKEIFESclCKLMsNKTRILVTSKLEH-----LKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-234 |
1.50e-17 |
|
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: 79.52 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGkditsmppheiaklRIAQSPEGRRIFPRmTVLEN 107
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------------RISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDNQQY--------FDEDVKlmfdLFPRLKERINQRGG-TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL 178
Cdd:cd03291 118 IIFGVSYDEYRYksvvkacqLEEDIT----KFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 179 IVKQIFEA-IKEL--NRTQGLTVFLVEQnafgaLKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:cd03291 194 TEKEIFEScVCKLmaNKTRILVTSKMEH-----LKKADKILILHEGSSYFYGTFSELQS 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-237 |
1.60e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 80.27 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiaklR-IAQSPEGRRI 98
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD----RdIAMVFQNYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 FPRMTVLENlqMGASLDN--------QQYFDEDVKlMFDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:PRK11650 88 YPHMSVREN--MAYGLKIrgmpkaeiEERVAEAAR-ILELEPLLDRKPRE----LSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 171 PSLGL-APLIVKQIFEaIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK11650 161 PLSNLdAKLRVQMRLE-IQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-237 |
1.72e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVETYYGNI----CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG---SPRAR--TGRILFNGKDITSMP 80
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpSPPVVypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 81 PHEIAKLR------IAQSPegrrifprMTVLENLQmgaSLDNQQYfdEDVKL------------MFDLFPRL-----KER 137
Cdd:PRK15134 83 EQTLRGVRgnkiamIFQEP--------MVSLNPLH---TLEKQLY--EVLSLhrgmrreaargeILNCLDRVgirqaAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 138 INQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYV 217
Cdd:PRK15134 150 LTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAV 229
|
250 260
....*....|....*....|
gi 492862668 218 MVNGSITMSGSGRELLSDPE 237
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSAPT 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-238 |
1.80e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDiTSMPPHeIAKLR-----IAQSPEGRRIfpr 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEEN-LWDIRnkagmVFQNPDNQIV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLE--------NLQMgASLDNQQYFDEDVKL--MFDL---FPRLkerinqrggtLSGGEQQMLAIARALMARPKLLLL 168
Cdd:PRK13633 100 ATIVEedvafgpeNLGI-PPEEIRERVDESLKKvgMYEYrrhAPHL----------LSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 169 DEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKlADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEM 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-245 |
1.85e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG--SPRARTGRILFN----------------GK 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 75 DI----TSMPPHEIAKLRIAQsPEGRRIFPRM--------------TVLENLQmgASLDNQQY-FDEDVKLMFDLFP--R 133
Cdd:TIGR03269 81 PCpvcgGTLEPEEVDFWNLSD-KLRRRIRKRIaimlqrtfalygddTVLDNVL--EALEEIGYeGKEAVGRAVDLIEmvQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 134 LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLAD 213
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270
....*....|....*....|....*....|...
gi 492862668 214 RGYVMVNGSITMSGsgrellsDP-EVRAAYLEG 245
Cdd:TIGR03269 238 KAIWLENGEIKEEG-------TPdEVVAVFMEG 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-223 |
2.46e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.96 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYY---------GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsmpp 81
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 82 heiaKLRIAQSPEGRR----IF--------PRMTV----LENLQMGASLD--NQQYFDEDVKLMFDLFPRLKERinqRGG 143
Cdd:PRK10419 78 ----KLNRAQRKAFRRdiqmVFqdsisavnPRKTVreiiREPLRHLLSLDkaERLARASEMLRAVDLDDSVLDK---RPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 144 TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-235 |
2.51e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.02 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPH-EIAKLR-----IAQSPEGRrIFP 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQIRkkvglVFQFPESQ-LFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RmTVLENLQMG------ASLDNQQYFDEDVKLMF---DLFprlkeriNQRGGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13649 101 E-TVLKDVAFGpqnfgvSQEEAEALAREKLALVGiseSLF-------EKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 172 SLGLAPLIVKQIFEAIKELNRTqGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-234 |
2.57e-17 |
|
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: 78.30 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPhEIAKLRIAQSPEGRRIFPRmTVLE 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASLDNQQYFDEDVKLM--FDLFPRLKERINQ----RGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIV 180
Cdd:cd03252 95 NIALADPGMSMERVIEAAKLAgaHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492862668 181 KQIFEAIKELnrTQGLTVFLVEQNaFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:cd03252 175 HAIMRNMHDI--CAGRTVIIIAHR-LSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-224 |
3.61e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 31 IDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRR---IFPRMTVLEN 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGAS---------LDNQQ---YFDEDVKLMfdlfpRLKER-INQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLG 174
Cdd:PRK11288 352 INISARrhhlragclINNRWeaeNADRFIRSL-----NIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492862668 175 LAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSIT 224
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-223 |
4.84e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 31 IDMTVDEGEIVALIGANGAGKSTLMMTIFGS-PRARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRR---IFPRMTVLE 106
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGA--SLDNQQYFDE--DVKLMFDLFPRLKERINQRG---GTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLI 179
Cdd:TIGR02633 359 NITLSVlkSFCFKMRIDAaaELQIIGSAIQRLKVKTASPFlpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492862668 180 VKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSI 223
Cdd:TIGR02633 439 KYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-243 |
5.19e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 26 CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARtGRILFNGKDITSMPP----HEIAKLriAQSPEgrriFPR 101
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPeswrKHLSWV--GQNPQ----LPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGASLDNQQYFDEDVKLMF--DLFPRLKE----RINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK11174 437 GTLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLPQgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 176 APLIVKQIFEAIKELnrTQGLTVFLV----EQnafgaLKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYL 243
Cdd:PRK11174 517 DAHSEQLVMQALNAA--SRRQTTLMVthqlED-----LAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
11-175 |
8.36e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDIT-SMPPHEIAKLri 89
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 aqspeGRRIF--PRMTVLENLQMGASLDNQQYFDEDVKL-MFDLFPRLkeriNQRGGTLSGGEQQMLAIARALMARPKLL 166
Cdd:PRK13539 79 -----GHRNAmkPALTVAENLEFWAAFLGGEELDIAAALeAVGLAPLA----HLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
....*....
gi 492862668 167 LLDEPSLGL 175
Cdd:PRK13539 150 ILDEPTAAL 158
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-236 |
8.97e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 77.86 E-value: 8.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGN----ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG----SPRARTGRILFNGKDITSMPPHE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 84 IAKL------RIAQSPE---------GRRIfprMTVLENLQMGASLDNQQYFDEDVKLMFdlFPRLKERINQRGGTLSGG 148
Cdd:PRK11022 83 RRNLvgaevaMIFQDPMtslnpcytvGFQI---MEAIKVHQGGNKKTRRQRAIDLLNQVG--IPDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 149 EQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGS 228
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....*...
gi 492862668 229 GRELLSDP 236
Cdd:PRK11022 238 AHDIFRAP 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-201 |
9.17e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 9.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 6 MQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPhEIA 85
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 86 KLRI---AQSPEgrrIFPRmTVLENLQMGASLDNQQyfDEDVKLMFDL----FPR--LKERINQrggtLSGGEQQMLAIA 156
Cdd:PRK10247 80 RQQVsycAQTPT---LFGD-TVYDNLIFPWQIRNQQ--PDPAIFLDDLerfaLPDtiLTKNIAE----LSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492862668 157 RALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLV 201
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-228 |
1.12e-16 |
|
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: 79.29 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDI-TSMpphEIAKLRIAQSPEGRRIFPRMTVL 105
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNL---DAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGASLDNQQYfdEDVKLMFDLFPR---LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQ 182
Cdd:TIGR01257 1022 EHILFYAQLKGRSW--EEAQLEMEAMLEdtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492862668 183 IFEAIkeLNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGS 228
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-228 |
1.34e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKdITSMppheiakLRIAQSpegrriF 99
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL-------LELGAG------F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 -PRMTVLENLQMGASL------DNQQYFDEDVKlmfdlFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEps 172
Cdd:COG1134 100 hPELTGRENIYLNGRLlglsrkEIDEKFDEIVE-----FAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 173 lGLApliV------KQIFEAIKELnRTQGLTVFLVEQNAfGALK-LADRGYVMVNGSITMSGS 228
Cdd:COG1134 173 -VLA---VgdaafqKKCLARIREL-RESGRTVIFVSHSM-GAVRrLCDRAIWLEKGRLVMDGD 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-227 |
1.56e-16 |
|
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: 75.65 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItsmPPHEIaklriaqspeGRRIFPR 101
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLLGL----------GGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGASLDNQQyfDEDVKLMFDL---FPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEpslGLA-- 176
Cdd:cd03220 99 LTGRENIYLNGRLLGLS--RKEIDEKIDEiieFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VLAvg 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492862668 177 -PLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSG 227
Cdd:cd03220 174 dAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-234 |
3.41e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIA-- 90
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-RLAll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 ----QSPEGrrifprMTVLENLQMGAS----------LDNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIA 156
Cdd:PRK11231 82 pqhhLTPEG------ITVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 157 RALMARPKLLLLDEPSLGLAplIVKQI--FEAIKELNrTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD--INHQVelMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-198 |
3.83e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 14 SVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmpPHEIAKL--RIAQ 91
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAVcpRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPE--GRRIFPRMTVLENLqmgasldnqqyfdedvklmfDLFPRL--------KERINQ------------R-GGTLSGG 148
Cdd:NF033858 81 MPQglGKNLYPTLSVFENL--------------------DFFGRLfgqdaaerRRRIDEllratglapfadRpAGKLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492862668 149 EQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQ-GLTV 198
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSV 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-201 |
3.96e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditsmppHEIAKLRIA---QSPEGRRI 98
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAyvpQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 FPrMTVLENLQMGASLDN---QQYFDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:NF040873 70 LP-LTVRDLVAMGRWARRglwRRLTRDDRAAVDDALERvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*...
gi 492862668 174 GLAPLIVKQIFEAIKELNRtQGLTVFLV 201
Cdd:NF040873 149 GLDAESRERIIALLAEEHA-RGATVVVV 175
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-234 |
5.84e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.15 E-value: 5.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKL--RIAQSPEGRriFPRMTVL 105
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKigMVFQNPDNQ--FVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGasLDNQ----QYFDEDVKLMFDL--FPRLKERINQRggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLI 179
Cdd:PRK13650 101 DDVAFG--LENKgiphEEMKERVNEALELvgMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 180 VKQIFEAIKELNRTQGLTVFLVEQNaFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-234 |
5.91e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSPEGRRIFPR 101
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR-RIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGaSLDNQQYF------DEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK10253 96 ITVQELVARG-RYPHQPLFtrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 176 AplIVKQI--FEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:PRK10253 175 D--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-241 |
7.63e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKL--RIAQSPEGrRIFPrMTV 104
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKvgLVFQDPDD-QVFS-STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMGA---SLDNQQyFDEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVK 181
Cdd:PRK13647 98 WDDVAFGPvnmGLDKDE-VERRVEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 182 QIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGsGRELLSDPEVRAA 241
Cdd:PRK13647 176 TLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDIVEQ 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-238 |
7.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG------SPRARtgrILFNGKDITSMPPHEI-AKLRIA-QSPEGRri 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddNPNSK---ITVDGITLTAKTVWDIrEKVGIVfQNPDNQ-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 FPRMTVLENLQMGasLDNQQY-FDEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK13640 97 FVGATVGDDVAFG--LENRAVpRPEMIKIVRDVLADvgMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 176 APLIVKQIFEAIKELNRTQGLTVFLVEQNAFGAlKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-234 |
1.14e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTI-FGSPRA--RTGRILFNGKDITSmpphEIAKLRIAQSPEGRRIFPRMTV 104
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGvkGSGSVLLNGMPIDA----KEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LENLQMGASL--DNQQYFDE------DVKLMFDLFPRLKERINQRGGT--LSGGEQQMLAIARALMARPKLLLLDEPSLG 174
Cdd:TIGR00955 117 REHLMFQAHLrmPRRVTKKEkrervdEVLQALGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 175 LAPLIVKQIFEAIKELNrTQGLTVFL-VEQNAFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLA-QKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-238 |
1.29e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITS--MPPHEIAKLR-----IAQSPEgRRIF 99
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLRkeiglVFQFPE-YQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 pRMTVLENLQMGASL--DNQQYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:PRK13645 105 -QETIEKDIAFGPVNlgENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 178 LIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-236 |
1.58e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.62 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTL--MMTIFGSPRArtGRILFNGKDITSMPPHEIAKLR-----IAQSPEGRrIF 99
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETPTG--GELYYQGQDLLKADPEAQKLLRqkiqiVFQNPYGS-LN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 PRMTV----LENLQMGASLDNQQYFDEDVKLM---------FDLFPRLkerinqrggtLSGGEQQMLAIARALMARPKLL 166
Cdd:PRK11308 107 PRKKVgqilEEPLLINTSLSAAERREKALAMMakvglrpehYDRYPHM----------FSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 167 LLDEPSLGLAPLIVKQIFEAIKELNRTQGLT-VFL------VEQnafgalkLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQELGLSyVFIshdlsvVEH-------IADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-244 |
1.73e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGS-PRARTGRILFNGKditsmppheiaklrIAQSPEGRRIFpRMTVLE 106
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVIRGS--------------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASLDNQQYFDE-DVKLM---FDLFP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVK 181
Cdd:PLN03232 698 NILFGSDFESERYWRAiDVTALqhdLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 182 QIFEA-IKElnRTQGLTVFLVeQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAYLE 244
Cdd:PLN03232 778 QVFDScMKD--ELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-170 |
1.82e-15 |
|
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: 75.24 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEiakLR--IAqspegrrIFPRMTVL 105
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRaaIG-------IVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ------ENLQMG---ASldnqqyfDEDV----KL--MFDLFPRLKE----RINQRGGTLSGGEQQMLAIARALMARPKLL 166
Cdd:COG5265 444 fndtiaYNIAYGrpdAS-------EEEVeaaaRAaqIHDFIESLPDgydtRVGERGLKLSGGEKQRVAIARTLLKNPPIL 516
|
....
gi 492862668 167 LLDE 170
Cdd:COG5265 517 IFDE 520
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-212 |
3.20e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmPPHEIAklrIAQ 91
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERG---VVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGrrIFPRMTVLENLQMGASL------DNQQYFDEDVKLMfDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKL 165
Cdd:PRK11248 77 QNEG--LLPWRNVQDNVAFGLQLagvekmQRLEIAHQMLKKV-GLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLA 212
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-238 |
4.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 25 ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFngKDITSmpPHEIAKLRIAQSPEGRRI--FPRM 102
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYI--GDKKNNHELITNPYSKKIknFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLenLQMGASLDNQQYFDEDVK--LMF----------DLFPRLKERINQRG----------GTLSGGEQQMLAIARALM 160
Cdd:PRK13631 115 RRR--VSMVFQFPEYQLFKDTIEkdIMFgpvalgvkksEAKKLAKFYLNKMGlddsylerspFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKElNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-242 |
4.97e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG------SPR--ARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRRIF 99
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggAPRgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 PrMTVLENLQMG----------ASLDNQQYFDEDVKLMfDLFPRLKERINqrggTLSGGEQQMLAIARAL---------M 160
Cdd:PRK13547 97 A-FSAREIVLLGrypharragaLTHRDGEIAWQALALA-GATALVGRDVT----TLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRA 240
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIAR 250
|
..
gi 492862668 241 AY 242
Cdd:PRK13547 251 CY 252
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-238 |
5.39e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItSMPPHEIAKLR-----IAQSPEgRRIFprM 102
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRqqvatVFQDPE-QQIF--Y 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 TVLENlQMGASLDNQQYFDEDVKLMFDLFPRL--KERINQRG-GTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLI 179
Cdd:PRK13638 93 TDIDS-DIAFSLRNLGVPEAEITRRVDEALTLvdAQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 180 VKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEV 238
Cdd:PRK13638 172 RTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-172 |
5.44e-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: 69.78 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditsmppHEIAKLRIAqs 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKIG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegrrifprmtvlenlqmgasldnqqYFDEdvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:cd03221 67 --------------------------YFEQ----------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-241 |
7.23e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.60 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKST--LMMTIFGSPraRTGRILFNGKDITSMPPHEIAK--LRIAQSPEgrrIFPRmT 103
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTvaALLQNLYQP--TGGQVLLDGVPLVQYDHHYLHRqvALVGQEPV---LFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 VLENLQMGAsldnQQYFDEDV----KLMF--DLFPRLKERIN----QRGGTLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:TIGR00958 571 VRENIAYGL----TDTPDEEImaaaKAANahDFIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 174 GLAplivKQIFEAIKELNRTQGLTVFLVeqnaFGALKL---ADRGYVMVNGSITMSGSGRELLSDPEVRAA 241
Cdd:TIGR00958 647 ALD----AECEQLLQESRSRASRTVLLI----AHRLSTverADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-195 |
1.03e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKditsmpPHEIAKLR------IAQSPEGRRIFP 100
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRFASTTaalaagVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RMTVLENLQMG-----ASLDNQQYFDEDVKLMFDlfpRLKERI--NQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSL 173
Cdd:PRK11288 93 EMTVAENLYLGqlphkGGIVNRRLLNYEAREQLE---HLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180
....*....|....*....|..
gi 492862668 174 GLAPLIVKQIFEAIKELnRTQG 195
Cdd:PRK11288 170 SLSAREIEQLFRVIREL-RAEG 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-196 |
1.40e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 7 QKKQPLLSVEKVETYY-----------GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARtGRILFNGKD 75
Cdd:PRK15134 270 EPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 76 ITSMPPHEIAKLR-----IAQSPEGRrIFPRMTVLENLQMG-----ASLDNQQYFDEDVKLMFD--LFPRLKERINqrgG 143
Cdd:PRK15134 349 LHNLNRRQLLPVRhriqvVFQDPNSS-LNPRLNVLQIIEEGlrvhqPTLSAAQREQQVIAVMEEvgLDPETRHRYP---A 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492862668 144 TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGL 196
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQL 477
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-198 |
1.59e-14 |
|
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: 70.19 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItSMPPHEIAKLRIAQSPEGRRIFPRmTVLEN 107
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGAsldnQQYFDEDVKLM------FDLFPRLK----ERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:cd03248 108 IAYGL----QSCSFECVKEAaqkahaHSFISELAsgydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180
....*....|....*....|.
gi 492862668 178 LIVKQIFEAIKELNRTQGLTV 198
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLV 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-175 |
2.10e-14 |
|
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: 69.44 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPhEIAK--LRIAQSPEgrrIFPRMTVL 105
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARglLYLGHAPG---IKTTLSVL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 106 ENLQMGASLDNqqyfDEDVKLMFDlfprlkeRINQRG------GTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:cd03231 92 ENLRFWHADHS----DEQVEEALA-------RVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-201 |
2.62e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGkditsmppheiaKLRIA 90
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------KLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 91 QSPEGRRIFPRM--TVLENLQMGASLDNQqyfdedvklmfDLFPRLK-----ERINQRGGTLSGGEQQMLAIARALMARP 163
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRPGTKKE-----------DILPALKrvqagHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 492862668 164 KLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLV 201
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMV 177
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
29-241 |
2.70e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 29 KGIDMTVDEGEIVALIGANGAGKSTLMMTIFG----SPRARTGRILFNGKditsmpPHEIAKLR------IAQSPegRRI 98
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGilpaGVRQTAGRVLLDGK------PVAPCALRgrkiatIMQNP--RSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 F-PRMT----VLENL-QMGASLDNQQYFD-------EDVKLMFDLFPRlkerinqrggTLSGGEQQMLAIARALMARPKL 165
Cdd:PRK10418 92 FnPLHTmhthARETClALGKPADDATLTAaleavglENAARVLKLYPF----------EMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAA 241
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-190 |
6.02e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRRIFPRMTVLE 106
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASLDNQQYFDEDvKLMFD---LFPRLKERINQR--GGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVK 181
Cdd:PRK10982 93 NMWLGRYPTKGMFVDQD-KMYRDtkaIFDELDIDIDPRakVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
....*....
gi 492862668 182 QIFEAIKEL 190
Cdd:PRK10982 172 HLFTIIRKL 180
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-237 |
6.13e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsmpPHEIAKLR-----IAQSPEGRriFPR 101
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRkhigiVFQNPDNQ--FVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGasLDNQQYFDEDvklMFDLFPR------LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK13648 99 SIVKYDVAFG--LENHAVPYDE---MHRRVSEalkqvdMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 176 APLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKlADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-235 |
7.44e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.73 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDI---TSMPPHEIAKLRIAQSPEGRRIFPRMT 103
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkKKTKEKEKVLEKLVIQKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 VLENlQMGASLDNQQY--FDEDVK--LMF----------DLFPRLKERINQRG----------GTLSGGEQQMLAIARAL 159
Cdd:PRK13651 102 EIRR-RVGVVFQFAEYqlFEQTIEkdIIFgpvsmgvskeEAKKRAAKYIELVGldesylqrspFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 160 MARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-236 |
1.16e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.06 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVE----TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFG----SPRARTGRILFNGKDITSMPPH 82
Cdd:PRK15093 2 PLLDIRNLTiefkTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 83 EIAKL------RIAQSPE---------GRRIFPRMTvlenlqmGASLDNQ--QYFDEDVKLMFDLFPRL-----KERINQ 140
Cdd:PRK15093 82 ERRKLvghnvsMIFQEPQscldpservGRQLMQNIP-------GWTYKGRwwQRFGWRKRRAIELLHRVgikdhKDAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 141 RGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVN 220
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|....*.
gi 492862668 221 GSITMSGSGRELLSDP 236
Cdd:PRK15093 235 GQTVETAPSKELVTTP 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-170 |
1.71e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.45 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditSMPPHE------------IAKLRIAQS-PE 94
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGArvlflpqrpylpLGTLREALLyPA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 95 GRRIFPRMTVLENLqmgasldnqqyfdEDVKLmfdlfPRLKERINQR---GGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:COG4178 451 TAEAFSDAELREAL-------------EAVGL-----GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-197 |
2.00e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTI-----FGSpraRTGRILFNGkditsmpphEIAKLR-IAQSpEGRRI-- 98
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGS---YEGEILFDG---------EVCRFKdIRDS-EALGIvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 99 -------FPRMTVLENLQMG---AS---LDNQQYFDEDVKLMFDLfpRLKERINQRGGTLSGGEQQMLAIARALMARPKL 165
Cdd:NF040905 83 ihqelalIPYLSIAENIFLGnerAKrgvIDWNETNRRARELLAKV--GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190
....*....|....*....|....*....|..
gi 492862668 166 LLLDEPSLGLAPLIVKQIFEAIKELnRTQGLT 197
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLEL-KAQGIT 191
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-171 |
2.08e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 30 GIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsmppheiaklriAQSPEGRR----------IF 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR------------RQRDEYHQdllylghqpgIK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 100 PRMTVLENLQMGASLDNQQyfDEDvklmfDLFPRLkERINQRG------GTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13538 87 TELTALENLRFYQRLHGPG--DDE-----ALWEAL-AQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-236 |
2.72e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsMPPHEIAKLRIaqspegRRIFPRMTVLE 106
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQRI------RMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASldnqQYFDEDVKLMFDLFPRLKE-RINQR--------------GGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK15112 101 NPRQRIS----QILDFPLRLNTDLEPEQREkQIIETlrqvgllpdhasyyPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 172 SLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNaFGALK-LADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQH-LGMMKhISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-242 |
4.25e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.45 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPH-EIAKLR-----IAQSPEGRrIFP 100
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkEIKPVRkkvgvVFQFPESQ-LFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 RmTVLENLQMGASldNQQYFDEDVKLM----FDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLA 176
Cdd:PRK13643 100 E-TVLKDVAFGPQ--NFGIPKEKAEKIaaekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 177 P---LIVKQIFEAIKELNRTQGLTVFLVEQNAfgalKLADRGYVMVNGSITMSGSGRELLSDPEVRAAY 242
Cdd:PRK13643 177 PkarIEMMQLFESIHQSGQTVVLVTHLMDDVA----DYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-200 |
4.41e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQ 91
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGrrIFPRMTVLEN--LQMGASLDNQQyFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLD 169
Cdd:PRK13540 81 HRSG--INPYLTLRENclYDIHFSPGAVG-ITELCRLF-----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|.
gi 492862668 170 EPSLGLAPLIVKQIFEAIKElNRTQGLTVFL 200
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQE-HRAKGGAVLL 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-201 |
5.53e-13 |
|
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: 65.82 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmPPHEIAKLR-------IAQS 92
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESE-PSFEATRSRnrysvayAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PegrrIFPRMTVLENLQMGASLDNQQY--FDEDVKLM--FDLFPRLKE-RINQRGGTLSGGEQQMLAIARALMARPKLLL 167
Cdd:cd03290 88 P----WLLNATVEENITFGSPFNKQRYkaVTDACSLQpdIDLLPFGDQtEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190
....*....|....*....|....*....|....*
gi 492862668 168 LDEPSLGLAPLIVKQIF-EAIKELNRTQGLTVFLV 201
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLV 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-170 |
6.16e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIaKLRIAqspegrrIFPRMTVLEN 107
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKIT-------IIPQDPVLFS 1373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 108 LQMGASLDN-QQYFDEDVKLMFDL---------FP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:TIGR00957 1374 GSLRMNLDPfSQYSDEEVWWALELahlktfvsaLPdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-242 |
6.53e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYG-NICALKGIDMTVDEGEIVALIGANGAGKSTL--MMTIFGSprARTGRILFNGKDITSmppHEIAKLR-------- 88
Cdd:PRK11176 350 TYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYD--IDEGEILLDGHDLRD---YTLASLRnqvalvsq 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 ------------IAQSPEGRriFPRMTVLENLQMGASLDnqqyFDEDVKLMFDLFprlkerINQRGGTLSGGEQQMLAIA 156
Cdd:PRK11176 425 nvhlfndtiannIAYARTEQ--YSREQIEEAARMAYAMD----FINKMDNGLDTV------IGENGVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 157 RALMARPKLLLLDEPSLGLAPLIVKQIFEAIKEL--NRTQgltvfLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLs 234
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELqkNRTS-----LVIAHRLSTIEKADEILVVEDGEIVERGTHAELL- 566
|
....*...
gi 492862668 235 dpEVRAAY 242
Cdd:PRK11176 567 --AQNGVY 572
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-170 |
7.27e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPpHEIAKLRIA---QSPegrrIFPRMTV 104
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAmvqQDP----VVLADTF 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492862668 105 LENLQMGASLDNQQYFD--EDVKLMfDLFPRLKE----RINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:PRK10790 432 LANVTLGRDISEEQVWQalETVQLA-ELARSLPDglytPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-237 |
7.93e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 12 LLSVEKVETYY---GNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmppHEIAKLR 88
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 -----IAQSPEGRriFPRMTVLENLQMGasLDNQQYFDEDVKLMFD---LFPRLKERINQRGGTLSGGEQQMLAIARALM 160
Cdd:PRK13642 81 rkigmVFQNPDNQ--FVGATVEDDVAFG--MENQGIPREEMIKRVDealLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKlADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-190 |
1.11e-12 |
|
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: 64.10 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditSMPPHEiAKLRIAQSPegrrIFPRMTVLEN 107
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE-DLLFLPQRP----YLPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LqmgasldnqqyfdedvklmfdLFPRLKErinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAI 187
Cdd:cd03223 84 L---------------------IYPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
...
gi 492862668 188 KEL 190
Cdd:cd03223 135 KEL 137
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-237 |
1.31e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 38 GEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLR-----IAQSPEGRrIFPRMTV----LENL 108
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRrdiqfIFQDPYAS-LDPRQTVgdsiMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 109 QMGASLDNQQYfDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIK 188
Cdd:PRK10261 429 RVHGLLPGKAA-AARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492862668 189 ELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-233 |
1.36e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKditsmppheiaklrIAQSPEGRRIfPRMTVLEN 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDNQQYFD--EDVKLMFDL--FPR-LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQ 182
Cdd:TIGR00957 719 ILFGKALNEKYYQQvlEACALLPDLeiLPSgDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492862668 183 IFE-AIKELNRTQGLTVFLVeQNAFGALKLADRGYVMVNGSITMSGSGRELL 233
Cdd:TIGR00957 799 IFEhVIGPEGVLKNKTRILV-THGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-227 |
2.64e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 10 QPLLSVEKVE-TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkDITSMPPHEIAKLR 88
Cdd:PRK15056 4 QAGIVVNDVTvTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 ----IAQSPEGRRIFPrmTVLENLQMGASLDNQQYF----DEDVKLMFDLFPR--LKERINQRGGTLSGGEQQMLAIARA 158
Cdd:PRK15056 79 lvayVPQSEEVDWSFP--VLVEDVVMMGRYGHMGWLrrakKRDRQIVTAALARvdMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 159 LMARPKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAFGALKLADRGyVMVNGSITMSG 227
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-202 |
4.36e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 34 TVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFngkditsmppheiaKLRIAQSPEGRRIFPRMTVLENL-QMGA 112
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--------------ELKISYKPQYIKPDYDGTVEDLLrSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 113 SLDNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSlglAPLIVKQ---IFEAIKE 189
Cdd:PRK13409 427 DLGSSYYKSEIIKPL-----QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS---AHLDVEQrlaVAKAIRR 498
|
170
....*....|...
gi 492862668 190 LNRTQGLTVFLVE 202
Cdd:PRK13409 499 IAEEREATALVVD 511
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
28-224 |
5.11e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRAR--TGRILFNGKDITSMPPHEIAKLRIAQSPEGRRIF------ 99
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYglnlid 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 --PRMTVLENLQMGAS---LDNQqyfdEDVKLMFDLFPRLKER---INQRGGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:NF040905 356 diKRNITLANLGKVSRrgvIDEN----EEIKVAEEYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 172 SLGL---AplivK-QIFEAIKELNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSIT 224
Cdd:NF040905 432 TRGIdvgA----KyEIYTIINELAA-EGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-242 |
5.87e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSPEGRRIFPRMTVLEN 107
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGA----------SLDNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAp 177
Cdd:PRK10575 106 VAIGRypwhgalgrfGAADREKVEEAISLV-----GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD- 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492862668 178 lIVKQI--FEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPEVRAAY 242
Cdd:PRK10575 180 -IAHQVdvLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-214 |
6.30e-12 |
|
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: 62.34 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFgsprartgrilfngkditsmppHEIAKLRIAQSPEgrrIFPRMTVLE 106
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------------------YASGKARLISFLP---KFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASLDNQ-QYFdedvklmfdlfprlkeRINQRGGTLSGGEQQMLAIARALMARPK--LLLLDEPSLGLAPLIVKQI 183
Cdd:cd03238 65 IDQLQFLIDVGlGYL----------------TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|.
gi 492862668 184 FEAIKELnRTQGLTVFLVEQNAFgALKLADR 214
Cdd:cd03238 129 LEVIKGL-IDLGNTVILIEHNLD-VLSSADW 157
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-219 |
8.39e-12 |
|
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: 63.20 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 34 TVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItSMPPHEIaklrIAQSPegrrifprMTVLENL-QMGA 112
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYI----KADYE--------GTVRDLLsSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 113 SLDNQQYFDEDVklmfdLFPRLKERI-NQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSlglAPLIVKQIFEAIKELN 191
Cdd:cd03237 88 DFYTHPYFKTEI-----AKPLQIEQIlDREVPELSGGELQRVAIAACLSKDADIYLLDEPS---AYLDVEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|.
gi 492862668 192 R---TQGLTVFLVEQNAFGALKLADRgyVMV 219
Cdd:cd03237 160 RfaeNNEKTAFVVEHDIIMIDYLADR--LIV 188
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-234 |
8.92e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 20 TYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAqspegrrIF 99
Cdd:PRK10522 331 AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA-------VF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 100 PRMTVLENLQmgasldNQQYFDEDVKLMFDLFPRLK--ERINQRGGT-----LSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:PRK10522 404 TDFHLFDQLL------GPEGKPANPALVEKWLERLKmaHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 173 LGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNA--FgalKLADRGYVMVNGSIT-MSGSGRELLS 234
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDhyF---IHADRLLEMRNGQLSeLTGEERDAAS 539
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-172 |
1.26e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRI-LFNGKDITSMPPHEIAKLRI 89
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGR--RIFPRMTvlenlqmgasldNQQYFDedvklMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLL 167
Cdd:PRK10636 391 DESPLQHlaRLAPQEL------------EQKLRD-----YLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
....*
gi 492862668 168 LDEPS 172
Cdd:PRK10636 454 LDEPT 458
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-224 |
2.81e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIAKLRIAQSPEGRR---IFPRMT 103
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 V--------LENLQMGASLDNQQYFDEDVKLMFDLF----PRLKERInqrgGTLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK10982 343 IgfnslisnIRNYKNKVGLLDNSRMKSDTQWVIDSMrvktPGHRTQI----GSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492862668 172 SLGLAPLIVKQIFEAIKEL-NRTQGLTVFLVEQNAFgaLKLADRGYVMVNGSIT 224
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPEL--LGITDRILVMSNGLVA 470
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-175 |
3.97e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRAR--TGRILFNGKDITSmpphEIAKlRIAQSPEGRRIFPRMTVL 105
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILK-RTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGASLDNQQYFDEDVKLmfdlfpRLKER-INQRGGT--------------LSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKI------LVAESvISELGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
....*
gi 492862668 171 PSLGL 175
Cdd:PLN03211 233 PTSGL 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-228 |
4.70e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 19 ETYYGNIcaLKGIDMTVDEGEIVALIGANGAGKSTLMMTI----FGSPRARTGRILFNGkditsMPPHEIAK---LRIAQ 91
Cdd:TIGR00956 70 DTKTFDI--LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG-----ITPEEIKKhyrGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGRRIFPRMTVLENLQMGASLDNQQYF------DEDVKLMFDLFPR---LKERINQRGGT-----LSGGEQQMLAIAR 157
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKTPQNRpdgvsrEEYAKHIADVYMAtygLSHTRNTKVGNdfvrgVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 158 ALMARPKLLLLDEPSLGL----APLIVKQIFEAIKELNRTQGLTVFLVEQNAFgalKLADRGYVMVNGSITMSGS 228
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLdsatALEFIRALKTSANILDTTPLVAIYQCSQDAY---ELFDKVIVLYEGYQIYFGP 294
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-223 |
5.82e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.67 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAG--KSTLMMTIFGsPRA-----RTGRILFNGKDIT-SMPPHEI 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAgrrpwRF*TWCANRRALRrTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 85 AKLRIAQSPEGRrifprmtvlENLQM-GASLDNQQyfdEDVKLMFD-LFPR--LKERINQRGGTLSGGEQQMLAIARALM 160
Cdd:NF000106 93 VR*GRRESFSGR---------ENLYMiGR*LDLSR---KDARARADeLLERfsLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 161 ARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNAFGALKLA------DRGYVMVNGSI 223
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAheltviDRGRVIADGKV 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-171 |
6.05e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 22 YGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSM----PP---------------- 81
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdPPrnvegtvydfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 82 ---------HEIAKLrIAQSPEGRRIfprmTVLENLQmgASLDNQQYFdedvklmfdlfpRLKERINQRGGT-------- 144
Cdd:PRK11147 93 eqaeylkryHDISHL-VETDPSEKNL----NELAKLQ--EQLDHHNLW------------QLENRINEVLAQlgldpdaa 153
|
170 180 190
....*....|....*....|....*....|
gi 492862668 145 ---LSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK11147 154 lssLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-202 |
6.20e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 34 TVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditsmppheIAKLRIAQSPEGRRIFPRMTVLENLQM--G 111
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------------DEDLKISYKPQYISPDYDGTVEEFLRSanT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 112 ASLDNQQYFDEDVKLMfdlfpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSlglAPLIVKQIFE---AIK 188
Cdd:COG1245 428 DDFGSSYYKTEIIKPL-----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS---AHLDVEQRLAvakAIR 499
|
170
....*....|....
gi 492862668 189 ELNRTQGLTVFLVE 202
Cdd:COG1245 500 RFAENRGKTAMVVD 513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-234 |
1.03e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMpphEIAKLRIAQSpegrrIFPRMTVLEN 107
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRRVLS-----IIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDN-QQYFDED---------VKLMFDLFP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLA 176
Cdd:PLN03232 1324 GTVRFNIDPfSEHNDADlwealerahIKDVIDRNPfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 177 PLIVKQIFEAIKELNRTqglTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKS---CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-237 |
1.69e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 25 ICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIF-----GSPRARTGRILFN--GKDITSMPPHEIAKLRIAQSPEGRR 97
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqAGGLVQCDKMLLRrrSRQVIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IF--------PRMTVLEnlQMGASLDNQQYFDED-----VKLMFDL--FPRLKERINQRGGTLSGGEQQMLAIARALMAR 162
Cdd:PRK10261 109 IFqepmtslnPVFTVGE--QIAESIRLHQGASREeamveAKRMLDQvrIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 163 PKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDPE 237
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-221 |
1.90e-10 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 58.81 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMM-TIFG----------SPRARTGRILFNGKDITSM----PPHEIAKLRIAQS 92
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFdTIYAegqrryveslSAYARQFLGQMDKPDVDSIeglsPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 PEG------------RRIFPRMTVLENLQmgasldnqqyFDEDVKLmfdlfPRLkeRINQRGGTLSGGEQQMLAIARALM 160
Cdd:cd03270 91 PRStvgtvteiydylRLLFARVGIRERLG----------FLVDVGL-----GYL--TLSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 161 ARPK--LLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAfGALKLADR------------GYVMVNG 221
Cdd:cd03270 154 SGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHvidigpgagvhgGEIVAQG 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-171 |
6.26e-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: 58.79 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMmtifgsprartgRIL------FNGKdITSMPPHEIAKLriAQSPEgrrIFPR 101
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagvdkdFNGE-ARPQPGIKVGYL--PQEPQ---LDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMGAS--LDNQQYFDE----------DVKLMFDLFPRLKERINQRGG------------------------TL 145
Cdd:TIGR03719 83 KTVRENVEEGVAeiKDALDRFNEisakyaepdaDFDKLAAEQAELQEIIDAADAwdldsqleiamdalrcppwdadvtKL 162
|
170 180
....*....|....*....|....*.
gi 492862668 146 SGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-188 |
8.15e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMpphEIAKLRIAQSpegrrIFPRMTVLEN 107
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLG-----IIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDNqqyFDE--DVKL--------MFDLFPR----LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPS- 172
Cdd:PLN03130 1327 GTVRFNLDP---FNEhnDADLweslerahLKDVIRRnslgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATa 1403
|
170
....*....|....*....
gi 492862668 173 ---LGLAPLIVKQIFEAIK 188
Cdd:PLN03130 1404 avdVRTDALIQKTIREEFK 1422
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-234 |
9.85e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 35 VDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSmpphEIAKLR--IAQSPEGRRIFPRMTVLENLQMGA 112
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHqnMGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 113 SLDNQQyfDEDVKLMFDLFPR---LKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKE 189
Cdd:TIGR01257 2038 RLRGVP--AEEIEKVANWSIQslgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492862668 190 LNRtQGLTVFLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLS 234
Cdd:TIGR01257 2116 IIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-235 |
1.22e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGrilfngkditsmpPHEIAKLRIAQSPEGRRIFpRMTVLEN 107
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-------------ASVVIRGTVAYVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDNQQYFDE-DVKLM---FDLFP--RLKErINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVK 181
Cdd:PLN03130 699 ILFGSPFDPERYERAiDVTALqhdLDLLPggDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 182 QIFEA-IKElnRTQGLTVFLVeQNAFGALKLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PLN03130 778 QVFDKcIKD--ELRGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-189 |
1.24e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMmTIFGSPRARTGRILFNGKDITSMpphEIAKLRIAQSPEGRRIFP-RMTVLE 106
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLL-SALLRLLSTEGEIQIDGVSWNSV---TLQTWRKAFGVIPQKVFIfSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQmgaslDNQQYFDEDV---------KLMFDLFP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLA 176
Cdd:TIGR01271 1311 NLD-----PYEQWSDEEIwkvaeevglKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170
....*....|...
gi 492862668 177 PLIVKQIFEAIKE 189
Cdd:TIGR01271 1386 PVTLQIIRKTLKQ 1398
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-175 |
1.69e-09 |
|
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: 55.71 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRA--RTGRILFNGKditsmpPHEIAKLRIAQSPEGRRIF-PRMTV 104
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGR------PLDKNFQRSTGYVEQQDVHsPNLTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 105 LENLQMGASLdnqqyfdedvklmfdlfprlkerinqRGgtLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:cd03232 97 REALRFSALL--------------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-243 |
1.74e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.92 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 144 TLSGGEQQMLAIARALMARPK--LLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAfGALKLADR------G 215
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDE-QMISLADRiidigpG 553
|
90 100
....*....|....*....|....*....
gi 492862668 216 YVMVNGSITMSGSGRELLSDPE-VRAAYL 243
Cdd:PRK00635 554 AGIFGGEVLFNGSPREFLAKSDsLTAKYL 582
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
66-234 |
2.07e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 66 TGRILFNGKDITSmppHEIAKLR-----IAQSPegrrIFPRMTVLENLQMGasldNQQYFDEDVK----------LMFDL 130
Cdd:PTZ00265 1276 SGKILLDGVDICD---YNLKDLRnlfsiVSQEP----MLFNMSIYENIKFG----KEDATREDVKrackfaaideFIESL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 131 FPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQGLTVFLVEQNaFGALK 210
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIK 1423
|
170 180
....*....|....*....|....*....
gi 492862668 211 LADRGYVMVN----GSITMS-GSGRELLS 234
Cdd:PTZ00265 1424 RSDKIVVFNNpdrtGSFVQAhGTHEELLS 1452
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-235 |
2.96e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; 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: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.02 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMmTIFGSPRARTGRILFNGKDITSMPPHEIAKlRIAQSPEGRRIFPRmTVLEN 107
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLL-SAFLRLLNTEGDIQIDGVSWNSVPLQKWRK-AFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQmgaslDNQQYFDEDV---------KLMFDLFP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:cd03289 97 LD-----PYGKWSDEEIwkvaeevglKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 178 LIVKQIFEAIKElnRTQGLTVFLVEQNAFGALKlADRGYVMVNGSITMSGSGRELLSD 235
Cdd:cd03289 172 ITYQVIRKTLKQ--AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-236 |
3.74e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEIaKLRIA---QSPegrRIFPRmT 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW-RSRLAvvsQTP---FLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 104 VLENLQMGASLDNQQYFDEDVKL--MFDLFPRLKE----RINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARLasVHDDILRLPQgydtEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 178 LIVKQIFEAIKELNrtQGLTVfLVEQNAFGALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PRK10789 485 RTEHQILHNLRQWG--EGRTV-IISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-175 |
3.92e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIfgSPRARTGRI-----LFNGKDITSMPPHEIA-----KLRIAQSpegrr 97
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVItggdrLVNGRPLDSSFQRSIGyvqqqDLHLPTS----- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 ifprmTVLENLQMGASL---------DNQQYFDEDVKL--MFDLFPRLkerINQRGGTLSGGEQQMLAIARALMARPKLL 166
Cdd:TIGR00956 852 -----TVRESLRFSAYLrqpksvsksEKMEYVEEVIKLleMESYADAV---VGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170
....*....|
gi 492862668 167 L-LDEPSLGL 175
Cdd:TIGR00956 924 LfLDEPTSGL 933
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
28-204 |
5.27e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.31 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARtgriLFNGKDITSMPPHEIAKLR-------IAQSPEGRRifP 100
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALAR----RLHLKKEQPGNHDRIEGLEhidkvivIDQSPIGRT--P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 101 R---------MT------------------VLENLQMGASLDnqqyfdeDVKLM--------FDLFPRLKERIN------ 139
Cdd:cd03271 85 RsnpatytgvFDeirelfcevckgkrynreTLEVRYKGKSIA-------DVLDMtveealefFENIPKIARKLQtlcdvg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492862668 140 -------QRGGTLSGGEQQMLAIARALMAR---PKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQN 204
Cdd:cd03271 158 lgyiklgQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHN 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-77 |
5.45e-09 |
|
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: 55.96 E-value: 5.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 492862668 31 IDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDIT 77
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-175 |
8.05e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSP--RARTGRILFNGKDITSMPPHEIAKLRI---AQSP-----EGRR 97
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIfmaFQYPveipgVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IFPRMTV--LENLQMGASLDN---QQYFDEDVKLMfDLFPRLKERINQRGgtLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:PRK09580 97 FFLQTALnaVRSYRGQEPLDRfdfQDLMEEKIALL-KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDESD 173
|
...
gi 492862668 173 LGL 175
Cdd:PRK09580 174 SGL 176
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-201 |
8.35e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITsmppheiaklriaqspegrrIFPRMTVLEN 107
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------------FGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASLDNQQYFDEDVKL--MFDLFPRLKErinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPLIVKQIFE 185
Cdd:COG2401 106 IGRKGDFKDAVELLNAVGLsdAVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*.
gi 492862668 186 AIKELNRTQGLTVFLV 201
Cdd:COG2401 178 NLQKLARRAGITLVVA 193
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-171 |
1.51e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNgkditsmppheiaklriaqs 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 93 pegrrifprmtvlENLQMG-ASLDNQQYFDEDVKLmFD----------------------LFPrlKERINQRGGTLSGGE 149
Cdd:PRK15064 380 -------------ENANIGyYAQDHAYDFENDLTL-FDwmsqwrqegddeqavrgtlgrlLFS--QDDIKKSVKVLSGGE 443
|
170 180
....*....|....*....|..
gi 492862668 150 QQMLAIARALMARPKLLLLDEP 171
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEP 465
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-248 |
1.92e-08 |
|
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: 54.63 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 139 NQRGGTLSGGEQQMLAIARALMARPK--LLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNAfGALKLADR-- 214
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE-DTIRAADYvi 560
|
90 100 110
....*....|....*....|....*....|....*....
gi 492862668 215 ----GYVMVNGSITMSGSGRELLSDPE-VRAAYLEGGRH 248
Cdd:TIGR00630 561 digpGAGEHGGEVVASGTPEEILANPDsLTGQYLSGRKK 599
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-171 |
2.30e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditsmppHEIAKLRIAQSPEGRRIF-PRMTVLE 106
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HCGTKLEVAYFDQHRAELdPEKTVMD 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492862668 107 NLQMGAS-----------LDNQQYFdedvklmfdLFPRLKERINQRGgtLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK11147 403 NLAEGKQevmvngrprhvLGYLQDF---------LFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-215 |
3.29e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSpraRTGRILFNGKDITSMPPHEIAKLRIAQSPEGRRIF-PRMTVLE 106
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHsPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 NLQMGASLDNQQYFDEDVKLMF-DLFPRLKERINQR-------GGT-LSGGEQQMLAIARALMARPKLLLLDEPSLGL-- 175
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMFvDEVMELVELDNLKdaivglpGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLda 1052
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492862668 176 -APLIVKQIFEAIKELNRTqglTVFLVEQ------NAFGALKLADRG 215
Cdd:PLN03140 1053 rAAAIVMRTVRNTVDTGRT---VVCTIHQpsidifEAFDELLLMKRG 1096
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-235 |
1.02e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 32 DMTVDEGEIVALIGANGAGKSTLmmtifgsPRARTGR-ILFNGKDITSMppHEIAKLRIAQ-----SPEGRRIFPRM--- 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSAL-------ARALAGElPLLSGERQSQF--SHITRLSFEQlqklvSDEWQRNNTDMlsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 103 -------TVLENLQMGASlDNQQYfdEDVKLMFDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PRK10938 94 geddtgrTTAEIIQDEVK-DPARC--EQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492862668 176 APLIVKQIFEAIKELNrTQGLTVFLVeQNAFGAL-KLADRGYVMVNGSITMSGSGRELLSD 235
Cdd:PRK10938 167 DVASRQQLAELLASLH-QSGITLVLV-LNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-171 |
1.52e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMmtifgsprartgRIL------FNGkDITSMPPHEIAKLriAQSPEgrrIFPR 101
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagvdkeFEG-EARPAPGIKVGYL--PQEPQ---LDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 102 MTVLENLQMG-----ASLD-----NQQYFDEDV---KLMfDLFPRLKERINQRGG------------------------T 144
Cdd:PRK11819 85 KTVRENVEEGvaevkAALDrfneiYAAYAEPDAdfdALA-AEQGELQEIIDAADAwdldsqleiamdalrcppwdakvtK 163
|
170 180
....*....|....*....|....*..
gi 492862668 145 LSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-172 |
3.68e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 13 LSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNgkditsmpphEIAKLR-IAQ 91
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----------ETVKLAyVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEGrrIFPRMTV-------LENLQMG-ASLDNQQYFDedvklmfdlfprlkeRINQRG-------GTLSGGEQQMLAIA 156
Cdd:TIGR03719 393 SRDA--LDPNKTVweeisggLDIIKLGkREIPSRAYVG---------------RFNFKGsdqqkkvGQLSGGERNRVHLA 455
|
170
....*....|....*.
gi 492862668 157 RALMARPKLLLLDEPS 172
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPT 471
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-170 |
4.66e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 40 IVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDItsmppHEIAKLRIAQSPEGRRIFPRMTVLENLQMGASLDNQQy 119
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-----NNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492862668 120 fdEDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:PRK13541 102 --ETLYAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-237 |
4.89e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMppheiaKLRiaqspEGRRIF---PRMTV 104
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY------GLR-----ELRRQFsmiPQDPV 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 105 LenlqmgasldnqqyFDEDVKLMFDLFPR--------------LKER-------INQR----GGTLSGGEQQMLAIARAL 159
Cdd:PTZ00243 1395 L--------------FDGTVRQNVDPFLEassaevwaalelvgLRERvasesegIDSRvlegGSNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 160 MAR-PKLLLLDEPSLGLAPLIVKQIFEAIkelnrtqgLTVFlveqNAFGALKLA---------DRGYVMVNGSITMSGSG 229
Cdd:PTZ00243 1461 LKKgSGFILMDEATANIDPALDRQIQATV--------MSAF----SAYTVITIAhrlhtvaqyDKIIVMDHGAVAEMGSP 1528
|
....*...
gi 492862668 230 RELLSDPE 237
Cdd:PTZ00243 1529 RELVMNRQ 1536
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-204 |
5.55e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 9 KQPLLSVEKVETYYgnicALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGkditsmpphEIAKLR 88
Cdd:PRK13546 25 KDALIPKHKNKTFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------EVSVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 89 IAQSPEGrrifpRMTVLENLQ-----MGASLdnqqyfDEDVKLMFDL--FPRLKERINQRGGTLSGGEQQMLAIARALMA 161
Cdd:PRK13546 92 ISAGLSG-----QLTGIENIEfkmlcMGFKR------KEIKAMTPKIieFSELGEFIYQPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492862668 162 RPKLLLLDEP-SLG---LAPLIVKQIFEaIKELNRtqglTVFLVEQN 204
Cdd:PRK13546 161 NPDILVIDEAlSVGdqtFAQKCLDKIYE-FKEQNK----TIFFVSHN 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-236 |
1.07e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILfngkditsmppheiAKLRIAQSPEGRRIfprmtvlen 107
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWI--------- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 lqMGASL-DNQQYFDED-----------VKLMFD---LFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:PTZ00243 733 --MNATVrGNILFFDEEdaarladavrvSQLEADlaqLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 173 LGL----APLIVKQIFeaikeLNRTQGLTVFLVEQNAFgALKLADRGYVMVNGSITMSGSGRELLSDP 236
Cdd:PTZ00243 811 SALdahvGERVVEECF-----LGALAGKTRVLATHQVH-VVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-231 |
1.10e-06 |
|
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: 48.13 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 16 EKVETYYGNICALKGIDmTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRilFNGKD-----ITSMPPHEI------ 84
Cdd:cd03236 5 EPVHRYGPNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELqnyftk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 85 ---AKLRIAQSPEGRRIFPRM---TVLENLQmgaSLDNQQYFDEDVKLMfDLFPRLKERINQrggtLSGGEQQMLAIARA 158
Cdd:cd03236 82 lleGDVKVIVKPQYVDLIPKAvkgKVGELLK---KKDERGKLDELVDQL-ELRHVLDRNIDQ----LSGGELQRVAIAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 159 LMARPKLLLLDEPSlglAPLIVKQIFEA---IKELNRtQGLTVFLVEQNAFGALKLADRGYVM-----VNGSITMSGSGR 230
Cdd:cd03236 154 LARDADFYFFDEPS---SYLDIKQRLNAarlIRELAE-DDNYVLVVEHDLAVLDYLSDYIHCLygepgAYGVVTLPKSVR 229
|
.
gi 492862668 231 E 231
Cdd:cd03236 230 E 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-170 |
1.11e-06 |
|
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: 48.37 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMPPHEI-AKLRIA-QSPegrrIFPRMTVL 105
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLrSRLSIIlQDP----ILFSGSIR 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGASLDNQQYFD----EDVKLMFDLFP-RLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDE 170
Cdd:cd03288 113 FNLDPECKCTDDRLWEaleiAQLKNMVKSLPgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 182
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-201 |
1.20e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 27 ALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGkditsmpphEIAKLRIAQSPEGrrifpRMTVLE 106
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------SAALIAISSGLNG-----QLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 107 N-----LQMGASldnQQYFDEDVKLMFDlFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEP-SLGlapliv 180
Cdd:PRK13545 105 NielkgLMMGLT---KEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG------ 174
|
170 180
....*....|....*....|....*
gi 492862668 181 KQIF--EAIKELN--RTQGLTVFLV 201
Cdd:PRK13545 175 DQTFtkKCLDKMNefKEQGKTIFFI 199
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-213 |
2.49e-06 |
|
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: 48.09 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 137 RINQRGGTLSGGEQQMLAIARALMAR---PKLLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQNaFGALKLAD 213
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHN-LDVIKTAD 899
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-218 |
2.90e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492862668 144 TLSGGEQQMLAIARALMA---RPKLLLLDEPSLGLAPLIVKQIFEAIKELNRtQGLTVFLVEQNaFGALKLADrgYVM 218
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHN-MHVVKVAD--YVL 882
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-198 |
3.28e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 2 QAETMQKKQPLLSVEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGS-PRART------GRILFNGK 74
Cdd:PRK10938 250 ARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGYSndltlfGRRRGSGE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 75 DITSMPPHeI--------------AKLR------------IAQSPEGRRIFPRMTVLENLQMGASLDNQQYFDedvklmf 128
Cdd:PRK10938 330 TIWDIKKH-IgyvssslhldyrvsTSVRnvilsgffdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHS------- 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492862668 129 dlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL---IVKQIFEAIKELNRTQGLTV 198
Cdd:PRK10938 402 ----------------LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLnrqLVRRFVDVLISEGETQLLFV 458
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-202 |
5.16e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 34 TVDEGEIVALIGANGAGKSTlMMTI--------FGSP----------RARTGRILFNG-KDITSmppheiAKLRIAQSPE 94
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTT-AVKIlsgelipnLGDYeeepswdevlKRFRGTELQNYfKKLYN------GEIKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 95 GRRIFPRM---TVLENLqmgASLDNQQYFDEDVKLmFDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLLLDEP 171
Cdd:PRK13409 168 YVDLIPKVfkgKVRELL---KKVDERGKLDEVVER-LGLENILDRDISE----LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 492862668 172 SlglAPLIVKQIFEA---IKELnrTQGLTVFLVE 202
Cdd:PRK13409 240 T---SYLDIRQRLNVarlIREL--AEGKYVLVVE 268
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-214 |
5.41e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 11 PLLSVEKVeTYYGNICALKG-IDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGKDITSMpphEIAKLrI 89
Cdd:PRK13543 10 PLLAAHAL-AFSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRF-M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 90 AQSPEGRRIFPRMTVLENLQMGASLDNQ--QYFDEDVKLMFDLFPRLKERINQrggtLSGGEQQMLAIARALMARPKLLL 167
Cdd:PRK13543 85 AYLGHLPGLKADLSTLENLHFLCGLHGRraKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492862668 168 LDEPSLGLAPLIVKQIFEAIKELNRTQGLTVfLVEQNAFGALKLADR 214
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISAHLRGGGAAL-VTTHGAYAAPPVRTR 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
35-217 |
1.11e-05 |
|
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: 44.49 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 35 VDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditsmpphEIAKLRIAQSPegrrifprmtvlenlqmgasl 114
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWDGITPVYKP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 115 dnqQYFDedvklmfdlfprlkerinqrggtLSGGEQQMLAIARALMARPKLLLLDEPSlglAPLIVKQ---IFEAIKELN 191
Cdd:cd03222 68 ---QYID-----------------------LSGGELQRVAIAAALLRNATFYLFDEPS---AYLDIEQrlnAARAIRRLS 118
|
170 180
....*....|....*....|....*.
gi 492862668 192 RTQGLTVFLVEQNAFGALKLADRGYV 217
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
35-193 |
1.54e-05 |
|
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: 45.51 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 35 VDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRIlfngkditSMPPhEIAKLRIAQSPE-GRR------IFPrMTVLEN 107
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL--------TKPA-KGKLFYVPQRPYmTLGtlrdqiIYP-DSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 108 LQMGASldnqqyfDEDVKLMFDLFPRlkERINQRGG----------TLSGGEQQMLAIARALMARPKLLLLDEPSLGLAP 177
Cdd:TIGR00954 545 KRRGLS-------DKDLEQILDNVQL--THILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170
....*....|....*.
gi 492862668 178 LIVKQIFEAIKELNRT 193
Cdd:TIGR00954 616 DVEGYMYRLCREFGIT 631
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-202 |
1.62e-05 |
|
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: 45.55 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 37 EGEIVALIGANGAGKSTLMmtifgspRARTGRILFNGKDITSMPPHE--IAKLRiaqspeGRRIFPRMTVLENLQMGASL 114
Cdd:COG1245 98 KGKVTGILGPNGIGKSTAL-------KILSGELKPNLGDYDEEPSWDevLKRFR------GTELQDYFKKLANGEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 115 DNQQ------YFDEDVKlmfDLFPRLKER---------------INQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSl 173
Cdd:COG1245 165 KPQYvdlipkVFKGTVR---ELLEKVDERgkldelaeklgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPS- 240
|
170 180 190
....*....|....*....|....*....|..
gi 492862668 174 glAPLIVKQ---IFEAIKELNRtQGLTVFLVE 202
Cdd:COG1245 241 --SYLDIYQrlnVARLIRELAE-EGKYVLVVE 269
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-199 |
5.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 21 YYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNGK-DITSMPPHEIAKLRIAQSP--EGRR 97
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGLDLSSNPllYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 98 IFPrmTVLENlQMGASLDNqqyfdedvklmFDLFPRLKErinQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAp 177
Cdd:PLN03073 598 CFP--GVPEQ-KLRAHLGS-----------FGVTGNLAL---QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD- 659
|
170 180
....*....|....*....|..
gi 492862668 178 livkqiFEAIKELnrTQGLTVF 199
Cdd:PLN03073 660 ------LDAVEAL--IQGLVLF 673
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-194 |
6.39e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 28 LKGIDMTVDEGeIVALIGANGAGKSTLM---MTIFGSPRARTGRIL-FNGKDITSMPPHEI------------AKLRIAQ 91
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILealRLLLGPSSSRKFDEEdFYLGDDPDLPEIEIeltfgsllsrllRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 92 SPEG-----------------------RRIFPRMTVLENLQMGASLDNQQYFDEDVKLMFDLFPRLkeRINQRGgtlsGG 148
Cdd:COG3593 93 DKEEleealeelneelkealkalnellSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKEL--PLDRLG----SG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492862668 149 EQQMLAIA--RALM-----ARPKLLLLDEPSLGLAPLIVKQIFEAIKELNRTQ 194
Cdd:COG3593 167 FQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKP 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-172 |
8.28e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 15 VEKVETYYGNICALKGIDMTVDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRILFNgkditsmpphEIAKLR-IAQSP 93
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----------ETVKLAyVDQSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 94 EGrrIFPRMTV-------LENLQMGasldnqqyfdedvklmfdlfprlKERINQRG----------------GTLSGGEQ 150
Cdd:PRK11819 397 DA--LDPNKTVweeisggLDIIKVG-----------------------NREIPSRAyvgrfnfkggdqqkkvGVLSGGER 451
|
170 180
....*....|....*....|..
gi 492862668 151 QMLAIARALMARPKLLLLDEPS 172
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPT 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-200 |
8.96e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 38 GEIVALIGANGAGKSTLMMTIFG-----SPRARtgriLFnGKDITsmpPHEIA-KLRI---AQSpegrriFP---RMTVL 105
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGllpasEGEAW----LF-GQPVD---AGDIAtRRRVgymSQA------FSlygELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 ENLQMGASLdnqqyFD-------EDVKLMFDLFpRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGLAPL 178
Cdd:NF033858 358 QNLELHARL-----FHlpaaeiaARVAEMLERF-DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180
....*....|....*....|..
gi 492862668 179 IVKQIFEAIKELNRTQGLTVFL 200
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFI 453
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-201 |
1.11e-04 |
|
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: 41.20 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 38 GEIVALIGANGAGKSTLMMTIfgsprartgrilfngkditsmppheiakLRIAQSPEGRRIfprmtvlenlqmgasldnq 117
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL----------------------------ARELGPPGGGVI------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 118 qYFDEDVKLMFDLFPRLKERINQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL-----APLIVKQIFEAIKELNR 192
Cdd:smart00382 35 -YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLdaeqeALLLLLEELRLLLLLKS 113
|
....*....
gi 492862668 193 TQGLTVFLV 201
Cdd:smart00382 114 EKNLTVILT 122
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
24-190 |
1.93e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 24 NICALKGIDmTVD-EGEIVALIGANGAGKSTLMMTI----FGSPRARTG---RILFNGKDITSM---------------P 80
Cdd:COG0419 9 NFRSYRDTE-TIDfDDGLNLIVGPNGAGKSTILEAIryalYGKARSRSKlrsDLINVGSEEASVelefehggkryrierR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 81 PHEIAKLRIAQSPEGRRIFPRMTVLENL-QMGASLDNQQYFDEDVKLMFDLFPRLKERINQR------GGTLSGGEQQML 153
Cdd:COG0419 88 QGEFAEFLEAKPSERKEALKRLLGLEIYeELKERLKELEEALESALEELAELQKLKQEILAQlsgldpIETLSGGERLRL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 492862668 154 AIARALMarpklLLLDEPSLGlaPLIVKQIFEAIKEL 190
Cdd:COG0419 168 ALADLLS-----LILDFGSLD--EERLERLLDALEEL 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-175 |
2.56e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 29 KGIDMTVDEGEIVALIGANGAGKSTLMMTI--FGSP---------------------RARTGRI---------------- 69
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIerLYDPtegdiiindshnlkdinlkwwRSKIGVVsqdpllfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 70 --LFNGKDITSMPPHEIAKLRIAQSPEGRRIFPRMTVLENLQ-MGASLDNQQYF----------DEDVK------LMFDL 130
Cdd:PTZ00265 482 ysLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNdMSNTTDSNELIemrknyqtikDSEVVdvskkvLIHDF 561
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492862668 131 FPRLKER----INQRGGTLSGGEQQMLAIARALMARPKLLLLDEPSLGL 175
Cdd:PTZ00265 562 VSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
35-69 |
2.83e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.46 E-value: 2.83e-04
10 20 30
....*....|....*....|....*....|....*
gi 492862668 35 VDEGEIVALIGANGAGKSTLMMTIFGSPRARTGRI 69
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-204 |
6.22e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 6.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492862668 144 TLSGGEQQMLAIARALMARPK---LLLLDEPSLGLAPLIVKQIFEAIKELnRTQGLTVFLVEQN 204
Cdd:COG0178 826 TLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRL-VDKGNTVVVIEHN 888
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
41-70 |
1.28e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.36 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|
gi 492862668 41 VALIGANGAGKSTLMMTIFGSPRARTGRIL 70
Cdd:COG3596 42 IALVGKTGAGKSSLINALFGAEVAEVGVGR 71
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-222 |
1.79e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 26 CALKGIDMTVDEGEIVALIGANGAGKSTLMMTIfgsprartGRILFngkditsmppheiaklrIAQSPEGRRifprmtvl 105
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI--------GLALG-----------------GAQSATRRR-------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492862668 106 enlqmgaSLDNQQYFDEDVKLMFDLFprlkerINQrggtLSGGEQQMLAIARAL----MARPKLLLLDEPSLGLAPLIVK 181
Cdd:cd03227 56 -------SGVKAGCIVAAVSAELIFT------RLQ----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492862668 182 QIFEAIKEL--NRTQGLTVFLVEQNAFGALKLADRGYVMVNGS 222
Cdd:cd03227 119 ALAEAILEHlvKGAQVIVITHLPELAELADKLIHIKKVITGVY 161
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-172 |
2.05e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 2.05e-03
10 20
....*....|....*....|....*....
gi 492862668 144 TLSGGEQQMLAIARALMARPKLLLLDEPS 172
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
30-72 |
2.79e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 2.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 492862668 30 GIDMTVDEGEIVALIGANGAGKSTL---MMTIF-GSPRARtgrilFN 72
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLldaIQTLLvPAKRAR-----FN 55
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-202 |
4.75e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492862668 143 GTLSGGEQQ--MLA--IARALMArpKLLLLDEPSLGLAP-----LIvkqifEAIKELnRTQGLTVFLVE 202
Cdd:COG0178 484 GTLSGGEAQriRLAtqIGSGLVG--VLYVLDEPSIGLHQrdndrLI-----ETLKRL-RDLGNTVIVVE 544
|
|
| |
