|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-333 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 557.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 241 VNSAFAAKIPEDVQKELQ---TTGEIVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLIIHMQGEQNE 317
Cdd:COG1135 241 LPTVLNDELPEELLARLReaaGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330
....*....|....*.
gi 446493510 318 INRALSFLQEQGIIVE 333
Cdd:COG1135 321 IDAALAYLREQGVVVE 336
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-333 |
7.50e-179 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 498.94 E-value: 7.50e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 241 VNSAFAAKIPEDVQKELQTT-----GEIVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLIIHMQGEQ 315
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEpttgsGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330
....*....|....*...
gi 446493510 316 NEINRALSFLQEQGIIVE 333
Cdd:PRK11153 321 GDIQAAIAYLQEHGVKVE 338
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
2.10e-142 |
|
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: 402.34 E-value: 2.10e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-333 |
3.66e-127 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 368.06 E-value: 3.66e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 241 VNSAFAAKIPEDVQKELQTTG-----EIVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLIIHMQGEQ 315
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPfadsvPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330
....*....|....*...
gi 446493510 316 NEINRALSFLQEQGIIVE 333
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVE 338
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-242 |
1.77e-103 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 303.84 E-value: 1.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtLSAKELAKA 80
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIAL-PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKK 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
...
gi 446493510 240 FVN 242
Cdd:COG1126 235 FLS 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
4.54e-98 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 289.64 E-value: 4.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 R-QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVE 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-244 |
1.29e-95 |
|
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: 293.35 E-value: 1.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTK-KGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAK 79
Cdd:COG1123 260 LLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 ARQKIGMIFQG----FNllKTVTVYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLFTR-KDAYPSELSGGQKQRVAIAR 153
Cdd:COG1123 340 LRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
250
....*....|.
gi 446493510 234 HVTTKKFVNSA 244
Cdd:COG1123 498 HPYTRALLAAV 508
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
1.17e-89 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 268.07 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkKGNVEALKSTSLQVKKGE-VFgIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAK 79
Cdd:COG2884 1 MIRFENVSKRY---PGGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 ARQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
2.33e-88 |
|
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: 264.35 E-value: 2.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 -QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-234 |
3.16e-87 |
|
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: 265.38 E-value: 3.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV-NLLEKP--TTGNIIVNSQDLTTLSAKEL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKAR-QKIGMIFQG----FNLLKTVtvYENIALPLRL-AGISKVEIEKRVEKYLRIVDL---FTRKDAYPSELSGGQKQR 148
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLNPVMTV--GDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 149 VAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*.
gi 446493510 229 FTNPQH 234
Cdd:COG0444 239 FENPRH 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-246 |
6.47e-87 |
|
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: 262.05 E-value: 6.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELaka 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQ----GFNLLKTVtvYENIALPLRLAGISkvEIEKRVEKYLRIVDLFTR-KDAYPSELSGGQKQRVAIARAL 155
Cdd:COG1124 78 RRRVQMVFQdpyaSLHPRHTV--DRILAEPLRIHGLP--DREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 156 SHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHV 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|.
gi 446493510 236 TTKKFVNSAFA 246
Cdd:COG1124 234 YTRELLAASLA 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
7.62e-87 |
|
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: 261.45 E-value: 7.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLR-LAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
4.02e-82 |
|
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: 248.60 E-value: 4.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtLSAKELAKAR 81
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLA-GISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
5.07e-82 |
|
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: 248.57 E-value: 5.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQ--GFNLLKTVTVYENIALPLRLAGISKVE--IEKRVEKYLRIVDLF-TRKDAYPSELSGGQKQRVAIARAL 155
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 156 SHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-232 |
4.76e-80 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 245.00 E-value: 4.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSqdlttlsaKELAKA 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHemNV---IqRICDRVAVMEHGavveSGTVKDIFTNP 232
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH--DVdeaV-FLADRVVVLSAR----PGRIVEEIDVD 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
7.87e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 243.81 E-value: 7.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENI---ALP----LR-LAGI-SKVEIEkRVEKYLRIVDL----FTRKDaypsELSGGQKQ 147
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVlagRLGrtstWRsLLGLfPPEDRE-RALEALERVGLadkaYQRAD----QLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-249 |
5.17e-79 |
|
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: 242.55 E-value: 5.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGNV-----------EALKST---------SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGN 61
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAfkllakgkskeEILKKTgqtvgvndvSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 62 IIVNSQDLTTLSAKELAKAR-QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSE 140
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....*....
gi 446493510 221 ESGTVKDIFTNPQHVTTKKFVNSAFAAKI 249
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
1.38e-78 |
|
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: 239.93 E-value: 1.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTtkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsAKELAKAR 81
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQgfN----LLKTvTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:COG1122 75 RKVGLVFQ--NpddqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
2.94e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 239.20 E-value: 2.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLttlsAKELAKAR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
1.57e-77 |
|
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: 236.65 E-value: 1.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAkelakAR 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-----ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-232 |
3.61e-77 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 241.93 E-value: 3.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVF--------------TTKK------GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTG 60
Cdd:COG4175 3 KIEVRNLYKIFgkrperalklldqgKSKDeilektGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 61 NIIVNSQDLTTLSAKELAKARQ-KIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPS 139
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 140 ELSGGQKQRVAIARALSHEPEVLLSDEATSALDPettdsiL------DLLLKINEEIGITILLITHEMNVIQRICDRVAV 213
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDP------LirremqDELLELQAKLKKTIVFITHDLDEALRLGDRIAI 236
|
250
....*....|....*....
gi 446493510 214 MEHGAVVESGTVKDIFTNP 232
Cdd:COG4175 237 MKDGRIVQIGTPEEILTNP 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-233 |
1.19e-76 |
|
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: 235.09 E-value: 1.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR 81
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF--TNPQ 233
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-280 |
1.04e-75 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 236.92 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaka 80
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQkIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG3842 77 RN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEmnviQ----RICDRVAVMEHGAVVESGTVKDIFTNPQHVT 236
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD----QeealALADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446493510 237 TKKFVNSA--FAAKIPEDVQKELQTTGEIVTLSFIGN-SSGEPALAV 280
Cdd:COG3842 232 VADFIGEAnlLPGTVLGDEGGGVRTGGRTLEVPADAGlAAGGPVTVA 278
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-246 |
1.52e-74 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 230.84 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTT--------- 71
Cdd:COG4598 8 ALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 72 -LSAKELAKARQKIGMIFQGFNLLKTVTVYEN-IALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRV 149
Cdd:COG4598 84 pADRRQLQRIRTRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 150 AIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*..
gi 446493510 230 TNPQHVTTKKFVNSAFA 246
Cdd:COG4598 243 GNPKSERLRQFLSSSLK 259
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.32e-73 |
|
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: 236.34 E-value: 1.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPT---TGNIIVNSQDLTTLSAKEL 77
Cdd:COG1123 4 LLEVRDLS--VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKarqKIGMIFQGF-NLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALS 156
Cdd:COG1123 82 GR---RIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-217 |
1.04e-71 |
|
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: 220.52 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSaKELAKAR 81
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLrlagiskveiekrvekylrivdlftrkdaypselSGGQKQRVAIARALSHEPEV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-236 |
2.53e-71 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 221.89 E-value: 2.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElAKA 80
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIAL-PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP------- 232
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPpsqrlqe 234
|
....*.
gi 446493510 233 --QHVT 236
Cdd:PRK09493 235 flQHVS 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-228 |
4.68e-71 |
|
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: 221.29 E-value: 4.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR 81
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIaLPLRLAGISKV--------EIEKRVEKY-LRIVDLFTRKDAYPSELSGGQKQRVAIA 152
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENV-LSGRLGRRSTWrslfglfpKEEKQRALAaLERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 153 RALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
5.44e-71 |
|
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: 220.52 E-value: 5.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEK-----PTTGNIIVNSQDLTTLSAKE 76
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 LAkARQKIGMIFQGFNLLKTvTVYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLFTR-KD-AYPSELSGGQKQRVAIAR 153
Cdd:cd03260 77 LE-LRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEvKDrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-249 |
6.94e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 224.26 E-value: 6.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTT-LSAKElaka 80
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQkIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG1118 75 RR-VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQhvttkkf 240
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA------- 226
|
....*....
gi 446493510 241 vnSAFAAKI 249
Cdd:COG1118 227 --TPFVARF 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-232 |
1.81e-70 |
|
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: 218.88 E-value: 1.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKelakar 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 qkIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03293 75 --RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHgavvESGTVKDIFTNP 232
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA----RPGRIVAEVEVD 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-217 |
3.38e-70 |
|
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: 217.72 E-value: 3.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQ 82
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQGFNL-LKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-234 |
5.84e-70 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 221.53 E-value: 5.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKG-------NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSA 74
Cdd:COG4608 8 LEVRDLKKHFPVRGGlfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 75 KELAKARQKIGMIFQ----GFNLLKTVtvYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLftRKDA---YPSELSGGQK 146
Cdd:COG4608 88 RELRPLRRRMQMVFQdpyaSLNPRMTV--GDIIAEPLRIHGLaSKAERRERVAELLELVGL--RPEHadrYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 147 QRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVK 226
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
....*...
gi 446493510 227 DIFTNPQH 234
Cdd:COG4608 244 ELYARPLH 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-243 |
7.95e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 221.87 E-value: 7.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaka 80
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RqKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG3839 75 R-NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHE----MnviqRICDRVAVMEHGAVVESGTVKDIFTNPQHVT 236
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
....*..
gi 446493510 237 TKKFVNS 243
Cdd:COG3839 230 VAGFIGS 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
3.38e-69 |
|
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: 216.15 E-value: 3.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 R-QKIGMIFQGFNLLKTVTVYENIALPLRLAGISkvEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVE 221
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
4.38e-69 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 217.32 E-value: 4.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKG---NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELA 78
Cdd:TIGR04521 1 IKLKNVS--YIYQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQgF---NLLKTvTVYENIAL-PLRLaGISKVEIEKRVEKYLRIVDL-FTRKDAYPSELSGGQKQRVAIAR 153
Cdd:TIGR04521 79 DLRKKVGLVFQ-FpehQLFEE-TVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-242 |
1.13e-67 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 212.57 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI-IVNSQ-DL-TTLSAKELA 78
Cdd:PRK11124 3 IQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNHfDFsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQGFNLLKTVTVYEN-IALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLllkINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTvKDIFTNPQhv 235
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSI---IRElaETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ-- 232
|
....*..
gi 446493510 236 tTKKFVN 242
Cdd:PRK11124 233 -TEAFKN 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
1.16e-67 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 212.57 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDL---TTLSAKELA 78
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQGFNLLKTVTVYEN-IALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLllkINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTvKDIFTNPQhv 235
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEI---IRElsQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ-- 232
|
....*..
gi 446493510 236 tTKKFVN 242
Cdd:COG4161 233 -TEAFAH 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-245 |
1.92e-67 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 212.59 E-value: 1.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkVFTtkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLL--EKP---TTGNIIVNSQDLttLSAK- 75
Cdd:COG1117 12 IEVRNLN-VYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDI--YDPDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQGFNLLKTvTVYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLFT----RKDAYPSELSGGQKQRVA 150
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
250
....*....|....*
gi 446493510 231 NPQHVTTKKFVNSAF 245
Cdd:COG1117 243 NPKDKRTEDYITGRF 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-243 |
2.56e-67 |
|
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: 220.33 E-value: 2.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKS-TLIRCVNLLEKP---TTGNIIVNSQDLTTLSAKE 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 LAKAR-QKIGMIFQ----GFNLLKTVtvYENIALPLRL-AGISKVEIEKRVEKYLR---IVDLFTRKDAYPSELSGGQKQ 147
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtSLNPLHTI--GKQIAEVLRLhRGLSGAAARARALELLErvgIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKD 227
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250
....*....|....*.
gi 446493510 228 IFTNPQHVTTKKFVNS 243
Cdd:COG4172 244 LFAAPQHPYTRKLLAA 259
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-232 |
3.70e-66 |
|
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: 208.69 E-value: 3.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDL--FTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
8.88e-66 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 208.07 E-value: 8.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkKGNVeALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNsqDLTTLSAKELAKA 80
Cdd:PRK11264 3 AIEVKNLVKKF---HGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 -------RQKIGMIFQGFNLLKTVTVYEN-IALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIA 152
Cdd:PRK11264 77 kglirqlRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 153 RALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
250
....*....|
gi 446493510 233 QHVTTKKFVN 242
Cdd:PRK11264 236 QQPRTRQFLE 245
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
1.53e-65 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 207.15 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTtkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPlRLAGISKV--------EIEKRVEKY-LRIVDLFTRKDAYPSELSGGQKQRVAI 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHG-RLGYKPTWrsllgrfsEEDKERALSaLERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGT 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
5.15e-65 |
|
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: 204.95 E-value: 5.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR 81
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
9.70e-65 |
|
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: 204.78 E-value: 9.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAkelakAR 81
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-----HK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-245 |
8.82e-64 |
|
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: 211.08 E-value: 8.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKG-------NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV-NLLekPTTGNIIVNSQDLTTLS 73
Cdd:COG4172 276 LEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLI--PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 74 AKELAKARQKIGMIFQ----GFN--LlktvTVYENIALPLRL--AGISKVEIEKRVEKYLRIVDLftrkDA-----YPSE 140
Cdd:COG4172 354 RRALRPLRRRMQVVFQdpfgSLSprM----TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGL----DPaarhrYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*
gi 446493510 221 ESGTVKDIFTNPQHVTTKKFVNSAF 245
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
2.61e-63 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 202.28 E-value: 2.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDltTLSAKELAKAR 81
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMN-VIQriCDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-246 |
1.44e-62 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 200.06 E-value: 1.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTL--------- 72
Cdd:TIGR03005 1 VRFSDVTKRF----GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMpgrngplvp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 73 -SAKELAKARQKIGMIFQGFNLLKTVTVYENIAL-PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVA 150
Cdd:TIGR03005 77 aDEKHLRQMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
|
250
....*....|....*.
gi 446493510 231 NPQHVTTKKFVNSAFA 246
Cdd:TIGR03005 237 QPKEERTREFLSKVIA 252
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
3.80e-62 |
|
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: 198.72 E-value: 3.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakA 80
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIA---------------LPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQ 145
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTV 225
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 446493510 226 KDIFTNPQ 233
Cdd:COG0411 238 AEVRADPR 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
6.19e-62 |
|
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: 197.77 E-value: 6.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDlttlSAKELAKA 80
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-245 |
8.20e-61 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 195.57 E-value: 8.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQD----------LTTLSAKELAKARQKIG 85
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 86 MIFQGFNLLKTVTVYENI-ALPLRLAGISKVEIEKRVEKYLRIVDLFTR-KDAYPSELSGGQKQRVAIARALSHEPEVLL 163
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFVNS 243
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
..
gi 446493510 244 AF 245
Cdd:PRK10619 255 SL 256
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
1.12e-59 |
|
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: 190.93 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakar 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-225 |
1.28e-59 |
|
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: 191.04 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsaKELAKAR 81
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTV 225
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-233 |
1.31e-59 |
|
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: 191.78 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakaR 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QkIGMIFQGFNLLKTVTVYENIALPLRLAGI----SKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:cd03296 75 N-VGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
1.43e-59 |
|
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: 189.15 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsaKELAKAR 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIalplrlagiskveiekrvekylrivdlftrkdaypsELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-252 |
3.14e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 191.59 E-value: 3.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKG-----NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKE 76
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 LAkarQKIGMIFQGFN--LLKTVTVYENIALPLRLA-GISKVEIEKRVEKYLRIVDLF-TRKDAYPSELSGGQKQRVAIA 152
Cdd:COG4167 85 RC---KHIRMIFQDPNtsLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 153 RALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
250 260
....*....|....*....|
gi 446493510 233 QHVTTKKFVNSAFAAKIPED 252
Cdd:COG4167 242 QHEVTKRLIESHFGEALTAD 261
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
7.74e-59 |
|
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: 189.57 E-value: 7.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAkaR 81
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKV----------EIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAI 151
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLllararreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
..
gi 446493510 232 PQ 233
Cdd:cd03219 234 PR 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
9.61e-58 |
|
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: 187.56 E-value: 9.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKa 80
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rqKIGMIFQGFNLLKTVTVYENIAL---PLR--LAGISKVEIEKrVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARAL 155
Cdd:COG1120 76 --RIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 156 SHEPEVLLSDEATSALDP----EttdsILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLahqlE----VLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
3.07e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.94 E-value: 3.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGnveaLKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIALPLRLAGisKVEIEKRVEKYLRIVDL---FTRKDAypSELSGGQKQRVAIARALSHE 158
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLppdILDKPV--ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 159 PEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
1.02e-55 |
|
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: 181.16 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTlsakELAKAR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVK 226
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-231 |
4.28e-55 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 181.78 E-value: 4.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKV------FTTKkgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAK 75
Cdd:PRK13637 3 IKIENLTHIymegtpFEKK-----ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 eLAKARQKIGMIFQ--GFNLLKTvTVYENIALPLRLAGISKVEIEKRVEKYLRIV--DLFTRKDAYPSELSGGQKQRVAI 151
Cdd:PRK13637 78 -LSDIRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-241 |
2.06e-54 |
|
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: 178.30 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 14 KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKelakaRQKIGMIFQGFNL 93
Cdd:cd03299 8 KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 94 LKTVTVYENIALPLRLAGISKVEIEKRVE---KYLRIVDLFTRKdayPSELSGGQKQRVAIARALSHEPEVLLSDEATSA 170
Cdd:cd03299 83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLeiaEMLGIDHLLNRK---PETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 171 LDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
1.07e-52 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 174.33 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLL-----EKPTTGNIIVNSQDLTTLSAKE 76
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 LakaRQKIGMIFQGFNLLKTVTVYENIALPLRLAGI--SKVEIEKRVEKYLRIVDLF----TRKDAYPSELSGGQKQRVA 150
Cdd:PRK14247 80 L---RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWdevkDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 446493510 231 NPQHVTTKKFV 241
Cdd:PRK14247 235 NPRHELTEKYV 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
2.07e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 173.02 E-value: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkgNVEALkSTSLQVKKGEVFGIIGYSGAGKSTLIrcvNLL---EKPTTGNIIVNSQDLTTLSAkel 77
Cdd:COG3840 1 MLRLDDLTYRY-----GDFPL-RFDLTIAAGERVAILGPSGAGKSTLL---NLIagfLPPDSGRILWNGQDLTALPP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 akARQKIGMIFQGFNLLKTVTVYENIAL---P-LRLAGISKveieKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIAR 153
Cdd:COG3840 69 --AERPVSMLFQENNLFPHLTVAQNIGLglrPgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-231 |
8.93e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 172.96 E-value: 8.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVE--ALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNsqDLTTLSAKELA 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--GLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMN-VIQriCDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEeAVE--ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-256 |
9.74e-52 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 174.51 E-value: 9.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQ 82
Cdd:PRK15079 19 DIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQG--FNLLKTVTVYENIALPLRL--AGISKVEIEKRVEKYLRIVDLFTRK-DAYPSELSGGQKQRVAIARALSH 157
Cdd:PRK15079 99 DIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTT 237
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
250
....*....|....*....
gi 446493510 238 KKFVNsafAAKIPeDVQKE 256
Cdd:PRK15079 259 KALMS---AVPIP-DPDLE 273
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
1.74e-51 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 171.79 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTT-----KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAK 75
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQ----GFNLLKTVTvyENIALPLR-LAGISKVEIEKRVEKYLRIVDL-FTRKDAYPSELSGGQKQRV 149
Cdd:PRK10419 83 QRKAFRRDIQMVFQdsisAVNPRKTVR--EIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 150 AIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKD 227
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-230 |
2.60e-51 |
|
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: 171.14 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTT-----KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAK 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQ----GFNLLKTVTvyENIALPLR-LAGISKVEIEKRVEKYLRIVDLFTR-KDAYPSELSGGQKQRV 149
Cdd:TIGR02769 82 QRRAFRRDVQLVFQdspsAVNPRMTVR--QIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 150 AIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
.
gi 446493510 230 T 230
Cdd:TIGR02769 240 S 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-263 |
3.23e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 172.84 E-value: 3.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 7 VSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKIGM 86
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 87 IFQ----GFNLLKTVTvyENIALPLRL-AGISKVEIEKRVEKYLRIVDLFTRK-DAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK11308 97 VFQnpygSLNPRKKVG--QILEEPLLInTSLSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKF 240
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQAL 254
|
250 260
....*....|....*....|...
gi 446493510 241 VnSAFAAKIPEDVQKELQTTGEI 263
Cdd:PRK11308 255 L-SATPRLNPDDRRERIKLTGEL 276
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-217 |
4.34e-51 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 169.28 E-value: 4.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTtkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK10908 1 MIRFEHVSKAYL---GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINeEIGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
6.20e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 176.36 E-value: 6.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakA 80
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQK-IGMIFQGFNLLKTVTVYENIAL---PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALS 156
Cdd:COG1129 77 QAAgIAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
7.58e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 173.21 E-value: 7.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKkgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKelakAR 81
Cdd:PRK09452 15 VELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----NR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QkIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:PRK09452 87 H-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-232 |
2.21e-50 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 171.42 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakar 81
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPL----RLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-287 |
2.41e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 169.52 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsakelAKA 80
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIgmifqGF-----NLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARAL 155
Cdd:COG4152 70 RRRI-----GYlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 156 SHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIftNPQHV 235
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI--RRQFG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446493510 236 TTKKFVNSAFAAKIPEDVQ--KELQTTGEIVTLSFIGNSSGEPALAVATKRFQV 287
Cdd:COG4152 222 RNTLRLEADGDAGWLRALPgvTVVEEDGDGAELKLEDGADAQELLRALLARGPV 275
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
2.65e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 167.96 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnsqdltTLSAKELAKA 80
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV--------RLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKT--VTVYENIALPLR-----LAGISKVEIEkRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIAR 153
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGaVVESGTVKDIFT 230
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-264 |
3.38e-50 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 174.44 E-value: 3.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakA 80
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQK-IGMIFQGFNLLKTVTVYENIAL---PLRLAGISKVEIEKRV----EKY-LRiVDLftrkDAYPSELSGGQKQRVAI 151
Cdd:COG3845 78 IALgIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIrelsERYgLD-VDP----DAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVesGTVkdiftN 231
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV--GTV-----D 224
|
250 260 270
....*....|....*....|....*....|...
gi 446493510 232 PQHVTTKKFVNSAFAAKIPEDVQKELQTTGEIV 264
Cdd:COG3845 225 TAETSEEELAELMVGREVLLRVEKAPAEPGEVV 257
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-248 |
6.00e-50 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 171.75 E-value: 6.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 14 KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR-QKIGMIFQGFN 92
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 93 LLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 173 PETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKF-----VNSAFAA 247
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFfrgvdISQVFSA 276
|
.
gi 446493510 248 K 248
Cdd:PRK10070 277 K 277
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
6.61e-50 |
|
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: 177.33 E-value: 6.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---R 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIAL--P----------LRLAGISKvEIEKRVEKYLRIVdlftrkdaypSE----LSGGQ 145
Cdd:COG2274 549 RQIGVVLQDVFLFSG-TIRENITLgdPdatdeeiieaARLAGLHD-FIEALPMGYDTVV----------GEggsnLSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIqRICDRVAVMEHGAVVESGT 224
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGT 692
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-217 |
1.39e-49 |
|
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: 163.71 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIalplrlagiskveiekrvekylrivdlftrkdaypseLSGGQKQRVAIARALSHEPEV 161
Cdd:cd03228 76 KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHG 217
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-223 |
2.82e-49 |
|
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: 164.39 E-value: 2.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVK---KGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAK-ELAKARQKIGMIFQGFNLLKT 96
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 97 VTVYENIALPLRlaGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETT 176
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493510 177 DSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
3.22e-49 |
|
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: 164.46 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDlttlSAKELAKA 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD----VVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKY---LRIVDLFTRKdayPSELSGGQKQRVAIARALSH 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELadrLGMEELLDRR---VGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
7.51e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 165.25 E-value: 7.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVskVFTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtLSAKELAKA 80
Cdd:PRK13639 1 ILETRDL--KYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGF-NLLKTVTVYENIAL-PLRLaGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHE 158
Cdd:PRK13639 77 RKTVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 159 PEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-228 |
9.08e-49 |
|
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: 163.37 E-value: 9.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKArqKIGMIFQGFNLLK 95
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA--GIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 TVTVYENIALPLRLAGISKVeiEKRVEkylRIVDLF----TRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSAL 171
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKR--KARLE---RVYELFprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 172 DPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:cd03224 164 APKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-253 |
1.03e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 167.20 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakar 81
Cdd:PRK11432 7 VVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
250
....*....|....
gi 446493510 242 NSA--FAAKIPEDV 253
Cdd:PRK11432 238 GDAniFPATLSGDY 251
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-207 |
2.77e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 162.29 E-value: 2.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 6 NVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR-QKI 84
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 85 GMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLS 164
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493510 165 DEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRI 207
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-264 |
1.97e-47 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 164.24 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKkgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsakELAKA 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKF 240
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
250 260
....*....|....*....|....
gi 446493510 241 VNSafaAKIPEDVQKELQTTGEIV 264
Cdd:PRK11607 250 IGS---VNVFEGVLKERQEDGLVI 270
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
2.15e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 161.44 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVeALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELaka 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQrICDRVAVMEHGAVVESGTVKDIF 229
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-229 |
3.53e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 160.95 E-value: 3.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQdltTLSAKELAKAR 81
Cdd:PRK13635 6 IRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIF 229
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-219 |
3.60e-47 |
|
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: 158.85 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNsqdlttlsAKELAKARQ 82
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF--------GKPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQGFNLLKT--VTVYENIALPL----RLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALS 156
Cdd:cd03235 69 RIGYVPQRRSIDRDfpISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
5.79e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 159.64 E-value: 5.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaka 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rqkiGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITH 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
5.84e-47 |
|
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: 158.99 E-value: 5.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvftTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAka 80
Cdd:COG0410 3 MLEVENLH----AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGiSKVEIEKRVEkylRIVDLF----TRKDAYPSELSGGQKQRVAIARALS 156
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLE---RVYELFprlkERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-217 |
8.44e-47 |
|
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: 155.87 E-value: 8.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQ 82
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQgfnllktvtvyenialplrlagiskveiekrvekylrivdlftrkdaypseLSGGQKQRVAIARALSHEPEVL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 163 LSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-223 |
1.06e-46 |
|
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: 156.44 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKvfttKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKarq 82
Cdd:cd03214 1 EVENLSV----GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQgfnllktvtvyeniALplrlagiskveiekrveKYLRIVDLftrKDAYPSELSGGQKQRVAIARALSHEPEVL 162
Cdd:cd03214 74 KIAYVPQ--------------AL-----------------ELLGLAHL---ADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 163 LSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-229 |
3.02e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 158.86 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 19 EALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtLSAKELAKARQKIGMIFQG-FNLLKTV 97
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 98 TVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTD 177
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493510 178 SILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-234 |
5.96e-46 |
|
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: 156.09 E-value: 5.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakarqkigMIFQGFNLLKTVTVY 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIALPLR--LAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDS 178
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 179 ILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI-FTNPQH 234
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-245 |
6.48e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 156.86 E-value: 6.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkVFTTKKgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLL-----EKPTTGNIIVNSQDLTTLSAk 75
Cdd:PRK14239 5 ILQVSDLS-VYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQGFNLLKtVTVYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLFTR-KDAYPSE---LSGGQKQRVA 150
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIWDEvKDRLHDSalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
250
....*....|....*
gi 446493510 231 NPQHVTTKKFVNSAF 245
Cdd:PRK14239 237 NPKHKETEDYISGKF 251
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-245 |
8.43e-46 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 156.87 E-value: 8.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKG-----NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTlsaK 75
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQ--GFNLLKTVTVYENIALPLRL-AGISKVEIEKRVEKYLRIVDLFT-RKDAYPSELSGGQKQRVAI 151
Cdd:PRK15112 81 DYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|....
gi 446493510 232 PQHVTTKKFVNSAF 245
Cdd:PRK15112 241 PLHELTKRLIAGHF 254
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-266 |
2.51e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 156.33 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 20 ALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLT-TLSAKELAKARQKIGMIFQgF--NLLKT 96
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 97 VTVYENIAL-PLRLaGISKVEIEKRVEKYLRIV----DLFTRKdayPSELSGGQKQRVAIARALSHEPEVLLSDEATSAL 171
Cdd:PRK13634 101 ETVEKDICFgPMNF-GVSEEDAKQKAREMIELVglpeELLARS---PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 172 DPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVT--------TKKF--- 240
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEaigldlpeTVKFkra 256
|
250 260
....*....|....*....|....*.
gi 446493510 241 VNSAFAAKIPEDVQKELQTTGEIVTL 266
Cdd:PRK13634 257 LEEKFGISFPKPCLTLEELAHEVVQL 282
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
2.56e-45 |
|
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: 152.20 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElAKaR 81
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-AR-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQgfnllktvtvyenialplrlagiskveiekrvekylrivdlftrkdaypseLSGGQKQRVAIARALSHEPEV 161
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
3.11e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.64 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLircVNLLEK---PTTGNIIVNSQDLTTLSAKELa 78
Cdd:COG1132 340 IEFENVS--FSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLRfydPTSGRILIDGVDIRDLTLESL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYENIAL--P----------LRLAGISKVeIEKRVEKYlrivdlftrkDAYPSE----LS 142
Cdd:COG1132 413 --RRQIGVVPQDTFLFSG-TIRENIRYgrPdatdeeveeaAKAAQAHEF-IEALPDGY----------DTVVGErgvnLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 143 GGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVES 222
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
..
gi 446493510 223 GT 224
Cdd:COG1132 556 GT 557
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-244 |
3.50e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 155.00 E-value: 3.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLL-----EKPTTGNIIVNSQDLTTLSAKELaKARQKIGMIFQG 90
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI-EVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 91 FNLLKTVTVYENIALPLRLAGI--SKVEIEKRVEKYLRIVDLF----TRKDAYPSELSGGQKQRVAIARALSHEPEVLLS 164
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 165 DEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFVNSA 244
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
3.59e-45 |
|
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: 153.50 E-value: 3.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnveALKSTSLQVKKGeVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsaKELAKAR 81
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-255 |
4.58e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 155.15 E-value: 4.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVnsqDLTTLSAKELAKA 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---DGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMN-VIQriCDRVAVMEHGAVVESGTVKDIFTNPQHVTTK 238
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
250
....*....|....*..
gi 446493510 239 KfVNSAFAAKIPEDVQK 255
Cdd:PRK13632 240 K-IDSPFIYKLSKKLKG 255
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-223 |
4.39e-44 |
|
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: 150.89 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLsakelakAR 81
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-------AR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
5.44e-44 |
|
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: 151.15 E-value: 5.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTlirCVNLLEK---PTTGNIIVNSQDLTTLSAKELa 78
Cdd:cd03249 1 IEFKNVSFRYPSRP-DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLNLRWL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYENIALPLRLAgiSKVEIE---KRVEKYLRIVDL----FTRKDAYPSELSGGQKQRVAI 151
Cdd:cd03249 76 --RSQIGLVSQEPVLFDG-TIAENIRYGKPDA--TDEEVEeaaKKANIHDFIMSLpdgyDTLVGERGSQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSI---LDLLLKineeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVqeaLDRAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-241 |
7.35e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 159.64 E-value: 7.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 8 SKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKIGMI 87
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 88 FQG--FNLLKTVTVYENIALPLRLAGISKVE-IEKRVEKYLRIVDLFTRKD-AYPSELSGGQKQRVAIARALSHEPEVLL 163
Cdd:PRK10261 407 FQDpyASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-223 |
1.03e-43 |
|
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: 149.95 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAkelakARQKIGMIFQGFNLLKTVTVYENIA 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-----ADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 105 L---P-LRLagisKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSIL 180
Cdd:cd03298 93 LglsPgLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493510 181 DLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
1.88e-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: 147.02 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsAKELAKARQKIGMIFQGFNLLKTVTVY 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT---DDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 101 ENIALPLRLAGISKVEIEKRVEKYL---RIVDLFTRK-DAYPSELSGGQKQRVAIARALSHEPEVLLSDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALeklGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-232 |
1.34e-42 |
|
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: 151.02 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTlSAKE--LAKARQKIGMIFQGFNLLKTVTVYEN 102
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGifLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 103 IalplrLAGISKVEIEKRVEKYLRIVDLF------TRkdaYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETT 176
Cdd:COG4148 98 L-----LYGRKRAPRAERRISFDEVVELLgighllDR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 177 DSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-235 |
3.18e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 147.97 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNV---EALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSA-KEL 77
Cdd:PRK13649 3 INLQNVS--YTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKARQKIGMIFQgF--NLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIV----DLFTRKdayPSELSGGQKQRVAI 151
Cdd:PRK13649 81 KQIRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVgiseSLFEKN---PFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFtn 231
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF-- 233
|
....
gi 446493510 232 pQHV 235
Cdd:PRK13649 234 -QDV 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-234 |
4.91e-42 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 149.10 E-value: 4.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKS-TLIRCVNLLEKP--TTGNIIVNSQDLTTLSAKEL 77
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKAR-QKIGMIFQG--FNLLKTVTVYENIALPLRL-AGISKVEIekrVEKYLRIVDLFTRKDA------YPSELSGGQKQ 147
Cdd:PRK09473 92 NKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEA---FEESVRMLDAVKMPEArkrmkmYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKD 227
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
....*..
gi 446493510 228 IFTNPQH 234
Cdd:PRK09473 249 VFYQPSH 255
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
7.95e-42 |
|
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: 144.67 E-value: 7.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDlttlsAKELAKAR 81
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-----YQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKveieKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
1.05e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 153.73 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQK-IGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRiCDRVAVMEHGAVV 220
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
2.44e-41 |
|
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: 144.11 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFT-----TKKgnVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV--NLLekPTTGNIIVNSQ----DL 69
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKR--LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVRHDggwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 70 TTLSAKELAKARQK-IGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRK-DAYPSELSGGQKQ 147
Cdd:COG4778 80 AQASPREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGA 218
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
2.94e-41 |
|
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: 151.45 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:COG4988 337 IELEDVS--FSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMI------FQGfnllktvTVYENIALPLRLAGiskveiEKRVEKYLRIVDLFTRKDAYP-----------SELSGG 144
Cdd:COG4988 411 RQIAWVpqnpylFAG-------TIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 145 QKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIqRICDRVAVMEHGAVVESGT 224
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGT 554
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-228 |
3.51e-41 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 144.07 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVF------------------TTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 63 IVNSQdLTTLsakeLAkarqkIGMIFQGfNLlktvTVYENIALPLRLAGISKVEIEKRVEKylrIVDlFtrkdaypSEL- 141
Cdd:COG1134 84 EVNGR-VSAL----LE-----LGAGFHP-EL----TGRENIYLNGRLLGLSRKEIDEKFDE---IVE-F-------AELg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 142 ----------SGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRV 211
Cdd:COG1134 138 dfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|....*..
gi 446493510 212 AVMEHGAVVESGTVKDI 228
Cdd:COG1134 217 IWLEKGRLVMDGDPEEV 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
5.24e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 144.51 E-value: 5.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsAKELAKA 80
Cdd:PRK13648 7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNPQHVTT 237
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
8.61e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 144.18 E-value: 8.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELaka 80
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFN-LLKTVTVYENIAL-PLRLaGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHE 158
Cdd:PRK13652 77 RKFVGLVFQNPDdQIFSPTVEQDIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 159 PEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-228 |
2.23e-40 |
|
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: 148.41 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVF-TTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQ----DLTTLSAK 75
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQGFNLLKTVTVYEN------IALPLRLAGISKVEIEKRV---EKYLRIVdlftrKDAYPSELSGGQK 146
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITLKMVgfdEEKAEEI-----LDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 147 QRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVK 226
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 446493510 227 DI 228
Cdd:TIGR03269 514 EI 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-233 |
5.52e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 142.25 E-value: 5.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKAR 81
Cdd:PRK13640 6 VEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQrICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
7.79e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 141.34 E-value: 7.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLL------EKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQGFNLL 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 95 KTVTVYENIALPLRLAGIS-KVEIEKRVEKYLRIVDL----FTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATS 169
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 170 ALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-241 |
7.90e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 143.07 E-value: 7.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGN-VEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI----IVNSQDLTTLSA- 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENeLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 75 --------KELAKARQKIGMIFQ--GFNLLKTvTVYENIAL-PLRLaGISKVEIEKRVEKYLRIVDL-FTRKDAYPSELS 142
Cdd:PRK13631 101 tnpyskkiKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 143 GGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVES 222
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|....*....
gi 446493510 223 GTVKDIFTNPQHVTTKKFV 241
Cdd:PRK13631 258 GTPYEIFTDQHIINSTSIQ 276
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-241 |
1.19e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 143.63 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsakELAKARQK 83
Cdd:PRK11000 6 LRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLL 163
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHvttkKFV 241
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN----RFV 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-210 |
1.83e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 139.14 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 R-QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDR 210
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDR 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-243 |
2.98e-39 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 145.62 E-value: 2.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKS-TLIRCVNLLEKP----TTGNIIVNSQDLTTLSAK 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKAR-QKIGMIFQ----GFNLLKTV--TVYENIAL-------PLRLAGISKVEiekRVEkylrIVDLFTRKDAYPSEL 141
Cdd:PRK15134 85 TLRGVRgNKIAMIFQepmvSLNPLHTLekQLYEVLSLhrgmrreAARGEILNCLD---RVG----IRQAAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 142 SGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVE 221
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|..
gi 446493510 222 SGTVKDIFTNPQHVTTKKFVNS 243
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNS 259
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
5.38e-39 |
|
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: 138.39 E-value: 5.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03252 1 ITFEHVR--FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGfNLLKTVTVYENIAL-----PL-------RLAGISKVeIEKRVEKYLRIVDlftrkdAYPSELSGGQKQRV 149
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNIALadpgmSMervieaaKLAGAHDF-ISELPEGYDTIVG------EQGAGLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 150 AIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-239 |
5.81e-39 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 144.85 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKG-------NVEALKSTSLQVKKGEVFGIIGYSGAGKST----LIRCVNllekpTTGNIIVNSQDL 69
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 70 TTLSAKELAKARQKIGMIFQGFN--LLKTVTVYENIALPLRL--AGISKVEIEKRVEKYLRIV--DLFTRKdAYPSELSG 143
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVglDPETRH-RYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 144 GQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
250
....*....|....*.
gi 446493510 224 TVKDIFTNPQHVTTKK 239
Cdd:PRK15134 509 DCERVFAAPQQEYTRQ 524
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-220 |
6.73e-39 |
|
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: 137.00 E-value: 6.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSkvFTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLttlSAKELAKArq 82
Cdd:cd03226 1 RIENIS--FSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKS-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 kIGMIFQ--GFNLLkTVTVYENIALPLRLAGiskvEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:cd03226 73 -IGYVMQdvDYQLF-TDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-232 |
7.21e-39 |
|
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: 141.02 E-value: 7.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAK-ELAKARQKIGMIFQGFNLLKTVTVYENI 103
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 104 alplrLAGISKVEIEKRVEKYLRIVDLFTRK---DAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSIL 180
Cdd:TIGR02142 97 -----RYGMKRARPSERRISFERVIELLGIGhllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493510 181 DLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
7.37e-39 |
|
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: 144.91 E-value: 7.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLircVNLL---EKPTTGNIIVNSQDLTTLSAKELa 78
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL---LALLlrfLDPQSGSITLGGVDLRDLDEDDL- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYENialpLRLA--GISkveiEKRVEKYLRIVDLFTRKDAYP-----------SELSGGQ 145
Cdd:COG4987 408 --RRRIAVVPQRPHLFDT-TLREN----LRLArpDAT----DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGT 552
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-251 |
8.70e-39 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 145.38 E-value: 8.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKS-TLIRCVNLLEKP----TTGNIIV---NSQ--DLT 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLrrrSRQviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 71 TLSAKELAKAR-QKIGMIFQG--FNLLKTVTVYENIALPLRL-AGISKVEI---EKRVEKYLRIVDLFTRKDAYPSELSG 143
Cdd:PRK10261 92 EQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 144 GQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....*...
gi 446493510 224 TVKDIFTNPQHVTTKkfvnsAFAAKIPE 251
Cdd:PRK10261 252 SVEQIFHAPQHPYTR-----ALLAAVPQ 274
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-244 |
8.83e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 140.43 E-value: 8.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRC-VNLLEKpttgNIIV-------NSQDLTTL 72
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKD----NWHVtadrfrwNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 73 SAKELAK-ARQKIGMIFQ--GFNLLKTVTVYENI--ALPlrlAGISKVEIEKR-VEKYLRIVDLFTR---KD------AY 137
Cdd:COG4170 79 SPRERRKiIGREIAMIFQepSSCLDPSAKIGDQLieAIP---SWTFKGKWWQRfKWRKKRAIELLHRvgiKDhkdimnSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 138 PSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCG 235
|
250 260
....*....|....*....|....*..
gi 446493510 218 AVVESGTVKDIFTNPQHVTTKKFVNSA 244
Cdd:COG4170 236 QTVESGPTEQILKSPHHPYTKALLRSM 262
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
1.43e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 138.20 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTkkgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSakELAKA 80
Cdd:PRK13644 1 MIRLENVSYSYPD---GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNL-LKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK13644 76 RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQrICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
1.72e-38 |
|
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: 136.98 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLircVNLLEK---PTTGNIIVNSQDLTTLSAKELa 78
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPRfydVDSGRILIDGHDVRDYTLASL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYENIALPLRLAGiskveiEKRVEKYLRIVDL--FTRK--DAYPSE-------LSGGQKQ 147
Cdd:cd03251 75 --RRQIGLVSQDVFLFND-TVAENIAYGRPGAT------REEVEEAARAANAheFIMElpEGYDTVigergvkLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSI---LDLLLKineeiGITILLITHEMNVIQRIcDRVAVMEHGAVVESGT 224
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVqaaLERLMK-----NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.80e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 139.07 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKG-NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI---IVNSQDLTTLSAKEL 77
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKA------------------RQKIGMIFQ--GFNLLKTvTVYENIALPLRLAGISKVEIEKRVEKYLRIVDL---FTRK 134
Cdd:PRK13651 83 VLEklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdesYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 135 DayPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVM 214
Cdd:PRK13651 162 S--PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*..
gi 446493510 215 EHGAVVESGTVKDIFTN 231
Cdd:PRK13651 239 KDGKIIKDGDTYDILSD 255
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-287 |
2.30e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 139.07 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGN-----------------VEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNII 63
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 64 VNSQDlttlSAKELAKARQKIGMIF-------------QGFNLLKTVtvYEnialplrlagISKVEIEKRVEKYLRIVDL 130
Cdd:COG4586 81 VLGYV----PFKRRKEFARRIGVVFgqrsqlwwdlpaiDSFRLLKAI--YR----------IPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 131 ------FTRKdaypseLSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVI 204
Cdd:COG4586 145 gelldtPVRQ------LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 205 QRICDRVAVMEHGAVVESGTVKDIFTN--PQHVTTKKFVNSAFAAKIPEDVqKELQTTGEIVTLSFIGNSSGEPALAVAT 282
Cdd:COG4586 219 EALCDRVIVIDHGRIIYDGSLEELKERfgPYKTIVLELAEPVPPLELPRGG-EVIEREGNRVRLEVDPRESLAEVLARLL 297
|
....*
gi 446493510 283 KRFQV 287
Cdd:COG4586 298 ARYPV 302
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-243 |
2.97e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 139.59 E-value: 2.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTtkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaka 80
Cdd:PRK11650 3 GLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIV---DLFTRKdayPSELSGGQKQRVAIARALSH 157
Cdd:PRK11650 76 -RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILelePLLDRK---PRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 158 EPEVLLSDEATSALDP--------EttdsildlLLKINEEIGITILLITHE----MNviqrICDRVAVMEHGAVVESGTV 225
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAklrvqmrlE--------IQRLHRRLKTTSLYVTHDqveaMT----LADRVVVMNGGVAEQIGTP 219
|
250
....*....|....*...
gi 446493510 226 KDIFTNPqhVTTkkFVNS 243
Cdd:PRK11650 220 VEVYEKP--AST--FVAS 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-255 |
3.27e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 137.65 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFT-----TKKGnveaLKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTT-LSAK 75
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKG----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQgF--NLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTR-KDAYPSELSGGQKQRVAIA 152
Cdd:PRK13641 79 NLKKLRKKVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 153 RALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
250 260
....*....|....*....|...
gi 446493510 233 QHVtTKKFVNSAFAAKIPEDVQK 255
Cdd:PRK13641 237 EWL-KKHYLDEPATSRFASKLEK 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-236 |
1.21e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 136.29 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKG-NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTT--LSAKELA 78
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQ--GFNLLKTvTVYENIAL-PLRLaGISKVEIEKRVEKYLRIVDL---FTRKDayPSELSGGQKQRVAIA 152
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLpedYVKRS--PFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 153 RALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ 242
|
....
gi 446493510 233 QHVT 236
Cdd:PRK13645 243 ELLT 246
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-224 |
1.36e-37 |
|
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: 134.28 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03254 3 IEFENVN--FSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIalplRLAG-ISKVEIEKRVEKYLRIvDLFTRK-----DAYPSE----LSGGQKQRVAI 151
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENI----RLGRpNATDEEVIEAAKEAGA-HDFIMKlpngyDTVLGEnggnLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-245 |
2.30e-37 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 134.91 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEK--PT---TGNIIVNSQDLTTlSAKELAKARQKIGMIFQG 90
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 91 FNLLKTvTVYENIALPLRLAGIsKVEIEKRVEKYLRIVDLFTR-KDAYP---SELSGGQKQRVAIARALSHEPEVLLSDE 166
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEvKDKLKqsgLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 167 ATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVM---------EHGAVVESGTVKDIFTNPQHVTT 237
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255
|
....*...
gi 446493510 238 KKFVNSAF 245
Cdd:PRK14243 256 RDYVSGRF 263
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
4.96e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 133.17 E-value: 4.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAkelakARQKIGMIFQGFNLLKTVTVYENIA 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-----SRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 105 L---P-LRLAGISKVEIEKRVEKyLRIVDLFTRkdaYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSIL 180
Cdd:PRK10771 94 LglnPgLKLNAAQREKLHAIARQ-MGIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493510 181 DLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
5.03e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.09 E-value: 5.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:PRK13647 5 IEVEDLH--FRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQG-FNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTvKDIFTNPQHV 235
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLLTDEDIV 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
5.45e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.65 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSqdlttlsaKELAKARQK 83
Cdd:PRK11247 15 LNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT--------APLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYENIALPLRlaGiskvEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLL 163
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGLK--G----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
5.90e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 135.73 E-value: 5.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnsqdlTTLSAKELAK-- 79
Cdd:PRK13536 42 IDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-------TVLGVPVPARar 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 -ARQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHE 158
Cdd:PRK13536 111 lARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 159 PEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
1.20e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 132.08 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttKKGNVeaLKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaKA 80
Cdd:COG1137 3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK--RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGM------IFQGfnllktVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARA 154
Cdd:COG1137 77 RLGIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 155 LSHEPEVLLSDEATSALDPETTDSILDLLLKINEE-IGItilLIT-HemNV--IQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGV---LITdH--NVreTLGICDRAYIISEGKVLAEGTPEEILN 225
|
...
gi 446493510 231 NPQ 233
Cdd:COG1137 226 NPL 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-251 |
1.32e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 134.48 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKS-TLIRCVNLLEKP---TTGNIIVNSQDLTTLSAKE 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 lakARQKIG----MIFQ------------GFNLLKTVTVYEnialplrlaGISKVEIEKRVEKYLRIV---DLFTRKDAY 137
Cdd:PRK11022 83 ---RRNLVGaevaMIFQdpmtslnpcytvGFQIMEAIKVHQ---------GGNKKTRRQRAIDLLNQVgipDPASRLDVY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 138 PSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
250 260 270
....*....|....*....|....*....|....
gi 446493510 218 AVVESGTVKDIFTNPQHVTTKkfvnsAFAAKIPE 251
Cdd:PRK11022 231 QVVETGKAHDIFRAPRHPYTQ-----ALLRALPE 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-241 |
1.82e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 132.47 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLL-----EKPTTGNIIVNSQDLTTLSAKe 76
Cdd:PRK14258 8 IKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 LAKARQKIGMIFQGFNLLKtVTVYENIALPLRLAGI-SKVEIEKRVEKYLRIVDLF--TRKDAYPS--ELSGGQKQRVAI 151
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWdeIKHKIHKSalDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEH-----GAVVESGTVK 226
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
250
....*....|....*
gi 446493510 227 DIFTNPQHVTTKKFV 241
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-228 |
3.01e-36 |
|
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: 130.72 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKArqKIGMIFQGFNLLK 95
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARA--GIAYVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 TVTVYENIALPLRLAGISKVEIEKRvekylrIVDLF-------TRKDAypsELSGGQKQRVAIARALSHEPEVLLSDEAT 168
Cdd:TIGR03410 89 RLTVEENLLTGLAALPRRSRKIPDE------IYELFpvlkemlGRRGG---DLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 169 SALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-236 |
3.10e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 132.60 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGN---VEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNsqDLTTLSA---K 75
Cdd:PRK13646 3 IRFDNVS--YTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD--DITITHKtkdK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 76 ELAKARQKIGMIFQgF--NLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLriVDL-FTRK--DAYPSELSGGQKQRVA 150
Cdd:PRK13646 79 YIRPVRKRIGMVFQ-FpeSQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLgFSRDvmSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
....*.
gi 446493510 231 NPQHVT 236
Cdd:PRK13646 236 DKKKLA 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-234 |
1.13e-35 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 130.66 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvFTtkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK11831 7 LVDMRGVS--FT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLR-LAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQH 234
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
3.56e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 130.31 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKelakAR 81
Cdd:PRK13537 8 IDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH----AR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-224 |
4.38e-35 |
|
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: 134.16 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLE--KPTTGNIIVN-------------- 65
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 66 ----------------SQDLTTLSAKELAKARQKIGMIFQ-GFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIV 128
Cdd:TIGR03269 77 kvgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 129 DLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*.
gi 446493510 209 DRVAVMEHGAVVESGT 224
Cdd:TIGR03269 237 DKAIWLENGEIKEEGT 252
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
4.59e-35 |
|
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: 127.32 E-value: 4.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03245 3 IEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIALPLRLAgiSKVEIEKRVEkyLRIVDLFTRKDAYPSE---------LSGGQKQRVAIA 152
Cdd:cd03245 78 RNIGYVPQDVTLFYG-TLRDNITLGAPLA--DDERILRAAE--LAGVTDFVNKHPNGLDlqigergrgLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 153 RALSHEPEVLLSDEATSALDPETTDSILDlllKINEEI-GITILLITHEMNVIQrICDRVAVMEHGAVVESG 223
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKE---RLRQLLgDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
4.74e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 135.08 E-value: 4.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLsakELAKAR 81
Cdd:TIGR03797 452 IEVDRVT--FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLkTVTVYENIA----LPL-------RLAGISKvEIEKRVekylriVDLFTRKDAYPSELSGGQKQRVA 150
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAggapLTLdeaweaaRMAGLAE-DIRAMP------MGMHTVISEGGGTLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINeeigITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
4.97e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKvfttKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRcvnLLE---KPTTGNIIVNSQDLTTLSAKEL 77
Cdd:PRK13548 2 MLEARNLSV----RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLR---ALSgelSPDSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKARqkiGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDL--FTRKDaYPsELSGGQKQRVAIARAL 155
Cdd:PRK13548 75 ARRR---AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLahLAGRD-YP-QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 156 ------SHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:PRK13548 150 aqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
.
gi 446493510 230 T 230
Cdd:PRK13548 230 T 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-229 |
5.04e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.47 E-value: 5.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 20 ALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSA-KELAKARQKIGMIFQ-GFNLLKTV 97
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIKPVRKKVGVVFQfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 98 TVYENIALPLRLAGISKVEIEKRVEKYLRIVDL---FTRKDayPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPE 174
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLadeFWEKS--PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 175 TTDSILDLLLKINeEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
5.22e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.66 E-value: 5.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGN-VEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAK 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 arqKIGMIFQgfNLLK----TVTVYENIAL--------PLRLaGISKVEIEkRVEKYLRIVD--LFTRKDAYPSELSGGQ 145
Cdd:COG1101 81 ---YIGRVFQ--DPMMgtapSMTIEENLALayrrgkrrGLRR-GLTKKRRE-LFRELLATLGlgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-232 |
7.92e-35 |
|
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: 127.27 E-value: 7.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaKAR 81
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK--RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 162 LLSDEATSALDPEttdSILDL--LLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:cd03218 155 LLLDEPFAGVDPI---AVQDIqkIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
9.37e-35 |
|
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: 126.96 E-value: 9.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIALPlRLaGISKVEIEkRVEKYLRIVDLFTR-KDAYPSE-------LSGGQKQRVAIAR 153
Cdd:cd03253 75 RAIGVVPQDTVLFND-TIGYNIRYG-RP-DATDEEVI-EAAKAAQIHDKIMRfPDGYDTIvgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
1.08e-34 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 132.60 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rqKIGMIFQGFNLLKTVTVYENI---ALPLR-LAGISKV---EIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIAR 153
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLyigRHLTKkVCGVNIIdwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-261 |
1.10e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 128.29 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 14 KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsAKELAKARQKIGMIFQG-FN 92
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENVWNLRRKIGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 93 LLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PRK13642 93 QFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 173 PETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTnpqhvTTKKFVNSAFAAKIPED 252
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA-----TSEDMVEIGLDVPFSSN 246
|
....*....
gi 446493510 253 VQKELQTTG 261
Cdd:PRK13642 247 LMKDLRKNG 255
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-232 |
1.55e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.03 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAka 80
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLR-------LAGISKVEIEKRVEK--------YLRIVDLFTRKDAYPSELSGGQ 145
Cdd:PRK11300 79 RMGVVRTFQHVRLFREMTVIENLLVAQHqqlktglFSGLLKTPAFRRAESealdraatWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTV 225
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
....*..
gi 446493510 226 KDIFTNP 232
Cdd:PRK11300 239 EEIRNNP 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-223 |
2.04e-34 |
|
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: 126.29 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTT-----------------KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIV 64
Cdd:cd03267 1 IEVSNLSKSYRVyskepgligslkslfkrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 65 NSQdlttLSAKELAKARQKIGMIF-QGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSG 143
Cdd:cd03267 81 AGL----VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 144 GQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
2.13e-34 |
|
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: 124.25 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIalplrlagiskveiekrvekylrivdlftrkdaypseLSGGQKQRVAIARALSHEPEV 161
Cdd:cd03246 76 DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRiCDRVAVMEHGAV 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
4.11e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.00 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvFTTkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG4559 1 MLEAENLS--VRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 R----QKIGMIFqGFnllktvTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKD-AYPsELSGGQKQRVAIARAL 155
Cdd:COG4559 77 RavlpQHSSLAF-PF------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 156 -------SHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:COG4559 149 aqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
....
gi 446493510 229 FTNP 232
Cdd:COG4559 228 LTDE 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-241 |
5.46e-34 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 125.58 E-value: 5.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKStlIRCVNLLE------KPTTGNIIVnsqDLTTLSAKELaKARqKIGMIFQ----GFNLL 94
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLL---DGKPVAPCAL-RGR-KIATIMQnprsAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 95 KTVTVY-----ENIALPLRLAGISKVEIEKRVEKYLRIVDLftrkdaYPSELSGGQKQRVAIARALSHEPEVLLSDEATS 169
Cdd:PRK10418 96 HTMHTHaretcLALGKPADDATLTAALEAVGLENAARVLKL------YPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 170 ALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
1.58e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 124.74 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLekpTTGNIIVNSQ-DLTTLS------ 73
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHiELLGRTvqregr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 74 -AKELAKARQKIGMIFQGFNLLKTVTVYENIAL------PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYP--SELSGG 144
Cdd:PRK09984 77 lARDIRKSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQrvSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 145 QKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGT 224
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
2.34e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.65 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:COG4604 1 MIEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 ----RQKigmifQGFNLLktVTVYENIAL---PL---RLagisKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVA 150
Cdd:COG4604 77 lailRQE-----NHINSR--LTVRELVAFgrfPYskgRL----TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-228 |
7.66e-33 |
|
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: 128.30 E-value: 7.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLircVNLLEK---PTTGNIIVNSQDLTTLSakeLA 78
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYT---LA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQGFNLLKTvTVYENIALPlRLAGISKVEIEKRVE-KYLR-IVD-----LFTRKDAYPSELSGGQKQRVAI 151
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAaAYAQdFVDklplgLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDI 228
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-223 |
2.10e-32 |
|
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: 120.33 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKK------------------GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNII 63
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 64 VNSQD--LTTLSAkelakarqkigmifqGFNllKTVTVYENIALPLRLAGISKVEIEKRVEkylRIVDlFTRKDAY---P 138
Cdd:cd03220 81 VRGRVssLLGLGG---------------GFN--PELTGRENIYLNGRLLGLSRKEIDEKID---EIIE-FSELGDFidlP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 139 -SELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd03220 140 vKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKG 218
|
....*.
gi 446493510 218 AVVESG 223
Cdd:cd03220 219 KIRFDG 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-201 |
4.18e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.57 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnsqdltTLSAKELAKA 80
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI--------TLDGKPVEGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK11248 69 GAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEM 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-202 |
5.37e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.12 E-value: 5.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNvskvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVN-LLEKP--TTGNIIVNSQDLTTLSAkel 77
Cdd:COG4136 1 MLSLEN----LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALPA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 akARQKIGMIFQGFNLLKTVTVYENIALPLRlAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:COG4136 74 --EQRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMN 202
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-245 |
9.69e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 9.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKarqKIGMIFQGFNLLK 95
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR---RLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 TVTVYENIA------LPL--RLAGISKVEIEKRVEKyLRIVDLFTRKdayPSELSGGQKQRVAIARALSHEPEVLLSDEA 167
Cdd:PRK11231 90 GITVRELVAygrspwLSLwgRLSAEDNARVNQAMEQ-TRINHLADRR---LTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 168 TSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTvkdiftnPQHVTTKKFVNSAF 245
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT-------PEEVMTPGLLRTVF 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
1.57e-31 |
|
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: 116.76 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 20 ALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA--------RQKIGmIFQGF 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG-LVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 92 nllktvTVYENIALPLRLagiskveiekrvekylrivdlftrkdaypselSGGQKQRVAIARALSHEPEVLLSDEATSAL 171
Cdd:cd03215 94 ------SVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493510 172 DPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:cd03215 136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-233 |
1.86e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 121.13 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVK-----KGeVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKE-LAKARQKIGMIFQGFNLL 94
Cdd:PRK11144 10 LGDLCLTVNltlpaQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 95 KTVTVYENIalplrLAGISKveieKRVEKYLRIVDLFTRK---DAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSAL 171
Cdd:PRK11144 89 PHYKVRGNL-----RYGMAK----SMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 172 DPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-232 |
2.02e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 124.83 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTlirCVNLLE---KPTTGNIIVNSQDLTTLSAKELa 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVPLVQYDHHYL- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGfNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLF-----TRKDAYPSELSGGQKQRVAIAR 153
Cdd:TIGR00958 554 --HRQVALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpngydTEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 154 ALSHEPEVLLSDEATSALDPEttdsILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-224 |
2.59e-31 |
|
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: 124.16 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRcvnLLEK---PTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQgfnllKTV 97
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDIRDVTQASL---RAAIGIVPQ-----DTV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 98 ----TVYENIALPlRlAGISKVEIEkRVEKYLRIVDLFTR-KDAYPSE-------LSGGQKQRVAIARALSHEPEVLLSD 165
Cdd:COG5265 443 lfndTIAYNIAYG-R-PDASEEEVE-AAARAAQIHDFIESlPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 166 EATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:COG5265 520 EATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-243 |
8.54e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 119.14 E-value: 8.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKP----TTGNIIVNSQDLTTLSAKE 76
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 LAK-ARQKIGMIFQ------------GFNLLKTVTVYENIALPLRLAGISKveieKRVEKYLRIVDLFTRKDA---YPSE 140
Cdd:PRK15093 83 RRKlVGHNVSMIFQepqscldpservGRQLMQNIPGWTYKGRWWQRFGWRK----RRAIELLHRVGIKDHKDAmrsFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260
....*....|....*....|...
gi 446493510 221 ESGTVKDIFTNPQHVTTKKFVNS 243
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRA 261
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-247 |
1.24e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 116.95 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 5 KNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKI 84
Cdd:PRK11701 10 RGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 85 ------GMIFQ----GfnLLKTVTVYENIALPLRLAG--------------ISKVEIEKrvekyLRIVDLftrkdayPSE 140
Cdd:PRK11701 86 llrtewGFVHQhprdG--LRMQVSAGGNIGERLMAVGarhygdiratagdwLERVEIDA-----ARIDDL-------PTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|....*..
gi 446493510 221 ESGTVKDIFTNPQHVTTKKFVNSAFAA 247
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSSVLQV 258
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-224 |
1.74e-30 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 122.16 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI-----IVNSQDLTTlsake 76
Cdd:NF033858 267 IEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT----- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 lakaRQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALS 156
Cdd:NF033858 338 ----RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDT 480
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.83e-30 |
|
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: 121.24 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---R 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIALPLRLAgiSKVEIEKRVEK--YLRIVD-----LFTRKDAYPSELSGGQKQRVAIARA 154
Cdd:TIGR02857 396 DQIAWVPQHPFLFAG-TIAENIRLARPDA--SDAEIREALERagLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 155 LSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVM 214
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
2.85e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 120.84 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIrcvNLLEK---PTTGNIIVNSQDLTTLSAKELa 78
Cdd:PRK13657 335 VEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRvfdPQSGRILIDGTDIRTVTRASL- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYENIAL--------PLRLAgISKVE----IEKRVEKYLRIVDLFTRKdaypseLSGGQK 146
Cdd:PRK13657 408 --RRNIAVVFQDAGLFNR-SIEDNIRVgrpdatdeEMRAA-AERAQahdfIERKPDGYDTVVGERGRQ------LSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 147 QRVAIARALSHEPEVLLSDEATSALDPETTDSI---LDLLLKineeiGITILLITHEMNVIqRICDRVAVMEHGAVVESG 223
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVkaaLDELMK-----GRTTFIIAHRLSTV-RNADRILVFDNGRVVESG 551
|
.
gi 446493510 224 T 224
Cdd:PRK13657 552 S 552
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
1.53e-29 |
|
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: 112.97 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:cd03244 3 IEFKNVS--LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMI------FQGfnllktvTVYENIAlPLRLAgiSKVEIEKRVEK---YLRIVDLFTRKDAYPSE----LSGGQKQR 148
Cdd:cd03244 78 SRISIIpqdpvlFSG-------TIRSNLD-PFGEY--SDEELWQALERvglKEFVESLPGGLDTVVEEggenLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 149 VAIARALSHEPEVLLSDEATSALDPETTDSILDLllkINEEI-GITILLITHEMN-VIQriCDRVAVMEHGAVVESGT 224
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDtIID--SDRILVLDKGRVVEFDS 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
3.91e-29 |
|
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: 112.49 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkVfttKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGN-IIVNSQDLTTLSAKELak 79
Cdd:COG1119 3 LLELRNVT-V---RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 aRQKIGMI--FQGFNLLKTVTVYE--------NIALPLRlagISKVEIEkRVEKYLRIVDLFTRKDAYPSELSGGQKQRV 149
Cdd:COG1119 77 -RKRIGLVspALQLRFPRDETVLDvvlsgffdSIGLYRE---PTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 150 AIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
.
gi 446493510 230 T 230
Cdd:COG1119 232 T 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
5.05e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.71 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAka 80
Cdd:PRK09536 3 MIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rQKIGMIFQGFNLLKTVTVYENIAL---P--LRLAGISKVEiEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARAL 155
Cdd:PRK09536 77 -RRVASVPQDTSLSFEFDVRQVVEMgrtPhrSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 156 SHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
9.94e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.12 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvftTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakA 80
Cdd:PRK11614 5 MLSFDKVS----AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--M 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQGFNLLKTVTVYENIALPLRLAgiSKVEIEKRVEkylRIVDLF----TRKDAYPSELSGGQKQRVAIARALS 156
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIK---WVYELFprlhERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
1.60e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.08 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIrcvNLLEK---PTTGNIIVNSQDLTTLSAKELa 78
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIADYSEAAL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYEN--IALPL----RLAGI-SKVEIEKRVEKYLRIvdlftrkDAYPSE----LSGGQKQ 147
Cdd:PRK11160 413 --RQAISVVSQRVHLFSA-TLRDNllLAAPNasdeALIEVlQQVGLEKLLEDDKGL-------NAWLGEggrqLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRIcDRVAVMEHGAVVESGT 224
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-229 |
1.01e-27 |
|
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: 113.69 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRC-VNLLeKPTTGNIIVNSQDLTTLSAKELAKArqkIGMIFQGFNLLKTvTV 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLlVGVW-PPTAGSVRLDGADLSQWDREELGRH---IGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 100 YENIAlplRLAgisKVEIEKrVEKYLRIVDLF-----------TRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEAT 168
Cdd:COG4618 423 AENIA---RFG---DADPEK-VVAAAKLAGVHemilrlpdgydTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 169 SALDPETTDSILDLLLKINEEiGITILLITHEMNVIQrICDRVAVMEHGAVVESGTVKDIF 229
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-217 |
1.03e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 107.87 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTlsaKELakar 81
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGISkveiEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEG 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-219 |
1.30e-27 |
|
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: 107.94 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTlirCVNLLEK---PTTGNIIVNSQDLTTLSAKELa 78
Cdd:cd03248 12 VKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHKYL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGfNLLKTVTVYENIALPLRLAGISKV-EIEKRVEKYLRIVDL----FTRKDAYPSELSGGQKQRVAIAR 153
Cdd:cd03248 87 --HSKVSLVGQE-PVLFARSLQDNIAYGLQSCSFECVkEAAQKAHAHSFISELasgyDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRiCDRVAVMEHGAV 219
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-228 |
2.37e-27 |
|
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: 112.91 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 17 NVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIG------MIFQG 90
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINylpqepYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 91 fnllktvTVYENIALPLR--------LAGISKVEIEKRVEKYLRIVDlfTRKDAYPSELSGGQKQRVAIARALSHEPEVL 162
Cdd:TIGR01193 563 -------SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQ--TELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 163 LSDEATSALDPETTDSILDLLLKINEEigiTILLITHEMNVIQRIcDRVAVMEHGAVVESGTVKDI 228
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
3.96e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 107.87 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTG-----NIIVNSQDLttLSAKELAKARQKIGMIFQGFNLLK 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 tVTVYENIALPLRLAG-ISKVEIEKRVEKYLRIVDLFT----RKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSA 170
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 171 LDPETTDSILDLLLKINEEigITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFV 241
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-211 |
5.37e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQGFNLLKTvTVY 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY---RQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIALPLRLAGISKVEiekrvEKYLRIVDLF----TRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETT 176
Cdd:PRK10247 99 DNLIFPWQIRNQQPDP-----AIFLDDLERFalpdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 446493510 177 DSILDLLLKINEEIGITILLITHEMNVIQRiCDRV 211
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
9.01e-27 |
|
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: 104.87 E-value: 9.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLttlsAKELAKA 80
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQKIGMIFQgFNLLKTV-TVYENIALPLRLAGISKVEIekRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:COG4133 74 RRRLAYLGH-ADGLKPElTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493510 160 EVLLSDEATSALDPETTDSILDLllkINEEI--GITILLITHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAEL---IAAHLarGGAVLLTTHQ 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-220 |
2.53e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.96 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSkvfTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA-- 80
Cdd:COG3845 259 EVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 ------RQKIGMIfqgfnllKTVTVYENIAL------PLRLAG-ISKVEIEKRVEkylRIVDLF----TRKDAYPSELSG 143
Cdd:COG3845 336 ayipedRLGRGLV-------PDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAE---ELIEEFdvrtPGPDTPARSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 144 GQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
2.76e-26 |
|
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: 102.78 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSaKELakaR 81
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KAL---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTvTVYENIALPLrlagiskveiekrvekylrivdlftrkdaypselSGGQKQRVAIARALSHEPEV 161
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRIcDRVAVMEHGAVVESG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-222 |
5.07e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.07 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFTtkkgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKArq 82
Cdd:PRK11288 6 SFDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQGFNLLKTVTVYENI---ALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 160 EVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVES 222
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-224 |
7.24e-26 |
|
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: 108.95 E-value: 7.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFttKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTlsakELAKARQK 83
Cdd:TIGR01257 931 VKNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLL 163
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRICDRVAVMEHGAVVESGT 224
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-220 |
1.07e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElakA-RQKIGMI-----FQGfnLLKTVT 98
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD---AiRAGIAYVpedrkGEG--LVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 99 VYENIALPL-----RLAGISKVEIEKRVEKYLRIVDLFTRKDAYP-SELSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:COG1129 347 IRENITLASldrlsRGGLLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493510 173 PETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:COG1129 427 VGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-229 |
1.29e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.55 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 19 EALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtLSAKELAKARQKIGMIFQGFNLLKTVT 98
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 99 -VYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTD 177
Cdd:PRK13638 94 dIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493510 178 SILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIF 229
Cdd:PRK13638 174 QMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-228 |
1.91e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKarqKIGMIFQGFNLLKTVTVY 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---KVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIAL---PLRLA-GISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETT 176
Cdd:PRK10575 104 ELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493510 177 DSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-233 |
3.14e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.89 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 5 KNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKElaKARQKI 84
Cdd:PRK10895 7 KNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 85 GMIFQGFNLLKTVTVYENIALPLRL-AGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLL 163
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 164 SDEATSALDPettDSILDlLLKINEEI---GITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:PRK10895 161 LDEPFAGVDP---ISVID-IKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-228 |
6.31e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 105.49 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLircVNLLEK---PTTGNIIVNSQDLttlSAKELA 78
Cdd:PRK11176 342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfydIDEGEILLDGHDL---RDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQGFNLLKTvTVYENIALPlRLAGISKVEIEKrvekylrivdlfTRKDAYPSE------------------ 140
Cdd:PRK11176 414 SLRNQVALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEE------------AARMAYAMDfinkmdngldtvigengv 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 -LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSI---LDLLLKiNEeigiTILLITHEMNVIQRiCDRVAVMEH 216
Cdd:PRK11176 480 lLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDELQK-NR----TSLVIAHRLSTIEK-ADEILVVED 553
|
250
....*....|..
gi 446493510 217 GAVVESGTVKDI 228
Cdd:PRK11176 554 GEIVERGTHAEL 565
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-231 |
1.63e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.98 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAkelAKA 80
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP---AKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQ-KIGMIFQGFNLLKTVTVYENIAlpLRLAGisKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:PRK15439 84 HQlGIYLVPQEPLLFPNLSVKENIL--FGLPK--RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 160 EVLLSDEATSALDPETTDSildLLLKINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK15439 160 RILILDEPTASLTPAETER---LFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-199 |
2.85e-24 |
|
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: 103.21 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKArqkIGMIFQGFNLLK 95
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 TvTVYENialpLRLA--GISKVEIEK-----RVEKYLRIVD--LFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDE 166
Cdd:TIGR02868 423 T-TVREN----LRLArpDATDEELWAalervGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 446493510 167 ATSALDPETTDSILDLLLKINEeiGITILLITH 199
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-223 |
4.56e-24 |
|
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: 98.11 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTL---IRCVNLLEKPTTGNIIVNSQDLTTlsakelAK 79
Cdd:cd03234 5 PWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRKP------DQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 ARQKIGMIFQGFNLLKTVTVYENI--ALPLRLAGISKVEIEKRVEKYLRIVDLFTRK--DAYPSELSGGQKQRVAIARAL 155
Cdd:cd03234 79 FQKCVAYVRQDDILLPGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 156 SHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
8.25e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVN--------SQDLTTL 72
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGetvkigyfDQHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 73 SAKElakarqkigmifqgfnllktvTVYENIAlplRLA-GISKVEIEKRVEKYLrivdlFTRKDAY-P-SELSGGQKQRV 149
Cdd:COG0488 391 DPDK---------------------TVLDELR---DGApGGTEQEVRGYLGRFL-----FSGDDAFkPvGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 150 AIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINeeiGiTILLITHEMNVIQRICDRVAVMEHGAVVE 221
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-217 |
9.63e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.54 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTT--GNIIVNSQDLTTLSAKELA 78
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KArqKIGMIFQGFNLLKTVTVYENIAL---PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARAL 155
Cdd:PRK13549 81 RA--GIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 156 SHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-230 |
2.58e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 97.36 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 11 FTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKarqKIGMIFQG 90
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 91 FNLLKTVTVYENIA---LPLR-LAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDE 166
Cdd:PRK10253 90 ATTPGDITVQELVArgrYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 167 ATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-223 |
4.05e-23 |
|
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: 94.93 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 6 NVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVN--LLEKPTTGNIIVNSQDLttlsakELAKARQK 83
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYENIALPLRLAGISkveiekrvekylrivdlftrkdaypselsGGQKQRVAIARALSHEPEVLL 163
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKLRGLS-----------------------------GGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEEiGITILLITHE-MNVIQRICDRVAVMEHGAVVESG 223
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-217 |
5.64e-23 |
|
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: 99.51 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTT--GNIIVNSQDLTTLSAKEla 78
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQGFNLLKTVTVYENIAL--PLRLAG--ISKVEIEKRVEKYLRIVDLFTRKDAYP-SELSGGQKQRVAIAR 153
Cdd:TIGR02633 75 TERAGIVIIHQELTLVPELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-228 |
5.83e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 99.31 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTtkkgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA 80
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rqKIGMIFQGFNLLKTVTVYENIAL----PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALS 156
Cdd:PRK10762 80 --GIGIIHQELNLIPQLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 157 HEPEVLLSDEATSAL-DPETTdsilDLLLKINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETE----SLFRVIRElkSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-224 |
1.38e-22 |
|
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: 93.63 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 19 EALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLsakELAKARQKIGMIFQGfnllktvt 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSSLTIIPQD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 99 vyenialPLRLAGIskveiekrVEKYLRIVDLFTRKDAYP--------SELSGGQKQRVAIARALSHEPEVLLSDEATSA 170
Cdd:cd03369 91 -------PTLFSGT--------IRSNLDPFDEYSDEEIYGalrvseggLNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 171 LDPETtdsilDLLLK--INEEI-GITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:cd03369 156 IDYAT-----DALIQktIREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-224 |
2.50e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIrcvNLLEK--PTTGNIIVNSQDLTTLsakELAKARQKIGMIFQGFNLLKtVTVYEN 102
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPH-GTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 103 IALplRLAGISKVEIEKRVEK--YLRIVDLFTRKDAYP-----SELSGGQKQRVAIARALSHEPEVLLSDEATSALDPET 175
Cdd:PRK11174 443 VLL--GNPDASDEQLQQALENawVSEFLPLLPQGLDTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493510 176 TDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:PRK11174 521 EQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGD 566
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-223 |
1.68e-21 |
|
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: 90.66 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV--NLLEKPTTGNIIVNSQDLTTLSAKElaKARQKIGMIFQgfnl 93
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 94 lktvtvyeniaLPLRLAGIskveiekRVEKYLRIVDLftrkdaypsELSGGQKQRVAIARALSHEPEVLLSDEATSALDP 173
Cdd:cd03217 85 -----------YPPEIPGV-------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493510 174 ETTDSILDLLLKINEEiGITILLITHEMNVIQRI-CDRVAVMEHGAVVESG 223
Cdd:cd03217 138 DALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-233 |
2.70e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 91.15 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV-NLLekPTTGNIIVNSQDLTTLSAKELAKARqkiGMIFQGFNLLKTVTV 99
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 100 YENIALPLRlAGISKVEIEKRVEK---YLRIVDLFTRKdayPSELSGGQKQRVAIA-------RALSHEPEVLLSDEATS 169
Cdd:PRK03695 87 FQYLTLHQP-DKTRTEAVASALNEvaeALGLDDKLGRS---VNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 170 ALDPeTTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:PRK03695 163 SLDV-AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-217 |
3.82e-21 |
|
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: 89.84 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVEA---LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVnLLE-KPTTGNIIVNSQdlttlsakeL 77
Cdd:cd03250 1 ISVEDAS--FTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS---------I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKARQKiGMIFQGfnllktvTVYENIalplrLAGisKVEIEKRVEKYLRI------VDLFTRKDAypSE-------LSGG 144
Cdd:cd03250 69 AYVSQE-PWIQNG-------TIRENI-----LFG--KPFDEERYEKVIKAcalepdLEILPDGDL--TEigekginLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493510 145 QKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHG 217
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-237 |
5.01e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCV-NLLekPTTGNIIVNSQDLTTLSAKELAKARqkiGMIFQGFNLLKTVTVYENI 103
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 104 ALPLRlAGISKVEIEKRVEK---YLRIVDLFTRkdayP-SELSGGQKQRVAIARAL-----SHEPE--VLLSDEATSALD 172
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQlaeALGLEDKLSR----PlTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 173 PeTTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTnPQHVTT 237
Cdd:COG4138 166 V-AQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PENLSE 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-222 |
6.31e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 93.32 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIrcvNLLEK--PT---TGNIIVNSQDLT--TLS 73
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSGvyPHgsyEGEILFDGEVCRfkDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 74 AKElakaRQKIGMIFQGFNLLKTVTVYENIAL---PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVA 150
Cdd:NF040905 74 DSE----ALGIVIIHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVES 222
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-228 |
1.27e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 92.48 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFTtkkgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKarQK 83
Cdd:PRK10982 1 MSNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYENIAL---PLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPE 160
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
1.50e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQdlttlsakelakarQK 83
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------------LR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYENI--------ALPLRLAGISKV--EIEKRVEKYLRIVDLFTRKDAY---------------- 137
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVldgdaelrALEAELEELEAKlaEPDEDLERLAELQEEFEALGGWeaearaeeilsglgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 138 -------PSELSGGQKQRVAIARALSHEPEVLLSDEATSALDpetTDSIL---DLLLKINeeigITILLITHEMNVIQRI 207
Cdd:COG0488 143 eedldrpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwleEFLKNYP----GTVLVVSHDRYFLDRV 215
|
250
....*....|
gi 446493510 208 CDRVAVMEHG 217
Cdd:COG0488 216 ATRILELDRG 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-230 |
2.79e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.17 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 7 VSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKIGM 86
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 87 IFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDE 166
Cdd:PRK15056 89 VDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 167 ATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDrVAVMEHGAVVESGTVKDIFT 230
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-232 |
3.06e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 91.70 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 9 KVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIF 88
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW---RSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 89 QGfNLLKTVTVYENIALPLRLAgiSKVEIEkRVEKYLRIVDLFTR-KDAYPSE-------LSGGQKQRVAIARALSHEPE 160
Cdd:PRK10789 396 QT-PFLFSDTVANNIALGRPDA--TQQEIE-HVARLASVHDDILRlPQGYDTEvgergvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493510 161 VLLSDEATSALDPETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
260-333 |
4.85e-20 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 82.94 E-value: 4.85e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 260 TGEIVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLIIHMQGEQNEINRALSFLQEQGIIVE 333
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVE 74
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-256 |
5.25e-20 |
|
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: 91.61 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFTTKKGnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVnllekptTGNIIVNSQDLTTLSAK---EL 77
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGDATVAGKSiltNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKARQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSH 157
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI---FTNPQH 234
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkskFGDGYI 2166
|
250 260 270
....*....|....*....|....*....|....
gi 446493510 235 VTTK------------KFVNSAFAAKIPEDVQKE 256
Cdd:TIGR01257 2167 VTMKikspkddllpdlNPVEQFFQGNFPGSVQRE 2200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-217 |
6.20e-20 |
|
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: 84.81 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVnsqdlttlsakelakar 81
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 qkigmifqgfnllktvtvyenialplrlagISKVEIekrvekylrivdlftrkdAYPSELSGGQKQRVAIARALSHEPEV 161
Cdd:cd03221 60 ------------------------------GSTVKI------------------GYFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKINeeigITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
5.19e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.85 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVeALKSTSLQVKKGEVFGIIGYSGAGKSTLircVNLLE---KPTTGNIIVNSQDLTTLSAKELa 78
Cdd:PRK10790 341 IDIDNVS--FAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSSLSHSVL- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 kaRQKIGMIFQGFNLLKTvTVYENIALPLRLAgiskveiEKRVEKYLRIVDL-----------FTRKDAYPSELSGGQKQ 147
Cdd:PRK10790 414 --RQGVAMVQQDPVVLAD-TFLANVTLGRDIS-------EEQVWQALETVQLaelarslpdglYTPLGEQGNNLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEigITILLITHEMNVIQRiCDRVAVMEHGAVVESGT 224
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-244 |
7.11e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFTTKKGNVealkstSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSakELAKARQ 82
Cdd:PRK09700 267 EVRNVTSRDRKKVRDI------SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 KIGMIFQ-----GFnlLKTVTVYENIALP--LRLAG-------ISKVEIEKRVEKYLRIVDLFTRK-DAYPSELSGGQKQ 147
Cdd:PRK09700 339 GMAYITEsrrdnGF--FPNFSIAQNMAISrsLKDGGykgamglFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVEsgtvkd 227
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ------ 489
|
250
....*....|....*..
gi 446493510 228 IFTNPQHVTTKKFVNSA 244
Cdd:PRK09700 490 ILTNRDDMSEEEIMAWA 506
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
263-333 |
7.64e-19 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 79.42 E-value: 7.64e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 263 IVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLIIHMQGEQNEINRALSFLQEQGIIVE 333
Cdd:pfam09383 2 LVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVE 72
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-233 |
8.50e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.40 E-value: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQdlttlsakelaka 80
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rQKIGMIFQGFNLLKTVTVYENIALPLRlAGISKVEIE---KRVEKYLRIvdlftrkDAYPSELSGGQKQRVAIARALSH 157
Cdd:PRK09544 67 -LRIGYVPQKLYLDTTLPLTVNRFLRLR-PGTKKEDILpalKRVQAGHLI-------DAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHgAVVESGTVKDIFTNPQ 233
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-199 |
1.07e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDlttlsakelakarqkiGMIFqgfnL-----LK 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------------RVLF----LpqrpyLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 TVTVYENIALPLRLAGISkveiEKRVEKYLRIVDL------FTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATS 169
Cdd:COG4178 439 LGTLREALLYPATAEAFS----DAELREALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|
gi 446493510 170 ALDPETTDSILDLLLKinEEIGITILLITH 199
Cdd:COG4178 515 ALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-199 |
1.66e-18 |
|
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: 81.43 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVeALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDlttlsakelakar 81
Cdd:cd03223 1 IELENLS--LATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 qkiGMIFqgfnllktvtvyeniaLPLRlagiskveiekrveKYLRIVDLftrKDA--YP--SELSGGQKQRVAIARALSH 157
Cdd:cd03223 65 ---DLLF----------------LPQR--------------PYLPLGTL---REQliYPwdDVLSGGEQQRLAFARLLLH 108
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLLlkinEEIGITILLITH 199
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-205 |
5.18e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNsqDLTTLSAKELAKAR 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGfNLLKTVTVYENIALPL------------------------------------RLAGISK-------VEIE 118
Cdd:PTZ00265 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagDLNDMSNttdsnelIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 119 KR-----------VEKYLRIVDLFTR-KDAY-------PSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSI 179
Cdd:PTZ00265 539 KNyqtikdsevvdVSKKVLIHDFVSAlPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|....*...
gi 446493510 180 LDLL--LKINEEiGITIlLITHEMNVIQ 205
Cdd:PTZ00265 619 QKTInnLKGNEN-RITI-IIAHRLSTIR 644
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-221 |
1.64e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.00 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKIGMIFQGFNLLKTVtvy 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNAV--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 enialplrlaGISKVEiekrvekylrivdLFTRKdayPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSIL 180
Cdd:COG2401 123 ----------GLSDAV-------------LWLRR---FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446493510 181 DLLLKINEEIGITILLITHEMNVIQRIC-DRVAVMEHGAVVE 221
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-244 |
3.24e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRcvnllekPTTGNIIVNSQDLTTLSAKELakaR 81
Cdd:PTZ00265 1226 IVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDYNLKDL---R 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGfNLLKTVTVYENIALPLRLAGISKVeieKRVEKYLRIVDLF--------TRKDAYPSELSGGQKQRVAIAR 153
Cdd:PTZ00265 1296 NLFSIVSQE-PMLFNMSIYENIKFGKEDATREDV---KRACKFAAIDEFIeslpnkydTNVGPYGKSLSGGQKQRIAIAR 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEH----GAVVESGTVKDIF 229
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTHEEL 1450
|
250
....*....|....*
gi 446493510 230 TNPQHVTTKKFVNSA 244
Cdd:PTZ00265 1451 LSVQDGVYKKYVKLA 1465
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-231 |
6.90e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 11 FTTKKGNVE-ALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI-IVNSQDLTTLSAkelakarqkigmif 88
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAALIAISS-------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 89 qGFNllKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEAT 168
Cdd:PRK13545 95 -GLN--GQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 169 SALDPETTDSILDlllKINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK13545 172 SVGDQTFTKKCLD---KMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-231 |
7.81e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.25 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 19 EALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKE--------LAKARQKIGMIFQ- 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDRQSSGLYLDa 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 90 --GFNLlkTVTVYENIALPLRLAGISKVeiekrVEKYLRIVDL-FTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDE 166
Cdd:PRK15439 357 plAWNV--CALTHNRRGFWIKPARENAV-----LERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 167 ATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD 493
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-235 |
8.56e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.10 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV--NLLEKPT------TGNIIVNSQDLTTLSAKELAKARQKIGMIFQ--- 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 90 GFNLLKTVTV--YENI----ALPLRLAGISKVEIEkrvekyLRIVDLFTRKDAypSELSGGQKQRVAIARALSH------ 157
Cdd:PRK13547 97 AFSAREIVLLgrYPHArragALTHRDGEIAWQALA------LAGATALVGRDV--TTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 158 ---EPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTnPQH 234
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
.
gi 446493510 235 V 235
Cdd:PRK13547 248 I 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-225 |
1.10e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIrcvNLLEKPTTGNIIVNSQDLTTLSAKELAKAR 81
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLLNGMPIDAKEMR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYE--NIALPLRL-AGISKVEIEKRVEKYLRIVDLftRKDA--------YPSELSGGQKQRVA 150
Cdd:TIGR00955 99 AISAYVQQDDLFIPTLTVREhlMFQAHLRMpRRVTKKEKRERVDEVLQALGL--RKCAntrigvpgRVKGLSGGERKRLA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTV 225
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-215 |
1.26e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 75.52 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVnsqDLTTLSAKElakarQKIGMIFQGfnllktvTVY 100
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKP-----QYIKADYEG-------TVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIALPLRLAGIS---KVEIEKRvekyLRIVDLFTRKdayPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTD 177
Cdd:cd03237 80 DLLSSITKDFYTHpyfKTEIAKP----LQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 446493510 178 SILDLLLKINEEIGITILLITHEMNVIQRICDRVAVME 215
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-285 |
1.74e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlSAKELAKAR 81
Cdd:NF033858 2 ARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGF--NLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEP 159
Cdd:NF033858 76 PRIAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 160 EVLLSDEATSALDPettdsiL------DLLLKINEE-IGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNp 232
Cdd:NF033858 156 DLLILDEPTTGVDP------LsrrqfwELIDRIRAErPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLAR- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 233 qhvTTKKFVNSAFAAKIPEDVQkelQTTGEIVTLSFIGNSSGEPALaVA---TKRF 285
Cdd:NF033858 228 ---TGADTLEAAFIALLPEEKR---RGHQPVVIPPRPADDDDEPAI-EArglTMRF 276
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-228 |
3.15e-15 |
|
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: 76.91 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQGFNLLKTvtvy 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLFSG---- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 eniALPLRLAGISKVEiEKRVEKYLRIVDLFTRKDAYPSE-----------LSGGQKQRVAIARALSHEPEVLLSDEATS 169
Cdd:TIGR00957 1375 ---SLRMNLDPFSQYS-DEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 170 ALDPETTDSILDLLLKINEEigITILLITHEMNVIQRICdRVAVMEHGAVVESGTVKDI 228
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-261 |
5.69e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.32 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSakeLAKARQKIGMIFQGfNLLKTVTVY 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQA-PVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIAlPLRLAgiSKVEIEKRVEK-YLRivDLFTRK----DAYPSE----LSGGQKQRVAIARALSHEPEVLLSDEATSAL 171
Cdd:PLN03130 1331 FNLD-PFNEH--NDADLWESLERaHLK--DVIRRNslglDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 172 DPETtdsilDLLLK--INEEI-GITILLITHEMNVIqrI-CDRVAVMEHGAVVESGTVKDIFTNPqhvttkkfvNSAFAa 247
Cdd:PLN03130 1406 DVRT-----DALIQktIREEFkSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSNE---------GSAFS- 1468
|
250
....*....|....
gi 446493510 248 kipedvqKELQTTG 261
Cdd:PLN03130 1469 -------KMVQSTG 1475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-217 |
1.14e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKE-LAKARQKIGMIFQGFNLLKTVTVYENI 103
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKRDGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 104 ALP-LRLAGISKVEIEKRVEKYL--RIVDLFTRK----DAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETT 176
Cdd:PRK10762 352 SLTaLRYFSRAGGSLKHADEQQAvsDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493510 177 DSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:PRK10762 432 KEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-215 |
1.73e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 27 QVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnSQDLtTLSAKElakarQKIGMIFQGfnllktvTVYENialp 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL-KISYKP-----QYIKPDYDG-------TVEDL---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 107 lrLAGIS--------KVEIEKRvekyLRIVDLFtrkDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDS 178
Cdd:PRK13409 421 --LRSITddlgssyyKSEIIKP----LQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 446493510 179 ILDLLLKINEEIGITILLITHEMNVIQRICDRVAVME 215
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
1.95e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSkvFTTKKGNVeALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsAKELAKAR 81
Cdd:PRK10522 323 LELRNVT--FAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 QKIGMIFQGFNLLKTVTVYENIALPLRLAGI--------SKVEIEKrvekyLRIVDLftrkdaypsELSGGQKQRVAIAR 153
Cdd:PRK10522 397 KLFSAVFTDFHLFDQLLGPEGKPANPALVEKwlerlkmaHKLELED-----GRISNL---------KLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 154 ALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVE 221
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-219 |
4.73e-14 |
|
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: 72.94 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCV-NLLEKPTTGNIIVNSQDLTTlsaKELAKA-RQKIGMIFQG---FNLLKTVTV 99
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDI---RNPAQAiRAGIAMVPEDrkrHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 100 YENIALPL--RLAGISKVEIEKRVEKYLRIVDLFTRKDAYP----SELSGGQKQRVAIARALSHEPEVLLSDEATSALDP 173
Cdd:TIGR02633 357 GKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446493510 174 ETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-220 |
5.57e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKA--------RQKIGMIfqgfnllKT 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEGII-------PV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 97 VTVYENIALPLRLAGIS-KVEIEKRVEKylRIVDLFTRKDAY--PS------ELSGGQKQRVAIARALSHEPEVLLSDEA 167
Cdd:PRK11288 346 HSVADNINISARRHHLRaGCLINNRWEA--ENADRFIRSLNIktPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493510 168 TSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-215 |
6.92e-14 |
|
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: 72.51 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 27 QVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSqdltTLSAKElakarQKIGMIFQGfnllktvTVYENI--A 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDL----KISYKP-----QYISPDYDG-------TVEEFLrsA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 105 LPLRLAG-ISKVEIEKRvekyLRIVDLFtrkDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLL 183
Cdd:COG1245 426 NTDDFGSsYYKTEIIKP----LGLEKLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190
....*....|....*....|....*....|..
gi 446493510 184 LKINEEIGITILLITHEMNVIQRICDRVAVME 215
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-231 |
9.84e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQGfNLLKTVTVY 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQS-PVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIAlplRLAGISKVEIEKRVEKyLRIVDLFTRK----DAYPSE----LSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PLN03232 1328 FNID---PFSEHNDADLWEALER-AHIKDVIDRNpfglDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 173 PEtTDSILDllLKINEEI-GITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PLN03232 1404 VR-TDSLIQ--RTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-233 |
1.04e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.50 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQGFNLLKTvTVY 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENI-----ALPLRL-AGISKVEIEKRVEKYLRIVDlfTRKDAYPSELSGGQKQRVAIARA-LSHEPEVLLSDEATSALDP 173
Cdd:PTZ00243 1402 QNVdpfleASSAEVwAALELVGLRERVASESEGID--SRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATANIDP 1479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 174 ETTDSILDLLLKINEeiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNPQ 233
Cdd:PTZ00243 1480 ALDRQIQATVMSAFS--AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-199 |
1.20e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVfttkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAka 80
Cdd:PRK13539 2 MLEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 rQKIGMIfqgfNLLK-TVTVYENIALPLRLAGISKVEIEKRVEkYLRIVDLFTRKDAYpseLSGGQKQRVAIARAL-SHE 158
Cdd:PRK13539 76 -HYLGHR----NAMKpALTVAENLEFWAAFLGGEELDIAAALE-AVGLAPLAHLPFGY---LSAGQKRRVALARLLvSNR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493510 159 PeVLLSDEATSALDPETTDSILDLLLKINEEIGItILLITH 199
Cdd:PRK13539 147 P-IWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
1.23e-13 |
|
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: 71.50 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSqdltTLsakelakar 81
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE----TV--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 qKIGMIFQGFNLLK-TVTVYENIALPLRLAGISKVEIEKRVekYlriVDLFTRKDA----YPSELSGGQKQRVAIARALS 156
Cdd:TIGR03719 386 -KLAYVDQSRDALDpNKTVWEEISGGLDIIKLGKREIPSRA--Y---VGRFNFKGSdqqkKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLkineEIGITILLITHEMNVIQRIC 208
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALL----NFAGCAVVISHDRWFLDRIA 507
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-200 |
1.77e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCvnLLEKPTTGNI-----IVNSQDLTTLSAKel 77
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVItggdrLVNGRPLDSSFQR-- 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 akarqKIGMIFQGFNLLKTVTVYENIALPLRL---AGISKVEIEKRVEKYLRIVDLFTRKDAY---PSE-LSGGQKQRVA 150
Cdd:TIGR00956 837 -----SIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLT 911
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493510 151 IARALSHEPEVLL-SDEATSALDPETTDSILDLLLKINEEiGITILLITHE 200
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQ 961
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-225 |
6.61e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.74 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 16 GNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV------NLLEkpttGNIIVNSQDLTTLSAKElakaRQKIGmIFQ 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESILDLEPEE----RAHLG-IFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 90 GFNLLKTVTVYENIALpLRLAGISKVEIEKRVE-----------KYLRIVDL---FTRKDAypSE-LSGGQKQRVAIARA 154
Cdd:CHL00131 89 AFQYPIEIPGVSNADF-LRLAYNSKRKFQGLPEldplefleiinEKLKLVGMdpsFLSRNV--NEgFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 155 LSHEPEVLLSDEATSALDpettdsiLDLLLKINEEIGI------TILLITHEMNVIQRIC-DRVAVMEHGAVVESGTV 225
Cdd:CHL00131 166 ALLDSELAILDETDSGLD-------IDALKIIAEGINKlmtsenSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-199 |
8.10e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.23 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 12 TTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLsAKELAKARQKIGMIfqgf 91
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 92 NLLKTV-TVYENIALPLRLAGISKVEIEKRVEKylriVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSA 170
Cdd:TIGR01189 82 PGLKPElSALENLHFWAAIHGGAQRTIEDALAA----VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 446493510 171 LDPETTDsILDLLLKINEEIGITILLITH 199
Cdd:TIGR01189 158 LDKAGVA-LLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-200 |
1.76e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.04 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFTTKKgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNiivnsqdlttlsakelAKARQ- 82
Cdd:TIGR03719 7 MNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----------------ARPQPg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 83 -KIGMIFQGFNLLKTVTVYENIALPL--------RLAGIS------KVEIEKRVEKYLRIVDLFTRKDAY---------- 137
Cdd:TIGR03719 68 iKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNEISakyaepDADFDKLAAEQAELQEIIDAADAWdldsqleiam 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 138 -----P------SELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLlkinEEIGITILLITHE 200
Cdd:TIGR03719 148 dalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-205 |
6.20e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAkELAKARQKIGMIfqgfNLLKTV-TVYENI 103
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHA----PGIKTTlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 104 ALPLRLAGISKVEiekrveKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLL 183
Cdd:cd03231 95 RFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180
....*....|....*....|..
gi 446493510 184 LKINEEIGITILLITHEMNVIQ 205
Cdd:cd03231 169 AGHCARGGMVVLTTHQDLGLSE 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-217 |
1.47e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCV-NLLEKPTTGNIIVNSQDLTTLSAKElaKARQKIGMIFQG---FNLLKTVTVY 100
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIALPL--RLAGISKVEIEKRVEKYLRIVDLFTRKDAYP----SELSGGQKQRVAIARALSHEPEVLLSDEATSALDPE 174
Cdd:PRK13549 360 KNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493510 175 TTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:PRK13549 440 AKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-199 |
1.67e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.16 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVftTKKGNVeALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVN--------LLEKPTTGNIIVNSQ----D 68
Cdd:TIGR00954 451 GIKFENIPLV--TPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQrpymT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 69 LTTLsakelakaRQKIgmifqgfnllktvtVYENIALPLRLAGISkveiEKRVEKYLRIVDL---FTRKDAYPS------ 139
Cdd:TIGR00954 528 LGTL--------RDQI--------------IYPDSSEDMKRRGLS----DKDLEQILDNVQLthiLEREGGWSAvqdwmd 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 140 ELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLlkinEEIGITILLITH 199
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-228 |
1.81e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTTKKGNVE----------------ALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVN 65
Cdd:PRK13546 5 VNIKNVTKEYRIYRTNKErmkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 66 SQdlttlsakelakarqkIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQ 145
Cdd:PRK13546 85 GE----------------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETTDSILDlllKINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVVESG 223
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD---KIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
....*
gi 446493510 224 TVKDI 228
Cdd:PRK13546 226 ELDDV 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-230 |
5.81e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAG--KSTLIRCVNlleKPTTGNiivNSQDLTTLSAKELAk 79
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*---GPDAGR---RPWRF*TWCANRRA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 80 ARQKIGM---IFQGFNllKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALS 156
Cdd:NF000106 83 LRRTIG*hrpVR*GRR--ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFT 230
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-231 |
1.05e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVnLLEKPttgniivNSQDLTTLSAKELAKARQkIGMIFQGfnllktvTVY 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELS-------HAETSSVVIRGSVAYVPQ-VSWIFNA-------TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIalplrLAGiSKVEiekrVEKYLRIVDLFTRK---DAYPSE-----------LSGGQKQRVAIARALSHEPEVLLSDE 166
Cdd:PLN03232 697 ENI-----LFG-SDFE----SERYWRAIDVTALQhdlDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 167 ATSALDPETTDSILDLLLKiNEEIGITILLITHEMNVIQRIcDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-221 |
3.98e-10 |
|
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: 60.97 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsAKELAKARQKIGMIFQGFNLLKtvtvyenia 104
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQLFSAVFSDFHLFD--------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 105 lplRLAGISKVEIEKRVEKYLRIVDL----------FTRKDaypseLSGGQKQRVAIARALSHEPEVLLSDEATSALDPE 174
Cdd:COG4615 420 ---RLLGLDGEADPARARELLERLELdhkvsvedgrFSTTD-----LSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 175 ------TTdsildLL--LKineEIGITILLITHEmnviQR---ICDRVAVMEHGAVVE 221
Cdd:COG4615 492 frrvfyTE-----LLpeLK---ARGKTVIAISHD----DRyfdLADRVLKMDYGKLVE 537
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-231 |
5.10e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 15 KGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVnLLEKPTT--GNIIVNSQdlttlsakeLAKARQkIGMIFQGfn 92
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPPRsdASVVIRGT---------VAYVPQ-VSWIFNA-- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 93 llktvTVYENIalplrLAGiSKVEIEkRVEKYLRIVDLFTRKDAYPS-----------ELSGGQKQRVAIARALSHEPEV 161
Cdd:PLN03130 694 -----TVRDNI-----LFG-SPFDPE-RYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 162 LLSDEATSALDPETTDSILDLLLKiNEEIGITILLITHEMNVIQRIcDRVAVMEHGAVVESGTVKDIFTN 231
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-220 |
1.01e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVN---LLEKpttGNIIVNsQDLTtLSAKELAKARQKIGMIF--------- 88
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYE-QDLI-VARLQQDPPRNVEGTVYdfvaegiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 89 QGfNLLKTvtvYENIALPL----------RLAGISKV-------EIEKRVEKYLRIVDLftRKDAYPSELSGGQKQRVAI 151
Cdd:PRK11147 94 QA-EYLKR---YHDISHLVetdpseknlnELAKLQEQldhhnlwQLENRINEVLAQLGL--DPDAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 152 ARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeigiTILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
1.28e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSqdltTLsakelakar 81
Cdd:PRK11819 325 IEAENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----TV--------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 qKIGMIFQGF-NLLKTVTVYENIALPLRLAGISKVEIEKRvekylrivdlftrkdAYPS--------------ELSGGQK 146
Cdd:PRK11819 388 -KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSR---------------AYVGrfnfkggdqqkkvgVLSGGER 451
|
170 180
....*....|....*....|....*....
gi 446493510 147 QRVAIARALSHEPEVLLSDEATSALDPET 175
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-204 |
1.55e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 25 SLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLttlsakelAKARQKigmiFQGfNLL--------KT 96
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRDE----YHQ-DLLylghqpgiKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 97 V-TVYENIALPLRLAGISKVEiekRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIAR-ALSHEPEVLLsDEATSALDPE 174
Cdd:PRK13538 88 ElTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|
gi 446493510 175 TTDSILDLLLKINEEIGITILLITHEMNVI 204
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTHQDLPVA 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-218 |
3.57e-09 |
|
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: 56.19 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 5 KNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKEL-AKARQK 83
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTvTVYENIAL--PLRlagiskveiEKRVEKYLRIVDLFTRKDAYPS-----------ELSGGQKQRVA 150
Cdd:cd03290 81 VAYAAQKPWLLNA-TVEENITFgsPFN---------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 151 IARALSHEPEVLLSDEATSALDPETTDSILDL-LLKINEEIGITILLITHEMNVIQRiCDRVAVMEHGA 218
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-200 |
4.40e-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: 55.33 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 5 KNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCvnLLEKPTTGNIIVNSqdltTLSAKELAKARQK- 83
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAGVITGEI----LINGRPLDKNFQRs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYEnialPLRLAGiskveiekrvekYLRivdlftrkdaypsELSGGQKQRVAIARALSHEPEVLL 163
Cdd:cd03232 81 TGYVEQQDVHSPNLTVRE----ALRFSA------------LLR-------------GLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 446493510 164 SDEATSALDPETTDSILDLLLKINEEiGITILLITHE 200
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQ 167
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-215 |
4.57e-09 |
|
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: 55.27 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 28 VKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnSQDLTTLSAKElakarQKIgmifqgfnllktvtvyenialpl 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND---EWDGITPVYKP-----QYI----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 108 rlagiskveiekrvekylrivdlftrkdaypsELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKIN 187
Cdd:cd03222 71 --------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*...
gi 446493510 188 EEIGITILLITHEMNVIQRICDRVAVME 215
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-219 |
6.12e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSKVfttkkgNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKE---- 76
Cdd:PRK10982 250 ILEVRNLTSL------RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 77 ----LAKARQKIGMIFQ---GFN-LLKTVTVYENialPLRLAGISKVEIEKRvekylRIVDLFTRKDayPSE------LS 142
Cdd:PRK10982 324 gfalVTEERRSTGIYAYldiGFNsLISNIRNYKN---KVGLLDNSRMKSDTQ-----WVIDSMRVKT--PGHrtqigsLS 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493510 143 GGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAV 219
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-223 |
1.19e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 1 MIELKNVSkvfTTKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLE--KPTTGNIIVNSQDLTTLSAKEla 78
Cdd:PRK09580 1 MLSIKDLH---VSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQ----------GFNL---LKTVTVYENIAlPLRLAGISKVeIEKRVEKYLRIVDLFTRkdAYPSELSGGQ 145
Cdd:PRK09580 75 RAGEGIFMAFQypveipgvsnQFFLqtaLNAVRSYRGQE-PLDRFDFQDL-MEEKIALLKMPEDLLTR--SVNVGFSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 146 KQRVAIARALSHEPEVLLSDEATSALDPETtdsildllLKINEEiGITIL--------LITHEMNVIQRI-CDRVAVMEH 216
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDA--------LKIVAD-GVNSLrdgkrsfiIVTHYQRILDYIkPDYVHVLYQ 221
|
....*..
gi 446493510 217 GAVVESG 223
Cdd:PRK09580 222 GRIVKSG 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-210 |
1.24e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSKVFTTKKgnvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGniivnsqdlttlsakelaKAR-- 81
Cdd:PRK11819 9 MNRVSKVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------------EARpa 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 82 --QKIGMIFQGFNLLKTVTVYENIALPLRlagiskvEIEKRVEKYLRIVDLFTRKDAYPSE------------------- 140
Cdd:PRK11819 68 pgIKVGYLPQEPQLDPEKTVRENVEEGVA-------EVKAALDRFNEIYAAYAEPDADFDAlaaeqgelqeiidaadawd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 -----------------------LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDsILDLLLKinEEIGiTILLI 197
Cdd:PRK11819 141 ldsqleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA-WLEQFLH--DYPG-TVVAV 216
|
250
....*....|....*....
gi 446493510 198 THEM----NVIQRIC--DR 210
Cdd:PRK11819 217 THDRyfldNVAGWILelDR 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-220 |
1.61e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCV--NLLEKPTTGNIIVNSQDLTTLSAKELAKA--------RQKIGMifqg 90
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTVSDAIDAglayvtedRKGYGL---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 91 fNLLKTVTvyENIALPlRLAGISKVEI-----EKRV-EKY---LRI----VDLFTRKdaypseLSGGQKQRVAIARALSH 157
Cdd:NF040905 352 -NLIDDIK--RNITLA-NLGKVSRRGVideneEIKVaEEYrkkMNIktpsVFQKVGN------LSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 158 EPEVLLSDEATSALDPETTDSILDLllkINE--EIGITILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-229 |
2.04e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 8 SKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQdlttlsakeLAKARQKIgmi 87
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------VAYVPQQA--- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 88 fqgfnLLKTVTVYENIALPLRLAgiskveiEKRVEKYLRIVDLFTRKDAYPS-----------ELSGGQKQRVAIARALS 156
Cdd:TIGR00957 709 -----WIQNDSLRENILFGKALN-------EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 157 HEPEVLLSDEATSALDPETTDSILDL------LLKineeiGITILLITHEMNVIQRIcDRVAVMEHGAVVESGTVKDIF 229
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEHvigpegVLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-223 |
2.34e-08 |
|
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: 53.42 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 4 LKNVSkvFTTKKGNVEA--LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLekpTTGNIIVNSqDLT--TLSAKELA- 78
Cdd:cd03233 6 WRNIS--FTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEG-DIHynGIPYKEFAe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 79 KARQKIGMIFQGFNLLKTVTVYENIALPLRLAGiskveiekrvekylrivdlftrkDAYPSELSGGQKQRVAIARALSHE 158
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 159 PEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNV-IQRICDRVAVMEHGAVVESG 223
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
2.60e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTtlsaKELAKARQKIGMIFQGFNLLKTVTVY 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIALPLRLAGiSKVEIEKRVekylRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPEttdSIL 180
Cdd:PRK13540 93 ENCLYDIHFSP-GAVGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL---SLL 164
|
170 180
....*....|....*....|..
gi 446493510 181 DLLLKINE--EIGITILLITHE 200
Cdd:PRK13540 165 TIITKIQEhrAKGGAVLLTSHQ 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-232 |
3.39e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRcvNLLekpttGNIIVNSQDLttLSAKELAKARQKIGMIfqgfnllkTVTVY 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLL-----SQFEISEGRV--WAERSIAYVPQQAWIM--------NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIAL-----PLRLAGISKVeieKRVEKYLRIVD--LFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDP 173
Cdd:PTZ00243 739 GNILFfdeedAARLADAVRV---SQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 174 ETTDSIL-DLLLkiNEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNP 232
Cdd:PTZ00243 816 HVGERVVeECFL--GALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-210 |
4.33e-08 |
|
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: 51.61 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 30 KGEVFGIIGYSGAGKSTLIRCV-NLLEKPTTGNIIVNSQDLTTlsakelakarqkigmifqgfnllktvtvyenialplr 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILE------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 109 lagiskveiekrvekYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDL-----L 183
Cdd:smart00382 44 ---------------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180
....*....|....*....|....*..
gi 446493510 184 LKINEEIGITILLITHEMNVIQRICDR 210
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-172 |
5.73e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 28 VKKGEVFGIIGYSGAGKSTLIRCV---------NLLEKPTTGNII-----VNSQD-LTTLSAKELaKARQKIGMI----- 87
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVLkrfrgTELQNyFKKLYNGEI-KVVHKPQYVdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 88 -FQG--FNLLKTVT---VYENIalplrlagISKVEIEKRVEKYLrivdlftrkdaypSELSGGQKQRVAIARALSHEPEV 161
Cdd:PRK13409 175 vFKGkvRELLKKVDergKLDEV--------VERLGLENILDRDI-------------SELSGGELQRVAIAAALLRDADF 233
|
170
....*....|.
gi 446493510 162 LLSDEATSALD 172
Cdd:PRK13409 234 YFFDEPTSYLD 244
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-267 |
6.76e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARALSHEPE--VLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQrICDRV------A 212
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMIS-LADRIidigpgA 554
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 213 VMEHGAVVESGTVKDiFTNPQHVTTKKFVNSAFAAKIPEDVQKELQTtgeiVTLS 267
Cdd:PRK00635 555 GIFGGEVLFNGSPRE-FLAKSDSLTAKYLRQELTIPIPEKRTNSLGT----LTLS 604
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
12-225 |
7.59e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 12 TTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIrcvnllekpttgniivnSQDLTTLSAKELAKARQKigmifqgF 91
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLISFLPK-------F 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 92 NLLKTVTVYEnialplrLAGISKVEIEkrvekYLRIvdlftrkDAYPSELSGGQKQRVAIARALSHEPE--VLLSDEATS 169
Cdd:cd03238 58 SRNKLIFIDQ-------LQFLIDVGLG-----YLTL-------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 170 ALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTV 225
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFGPGSGKSGGKV 172
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-205 |
7.85e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 36 IIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLsakelakarQKIGMIFQGFNL-LKT-VTVYENIALPLRLagIS 113
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---------AKPYCTYIGHNLgLKLeMTVFENLKFWSEI--YN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 114 KVEIEKRVEKYLRIVDLFTRKDAypsELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDsILDLLLKINEEIGIT 193
Cdd:PRK13541 100 SAETLYAAIHYFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD-LLNNLIVMKANSGGI 175
|
170
....*....|..
gi 446493510 194 ILLITHEMNVIQ 205
Cdd:PRK13541 176 VLLSSHLESSIK 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-172 |
8.63e-08 |
|
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: 53.63 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 29 KKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI--------IVNS------QD-LTTLSAKELaKARQKIGMIFQgfnl 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKRfrgtelQDyFKKLANGEI-KVAHKPQYVDL---- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 94 lktvtvyeniaLPLRLAG-----ISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEAT 168
Cdd:COG1245 172 -----------IPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 446493510 169 SALD 172
Cdd:COG1245 241 SYLD 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-228 |
1.53e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELakaRQKIGMIFQGFN--LLKTV- 97
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL---QKLVSDEWQRNNtdMLSPGe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 98 -----TVYENIalplrLAGISKVEIEKRVEKYLRIVDLFTRKDAYpseLSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PRK10938 96 ddtgrTTAEII-----QDEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 173 PETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDI 228
Cdd:PRK10938 168 VASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-217 |
1.66e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 31 GEVFGIIGYSGAGKSTLIRCV--NLLEKPTTGNIIVNSQDLTtlsaKELAKarqKIGMIFQGFNLLKTVTVYENIA---- 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPT----KQILK---RTGFVTQDDILYPHLTVRETLVfcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 105 --LPLRLAGISKVEIEKRVekylrIVDLFTRK-------DAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPET 175
Cdd:PLN03211 167 lrLPKSLTKQEKILVAESV-----ISELGLTKcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493510 176 TDSILDLLLKINEEiGITILLITHE-MNVIQRICDRVAVMEHG 217
Cdd:PLN03211 242 AYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-229 |
2.00e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.45 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTL----IRCVNLLEkpttGNIIVNSQDLTTLSAKELakaRQKIGMIFQGfnllkt 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL---RSRLSIILQD------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 97 vtvyenialPLRLAGISKVEIE-------KRVEKYLRIVDLFTRKDAYPSEL-----------SGGQKQRVAIARALSHE 158
Cdd:cd03288 104 ---------PILFSGSIRFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 159 PEVLLSDEATSALDpETTDSILDLLLkINEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIF 229
Cdd:cd03288 175 SSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-219 |
4.28e-07 |
|
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: 50.62 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFTtkKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTL----IRCVNllekpTTGNIIVNSQDLTTLSAKEL 77
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 78 AKA----RQKIgMIFQGfNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPseLSGGQKQRVAIAR 153
Cdd:cd03289 76 RKAfgviPQKV-FIFSG-TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 154 ALSHEPEVLLSDEATSALDPeTTDSILDLLLKiNEEIGITILLITHEMNVIQRiCDRVAVMEHGAV 219
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDP-ITYQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-199 |
5.98e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 27 QVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTlsakelAKARQKIGMIFQGFNLLKTVTVYENIALp 106
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR------GDRSRFMAYLGHLPGLKADLSTLENLHF- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 107 lrLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARA-LSHEPEVLLsDEATSALDPETTdSILDLLLK 185
Cdd:PRK13543 106 --LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLDLEGI-TLVNRMIS 181
|
170
....*....|....
gi 446493510 186 INEEIGITILLITH 199
Cdd:PRK13543 182 AHLRGGGAALVTTH 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-207 |
1.84e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 36 IIGYSGAGKSTLIRCVNLL---EKPTTGNIIVNSQDLTTLSAKelakaRQKIGMIFQGFNLlKTVTVYENIALPLRLAGI 112
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEV-----RAQVKLAFENANG-KKYTITRSLAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 113 SKVEIEKRvekylrIVDLFTRkdaypseLSGGQKQ------RVAIARALSHEPEVLLSDEATSALDPETTD-SILDLLLK 185
Cdd:cd03240 101 HQGESNWP------LLDMRGR-------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEE 167
|
170 180
....*....|....*....|..
gi 446493510 186 INEEIGITILLITHEMNVIQRI 207
Cdd:cd03240 168 RKSQKNFQLIVITHDEELVDAA 189
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-200 |
2.80e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 3 ELKNVSKVFTTKKgnveALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCvnLLE--KPTTGNIIVNsqdlTTLSAKELAKA 80
Cdd:PRK11147 321 EMENVNYQIDGKQ----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHCG----TKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 81 RQkigmifqgfNLLKTVTVYENIAlplrlAGISKVEIEKR---VEKYLRivD-LFTRKDAY-P-SELSGGQKQRVAIARA 154
Cdd:PRK11147 391 RA---------ELDPEKTVMDNLA-----EGKQEVMVNGRprhVLGYLQ--DfLFHPKRAMtPvKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446493510 155 LSHEPEVLLSDEATSALDPETtdsiLDLLLKINEEIGITILLITHE 200
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-228 |
3.44e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnsqdlttlsakelaKARQKIGMIFQgFNLLKTVTVY 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISFSSQ-FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIalplrLAGISKVEIE-KRVEKYLRI---VDLFTRKDAYPS-----ELSGGQKQRVAIARALSHEPEVLLSDEATSAL 171
Cdd:cd03291 116 ENI-----IFGVSYDEYRyKSVVKACQLeedITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 172 DPETTDSILD---LLLKINEeigiTILLITHEMNVIqRICDRVAVMEHGAVVESGTVKDI 228
Cdd:cd03291 191 DVFTEKEIFEscvCKLMANK----TRILVTSKMEHL-KKADKILILHEGSSYFYGTFSEL 245
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-172 |
4.22e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNvskvFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLE---KPTTGNII-----VNSQDLTTL- 72
Cdd:PLN03073 178 IHMEN----FSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQILhveqeVVGDDTTALq 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 73 ----SAKELAKARQKIGMIFQGFNLLKTVTVYENIALPLRlAGISKVEIEKRVEKYLRIVDLFtrkDAYPSE-------- 140
Cdd:PLN03073 254 cvlnTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEIYKRLELI---DAYTAEaraasila 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493510 141 ---------------LSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PLN03073 330 glsftpemqvkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-234 |
6.74e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 13 TKKGNvEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKpTTGNIIVNSQDLTTLSAKELAKA----RQKIgMIF 88
Cdd:TIGR01271 1228 TEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAfgviPQKV-FIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 89 QGfNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPseLSGGQKQRVAIARALSHEPEVLLSDEAT 168
Cdd:TIGR01271 1305 SG-TFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 169 SALDPeTTDSILDLLLKiNEEIGITILLITHEMNVIQRiCDRVAVMEHGAVVESGTVKDIFTNPQH 234
Cdd:TIGR01271 1382 AHLDP-VTLQIIRKTLK-QSFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNETSL 1444
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-185 |
7.10e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 2 IELKNVSKVFttkkGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRC-VNLLEkPTTG--------NIIVNSQDlttl 72
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGtvkwsenaNIGYYAQD---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 73 SAKELAkarqkigmifqgfnllKTVTVYEnialplrlaGISKVEIEKRVEKYLRIV---DLFTRKDAYPS--ELSGGQKQ 147
Cdd:PRK15064 391 HAYDFE----------------NDLTLFD---------WMSQWRQEGDDEQAVRGTlgrLLFSQDDIKKSvkVLSGGEKG 445
|
170 180 190
....*....|....*....|....*....|....*...
gi 446493510 148 RVAIARALSHEPEVLLSDEATSALDPETTDSiLDLLLK 185
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIES-LNMALE 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-172 |
1.86e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIrcvNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKiGMIFQGFNLLKTVTVY 100
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRISGFPKKQETFARIS-GYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 101 ENIALP--LRLAG-ISKVEIEKRVEKYLRIVDLFTRKDA---YP--SELSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PLN03140 972 ESLIYSafLRLPKeVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-217 |
2.74e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 31 GEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI-IVNSQDLTTLSAKELAkarqkigmiFQGFNLLKTV------------ 97
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQDQFA---------FEEFTVLDTVimghtelwevkq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 98 ---TVYeniALPlrlagiskveiEKRVEKYLRIVDL---FTRKDAYP-----------------------SELSGGQKQR 148
Cdd:PRK15064 98 erdRIY---ALP-----------EMSEEDGMKVADLevkFAEMDGYTaearagelllgvgipeeqhyglmSEVAPGWKLR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493510 149 VAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeigiTILLITHEMNVIQRICDRVAVMEHG 217
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNSVCTHMADLDYG 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-214 |
6.57e-05 |
|
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: 43.89 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 28 VKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNI--------IVNS------QD-LTTLSAKELaKARQKIgmifQGFN 92
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEfrgselQNyFTKLLEGDV-KVIVKP----QYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 93 LL-KTV--TVYENIalplrlagiSKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATS 169
Cdd:cd03236 98 LIpKAVkgKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446493510 170 ALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVM 214
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-172 |
7.86e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIivnsqdlttlsakELAKArQKIGMIFQgfNLLKTVTVY 100
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKG-IKLGYFAQ--HQLEFLRAD 391
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493510 101 ENialPLR-LAGISKVEIEKRVEKYLRIVDLFTRKDAYPSE-LSGGQKQRVAIARALSHEPEVLLSDEATSALD 172
Cdd:PRK10636 392 ES---PLQhLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-227 |
8.65e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEeigiTILLITHEMNVIQRICDRVAVMEHGAVV 220
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
....*...
gi 446493510 221 E-SGTVKD 227
Cdd:PLN03073 704 PfHGTFHD 711
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
14-225 |
2.30e-04 |
|
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: 41.86 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 14 KKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLircvnllekpTTGNIIVNSQD--LTTLSAKelakARQKIGMI---- 87
Cdd:cd03270 4 RGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRryVESLSAY----ARQFLGQMdkpd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 88 ----------------FQGFNLLKTV-TVYEnIALPLRLAgISKVEIEKRVEKYLRI-VDLFTRKDAYPSeLSGGQKQRV 149
Cdd:cd03270 70 vdsieglspaiaidqkTTSRNPRSTVgTVTE-IYDYLRLL-FARVGIRERLGFLVDVgLGYLTLSRSAPT-LSGGEAQRI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 150 AIARALSHEPEVLLS--DEATSALDPETTDSILDLLLKInEEIGITILLITHEMNVIqRICDRVAVMEHGAVVESGTV 225
Cdd:cd03270 147 RLATQIGSGLTGVLYvlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTI-RAADHVIDIGPGAGVHGGEI 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-243 |
3.08e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 21 LKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNL----LEKPTTGNIIVNSqdlttLSAKELAKA-RQKIGMIFQGFNLLK 95
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDG-----ITPEEIKKHyRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 96 TVTVYENIALPLRLA-------GISKVE-IEKRVEKYLRIVDL-FTRKDAYPSEL----SGGQKQRVAIARALSHEPEVL 162
Cdd:TIGR00956 152 HLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLsHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 163 LSDEATSALDPETTDSILDLLLKINEEIGITILL-ITHEMNVIQRICDRVAVMEHGAVVESGT---VKDIFTN-----PQ 233
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPadkAKQYFEKmgfkcPD 311
|
250
....*....|
gi 446493510 234 HVTTKKFVNS 243
Cdd:TIGR00956 312 RQTTADFLTS 321
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
139-224 |
5.87e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 139 SELSGGQKQRVAIARALSHE---PEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIqRICDRVAVM- 214
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVI-KCADWIIDLg 245
|
90
....*....|....*
gi 446493510 215 -EHGA----VVESGT 224
Cdd:cd03271 246 pEGGDgggqVVASGT 260
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-199 |
8.05e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 33 VFGIIGYSGAGKSTLIRCVN--LLEKPTTGNIIVNsqDLTTLSAKE---------------------------LAKARQK 83
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRyaLYGKARSRSKLRS--DLINVGSEEasvelefehggkryrierrqgefaeflEAKPSER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 84 IGMIFQGFNLLKTVTVYEN---IALPLRLAGISKVEIEKRVEKYLRIVDLFTRkdayPSELSGGQKQRVAIARALShepe 160
Cdd:COG0419 103 KEALKRLLGLEIYEELKERlkeLEEALESALEELAELQKLKQEILAQLSGLDP----IETLSGGERLRLALADLLS---- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 446493510 161 vLLSDeaTSALDPETTDSILDLLlkinEEIGItillITH 199
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDAL----EELAI----ITH 202
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-183 |
1.36e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 1.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493510 139 SELSGGQKQR---VAIARALS----------HEPEVLLSDEATSALDPETTDSILDLL 183
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-211 |
1.82e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493510 139 SELSGGQKQRVAIARAL---SHEPEVLLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIqRICDRV 211
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV-KVADYV 881
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-206 |
4.44e-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: 37.34 E-value: 4.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493510 141 LSGGQKQRVAIARALSHE-----PEVLLsDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQR 206
Cdd:cd03227 78 LSGGEKELSALALILALAslkprPLYIL-DEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAEL 146
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-236 |
5.50e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 141 LSGGQKQRVAIARAL-SHEPEVL-LSDEATSALDPETTDSILDLLLKInEEIGITILLITHEMNVIqRICDRVAVM---- 214
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTI-RAADYVIDIgpga 566
|
90 100
....*....|....*....|....
gi 446493510 215 -EHGA-VVESGTVKDIFTNPQHVT 236
Cdd:TIGR00630 567 gEHGGeVVASGTPEEILANPDSLT 590
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
141-207 |
5.92e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 38.63 E-value: 5.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493510 141 LSGGQKQRVAIARAL------SHEPEV--LLSDEATSALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRI 207
Cdd:PRK10246 950 LSGGESFLVSLALALalsdlvSHKTRIdsLFLDEGFGTLDSETLDTALDALDALNAS-GKTIGVISHVEAMKERI 1023
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
27-217 |
9.14e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.86 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 27 QVKKGEVFGIIGYSGAGKSTLIRCVNLlekPTTGNIIVNSQDLTTLSAKELAKARQKIGMIFQGFNLLKTVTvyenialp 106
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITY---ALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKYRVE-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493510 107 lRLAGISKveiekrvEKYLRIV-------DLFTRKDAypSELSGGQKQRVAIARALSHEPEVLLS----------DEATS 169
Cdd:cd03279 93 -RSRGLDY-------DQFTRIVllpqgefDRFLARPV--STLSGGETFLASLSLALALSEVLQNRggarlealfiDEGFG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493510 170 ALDPETTDSILDLLLKINEEiGITILLITHEMNVIQRICDRVAVMEHG 217
Cdd:cd03279 163 TLDPEALEAVATALELIRTE-NRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| |
