|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-334 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 599.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKE 317
Cdd:COG1135 241 LPTVLNDELPEELLARLReaaGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
|
330
....*....|....*..
gi 2050094043 318 IQKALQHLRLQVQLKEV 334
Cdd:COG1135 321 IDAALAYLREQGVVVEV 337
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-326 |
0e+00 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 528.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ-----NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQ 315
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQaepttGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330
....*....|.
gi 2050094043 316 KEIQKALQHLR 326
Cdd:PRK11153 321 GDIQAAIAYLQ 331
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.71e-153 |
|
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: 430.08 E-value: 1.71e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-326 |
6.12e-130 |
|
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: 374.60 E-value: 6.12e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQ--IYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQ 315
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQatpFADSvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330
....*....|.
gi 2050094043 316 KEIQKALQHLR 326
Cdd:TIGR02314 321 QDTQAAIAYLQ 331
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
3.85e-107 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 312.70 E-value: 3.85e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITsLSAKELRKL 80
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAY-PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQN 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
....*
gi 2050094043 240 FVRSV 244
Cdd:COG1126 235 FLSKV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-244 |
4.24e-106 |
|
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: 319.93 E-value: 4.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYES-GGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK 79
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQS-FNLFNSR-TVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:COG1123 340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
....*....
gi 2050094043 236 TTQNFVRSV 244
Cdd:COG1123 500 YTRALLAAV 508
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
1.28e-102 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 300.81 E-value: 1.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHvVKEICHRVAVMEKGKVIEE 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
1.79e-100 |
|
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: 295.74 E-value: 1.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVHavEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-233 |
1.15e-95 |
|
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: 286.56 E-value: 1.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERP--TAGTISIDDKDITSLSAKEL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKLR-QRIGMIFQ-SFNLFNSR-TVFGNIAYPLRL-AKLPKNEIKERVNELLKFVGL---EDKANYYPEQLSGGQKQRVG 150
Cdd:COG0444 81 RKIRgREIQMIFQdPMTSLNPVmTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 2050094043 231 QPK 233
Cdd:COG0444 241 NPR 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
4.03e-95 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 281.56 E-value: 4.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
4.80e-95 |
|
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: 281.30 E-value: 4.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 -QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
9.01e-91 |
|
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: 270.92 E-value: 9.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQ-SFNLFN-SRTVFGNIAYPLRLAKLPKNE--IKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:cd03257 81 RKEIQMVFQdPMSSLNpRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-243 |
3.29e-90 |
|
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: 269.76 E-value: 3.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVHavEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03261 1 IELRGLTKSF--GGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGklfdvfTQPKTKTTQN- 239
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG------TPEELRASDDp 230
|
....
gi 2050094043 240 FVRS 243
Cdd:cd03261 231 LVRQ 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-245 |
6.84e-90 |
|
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: 269.37 E-value: 6.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKL 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQ----SFNLFnsRTVFGNIAYPLRLAKLPknEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:COG1124 78 RRRVQMVFQdpyaSLHPR--HTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|
gi 2050094043 236 TTQNFVRSVI 245
Cdd:COG1124 234 YTRELLAASL 243
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-244 |
2.89e-86 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 265.04 E-value: 2.89e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVY---------------------ESGGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTA 59
Cdd:COG4175 3 KIEVRNLYKIFgkrperalklldqgkskdeilEKTGQTV-GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 60 GTISIDDKDITSLSAKELRKLRQ-RIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYP 138
Cdd:COG4175 82 GEVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 139 EQLSGGQKQRVGIARALATSPDILICDEATSALDP----ETTTEILNLLKKVNReynlTILLITHEMHvvkE---ICHRV 211
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKLKK----TIVFITHDLD---EalrLGDRI 234
|
250 260 270
....*....|....*....|....*....|...
gi 2050094043 212 AVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:COG4175 235 AIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-227 |
1.43e-85 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 258.06 E-value: 1.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIaypL--RLAKLP---------KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNV---LagRLGRTStwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIeegklFD 227
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV-----FD 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
1.69e-85 |
|
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: 256.69 E-value: 1.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlSAKELRKLR 81
Cdd:cd03262 1 IEIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLA-KLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
5.27e-85 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 260.42 E-value: 5.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkELRkl 80
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHvvkE---ICHRVAVMEKGKVIEEGKLFDVFTQPKTKTT 237
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE---EalaLADRIAVMNDGRIEQVGTPEEIYERPATRFV 232
|
....
gi 2050094043 238 QNFV 241
Cdd:COG3842 233 ADFI 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
9.92e-85 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 256.55 E-value: 9.92e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelrkl 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1116 81 --DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEmhvVKE---ICHRVAVMEK--GKVIEE 222
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVLSArpGRIVEE 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-233 |
1.58e-84 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 258.51 E-value: 1.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKVYESGG-------QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKEL 77
Cdd:COG4608 11 RDLKKHFPVRGglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGREL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKLRQRIGMIFQ-SFNLFNSR-TVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIAR 153
Cdd:COG4608 91 RPLRRRMQMVFQdPYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-244 |
2.53e-84 |
|
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: 256.03 E-value: 2.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 10 VYESGGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR-QRIGMIF 88
Cdd:cd03294 30 ILKKTGQTV-GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 QSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:cd03294 109 QSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 169 SALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
4.01e-83 |
|
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: 251.48 E-value: 4.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKLR 81
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQsfN----LFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:COG1122 75 RKVGLVFQ--NpddqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
6.73e-82 |
|
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: 247.43 E-value: 6.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklR 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-222 |
2.09e-81 |
|
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: 246.61 E-value: 2.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelrklr 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03293 74 -DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEK--GKVIEE 222
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-225 |
5.52e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 241.12 E-value: 5.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKLR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKL 225
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.91e-77 |
|
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: 245.97 E-value: 1.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgqSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTA---GTISIDDKDITSLSAKEL 77
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKlrqRIGMIFQSF-NLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:COG1123 82 GR---RIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
3.43e-77 |
|
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: 236.70 E-value: 3.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNI-----AY--PLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIAR 153
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgrlGRrsTWRsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
2.68e-76 |
|
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: 235.42 E-value: 2.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQsF---NLFnSRTVFGNIAY-PLRLaKLPKNEIKERVNELLKFVGLEDKanYY---PEQLSGGQKQRVGIAR 153
Cdd:TIGR04521 81 RKKVGLVFQ-FpehQLF-EETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEE--YLersPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
1.09e-74 |
|
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: 229.28 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 3 SFNNISKVYESGGQSvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrq 82
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIGMIFQSFN--LFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03225 76 KVGLVFQNPDdqFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
1.37e-73 |
|
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: 227.57 E-value: 1.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPlRLAKLP---------KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGI 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHG-RLGYKPtwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-244 |
1.47e-73 |
|
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: 236.50 E-value: 1.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTL----LRLVnmlerPTAGTISIDDKDITSLSAKELRKLRQRIGMIFQS-FN 92
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 93 LFNSR-TVFGNIAYPLRL--AKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:COG4172 374 SLSPRmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 169 SALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-245 |
7.55e-73 |
|
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: 225.86 E-value: 7.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSL--------- 72
Cdd:TIGR03005 1 VRFSDVTKRFGI----LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMpgrngplvp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 73 -SAKELRKLRQRIGMIFQSFNLFNSRTVFGNIAY-PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVG 150
Cdd:TIGR03005 77 aDEKHLRQMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
|
250
....*....|....*
gi 2050094043 231 QPKTKTTQNFVRSVI 245
Cdd:TIGR03005 237 QPKEERTREFLSKVI 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-241 |
2.08e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 228.03 E-value: 2.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG3839 75 R-NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDP----ETTTEIlnllKKVNREYNLTILLITHEMHvvkE---ICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:COG3839 154 VFLLDEPLSNLDAklrvEMRAEI----KRLHRRLGTTTIYVTHDQV---EamtLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
....*...
gi 2050094043 234 TKttqnFV 241
Cdd:COG3839 227 NL----FV 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
2.31e-72 |
|
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: 225.39 E-value: 2.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitSLSAKELRKLR 81
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMhvvKEI--CHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDM---EEAvlADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-234 |
3.96e-72 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 227.34 E-value: 3.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI-TSLSAKElrkl 80
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1118 75 R-RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPAT 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
8.73e-72 |
|
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: 231.88 E-value: 8.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERPTA---GTISIDDKDITSLSAKE 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 77 LRKLR-QRIGMIFQ----SFN-LFnsrTVFGNIAYPLRL-AKLPKNEIKERVNELLKFVGL---EDKANYYPEQLSGGQK 146
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtSLNpLH---TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
....*..
gi 2050094043 227 DVFTQPK 233
Cdd:COG4172 243 ELFAAPQ 249
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-243 |
3.89e-71 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 221.60 E-value: 3.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDIT---------- 70
Cdd:COG4598 8 ALEVRDLHKSF--GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 71 SLSAKELRKLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG4598 84 PADRRQLQRIRTRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVF 229
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....
gi 2050094043 230 TQPKTKTTQNFVRS 243
Cdd:COG4598 243 GNPKSERLRQFLSS 256
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
6.05e-71 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 220.65 E-value: 6.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI---TSLSAKELR 78
Cdd:COG4161 3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNrEYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLfDVFTQPKTKTT 237
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236
|
....*
gi 2050094043 238 QNFVR 242
Cdd:COG4161 237 AHYLS 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
6.68e-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: 218.21 E-value: 6.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesgGQsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSaKELRKLR 81
Cdd:cd03229 1 LELKNVSKRY---GQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPlrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
1.94e-70 |
|
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: 218.43 E-value: 1.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
3.43e-69 |
|
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: 215.51 E-value: 3.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKE 76
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 77 LRkLRQRIGMIFQSFNLFNSrTVFGNIAYPLRLA-KLPKNEIKERVNELLKFVGLED--KANYYPEQLSGGQKQRVGIAR 153
Cdd:cd03260 77 LE-LRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
3.71e-69 |
|
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: 215.95 E-value: 3.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklR 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-240 |
6.43e-69 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 215.65 E-value: 6.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI---TSLSAKELR 78
Cdd:PRK11124 3 IQLNGINCFYGAH-QALF---DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLfDVFTQPKTKTT 237
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAF 236
|
...
gi 2050094043 238 QNF 240
Cdd:PRK11124 237 KNY 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-245 |
3.24e-68 |
|
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: 213.70 E-value: 3.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDK--ANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:cd03295 76 -KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTkttqN 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN----D 230
|
....*.
gi 2050094043 240 FVRSVI 245
Cdd:cd03295 231 FVAEFV 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-244 |
9.04e-68 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 212.65 E-value: 9.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesgGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElRKL 80
Cdd:PRK09493 1 MIEFKNVSKHF---GPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAY-PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQN 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
....*
gi 2050094043 240 FVRSV 244
Cdd:PRK09493 235 FLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-247 |
5.52e-67 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 210.76 E-value: 5.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYEsgGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDIT---SLSAKE- 76
Cdd:PRK11264 3 AIEVKNLVKKFH--GQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarSLSQQKg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 77 -LRKLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK11264 79 lIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
250
....*....|...
gi 2050094043 235 KTTQNFVRSVIND 247
Cdd:PRK11264 238 PRTRQFLEKFLLQ 250
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
1.16e-66 |
|
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: 209.21 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPknEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEE 222
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
4.12e-66 |
|
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: 208.74 E-value: 4.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRkl 80
Cdd:COG0411 4 LLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNI-------------AYPLRLAKLPKNE--IKERVNELLKFVGLEDKANYYPEQLSGGQ 145
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 146 KQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
4.03e-65 |
|
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: 205.65 E-value: 4.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklR 81
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QrIGMIFQSFNLFNSRTVFGNIAYPLRLAK----LPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:cd03296 75 N-VGFVFQHYALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTT 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 2050094043 238 QNFV 241
Cdd:cd03296 234 YSFL 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-233 |
8.47e-64 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 202.28 E-value: 8.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklRQRIG 85
Cdd:cd03219 5 GLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIFQSFNLFNSRTVFGNIA--------YPLRLAKLPKNE--IKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMvaaqartgSGLLLARARREEreARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
1.41e-63 |
|
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: 202.01 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitslSAKELRKL 80
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-219 |
8.49e-62 |
|
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: 196.32 E-value: 8.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklrQRIG 85
Cdd:cd03301 5 NVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-227 |
7.63e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 194.59 E-value: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVHAvedvTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElRKl 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqrIGMIFQSFNLFNSRTVFGNIAYPLRLA-KLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG3840 73 ---VSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG---KLFD 227
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGptaALLD 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-241 |
1.19e-60 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 194.87 E-value: 1.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVN-MLER-PTA---GTISIDDKDITSLSAkELRKLRQRIGMIFQSFNL 93
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDLiPGArveGEILLDGEDIYDPDV-DVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FnSRTVFGNIAYPLRLA-KLPKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:COG1117 104 F-PKSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 169 SALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:COG1117 183 SALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-241 |
6.32e-60 |
|
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: 192.17 E-value: 6.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklRQRIGMIFQSFNLFNSRTVF 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-241 |
2.72e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 191.82 E-value: 2.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGG-----QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK 75
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 76 ELRKLRQRIGMIFQ-SFNLFNSR-TVFGNIAYPLR-LAKLPKNEIKERVNELLKFVGLEDK-ANYYPEQLSGGQKQRVGI 151
Cdd:PRK10419 83 QRKAFRRDIQMVFQdSISAVNPRkTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV--F 229
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltF 242
|
250
....*....|..
gi 2050094043 230 TQPKTKTTQNFV 241
Cdd:PRK10419 243 SSPAGRVLQNAV 254
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
3.83e-59 |
|
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: 189.64 E-value: 3.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsakELRKLR 81
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-219 |
4.12e-59 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 189.46 E-value: 4.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRL-AKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEmHVVKEICHRVAVMEKGKV 219
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-243 |
4.41e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 191.20 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKVYESGG-----QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRK 79
Cdd:COG4167 8 RNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQ-SFNLFNSRTVFGNI-AYPLRLA-KLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:COG4167 85 RCKHIRMIFQdPNTSLNPRLNIGQIlEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:COG4167 165 ILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHE 244
|
....*...
gi 2050094043 236 TTQNFVRS 243
Cdd:COG4167 245 VTKRLIES 252
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
1.13e-58 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 190.61 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRKLR 81
Cdd:PRK13635 6 IRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
1.30e-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: 189.48 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKl 80
Cdd:COG1120 1 MLEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQS----FNLfnsrTVF-----GNIAYPLRLAKLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGI 151
Cdd:COG1120 76 --RIAYVPQEppapFGL----TVRelvalGRYPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-244 |
1.34e-58 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 191.84 E-value: 1.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 16 QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQRIGMIFQS-FNLF 94
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDpLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 NSRTVFGNI-AYPLRL--AKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK15079 112 NPRMTIGEIiAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 171 LDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-234 |
1.12e-57 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 188.33 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKeLRKL 80
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQ--SFNLFnSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL--EDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13637 82 RKKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-263 |
1.41e-57 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 190.82 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYEsgGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelrkL 80
Cdd:PRK11607 19 LLEIRNLTKSFD--GQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-----Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPE----TTTEILNLLKKVnreyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKT 236
Cdd:PRK11607 170 LLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
250 260
....*....|....*....|....*..
gi 2050094043 237 TQNFVRSVindHLPESVLAKIQNGGQI 263
Cdd:PRK11607 246 SAEFIGSV---NVFEGVLKERQEDGLV 269
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-238 |
4.18e-57 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 187.86 E-value: 4.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYE------SGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK 79
Cdd:PRK11308 10 DLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQS-FNLFNSRTVFGNI-AYPLRL-AKLPKNEIKERVNELLKFVGLE-DKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK11308 90 LRQKIQIVFQNpYGSLNPRKKVGQIlEEPLLInTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHP 249
|
...
gi 2050094043 236 TTQ 238
Cdd:PRK11308 250 YTQ 252
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.81e-56 |
|
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: 182.95 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLR 81
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-244 |
1.95e-56 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 188.32 E-value: 1.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR-QRIGMIFQSFNLFNSRT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 99 VFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
3.04e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.98 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakelRKL 80
Cdd:COG1121 6 AIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNlFNSR---TVF-----GNIAYpLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIA 152
Cdd:COG1121 74 RRRIGYVPQRAE-VDWDfpiTVRdvvlmGRYGR-RGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGkVIEEGKLFDVFTQP 232
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPE 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
3.92e-56 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 182.00 E-value: 3.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNReYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-242 |
4.94e-56 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 182.86 E-value: 4.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSL----------SAKELRKLRQRIGMIFQSFNL 93
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FNSRTVFGNI-AYPLRLAKLPKNEIKERVNELLKFVGLEDKAN-YYPEQLSGGQKQRVGIARALATSPDILICDEATSAL 171
Cdd:PRK10619 104 WSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 172 DPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVR 242
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-269 |
5.66e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 185.67 E-value: 5.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklr 81
Cdd:PRK10851 3 IEIANIKKSF--GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLakLPKNE------IKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
250 260 270
....*....|....*....|....*....|....*
gi 2050094043 236 TTQNFVRSVinDHLPESVL-AKIQNGGQIYRLTFT 269
Cdd:PRK10851 232 FVLEFMGEV--NRLQGTIRgGQFHVGAHRWPLGYT 264
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-329 |
7.01e-56 |
|
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: 185.69 E-value: 7.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQR-IGMIFQSFNLFNSRTVFG 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRrIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLAklPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILN 181
Cdd:COG4148 97 NLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 182 LLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF--VRSVIN----DHLPESVLA 255
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGeeAGSVLEatvaAHDPDYGLT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 256 KIQNGGQIYRLTFTGEETGQPVLSYIAKNynvDV-------------NVLYGNIIELQNVLFGNLLVELQ-GEQK---EI 318
Cdd:COG4148 255 RLALGGGRLWVPRLDLPPGTRVRVRIRAR---DVslaleppegssilNILPGRVVEIEPADGGQVLVRLDlGGQTllaRI 331
|
330
....*....|..
gi 2050094043 319 -QKALQHLRLQV 329
Cdd:COG4148 332 tRRSADELGLAP 343
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
2.14e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 181.60 E-value: 2.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqriGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITH 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
2.62e-55 |
|
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: 177.97 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLR 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIayplrlaklpkneikervnellkfvgledkanyypeQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
6.85e-55 |
|
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: 190.43 E-value: 6.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:COG2274 474 IELENVSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIAyplrLAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENIT----LGDPDATD--EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKeICHRVAVMEKGKVIEEG 223
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
7.56e-55 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 183.61 E-value: 7.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklr 81
Cdd:PRK09452 15 VELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QR-IGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK09452 85 NRhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARF 244
|
.
gi 2050094043 241 V 241
Cdd:PRK09452 245 I 245
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
1.32e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.70 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFNLFnSRTVFGNIAYPLRLAKLPKNEikERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSPD 160
Cdd:COG4619 75 -QVAYVPQEPALW-GGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-231 |
1.71e-54 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 179.90 E-value: 1.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESG--GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitSLSAKELR 78
Cdd:PRK13633 4 MIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQS-FNLFNSRTVFGNIAY-PLRLAKLPKnEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFgPENLGIPPE-EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
2.43e-53 |
|
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: 172.95 E-value: 2.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNsRTVFGNIayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03228 76 KNIAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKeICHRVAVMEKGK 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.55e-52 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 174.41 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslSAKELRKL 80
Cdd:PRK13632 7 MIKVENVSFSY--PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEM-HVVKeiCHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-219 |
2.80e-52 |
|
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: 171.95 E-value: 2.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 3 SFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakelRKLRQ 82
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIGMIFQSFNL-FNSR-TVFGNIA----YPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:cd03235 69 RIGYVPQRRSIdRDFPiSVRDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
3.99e-52 |
|
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: 169.37 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsaKELRKLRQRIGMIFQSFNLFNSRTVF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 101 GNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKAN----YYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
4.21e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 180.75 E-value: 4.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:COG1132 340 IEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFNLFnSRTVFGNIAYplrlAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG1132 415 -QIGVVPQDTFLF-SGTIRENIRY----GRPDATD--EEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
8.24e-52 |
|
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: 170.45 E-value: 8.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsvHAVEDVTLSVEKGeIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLR 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
6.61e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 170.30 E-value: 6.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRKL 80
Cdd:PRK13650 4 IIEVKNLTFKYKED-QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKeICHRVAVMEKGKV 219
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
9.38e-51 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 175.99 E-value: 9.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNML---ERPTAGTISIDDKDITSLSAKEL 77
Cdd:COG3845 5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTL---MKILyglYQPDSGEILIDGKPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKLRqrIGMIFQSFNLFNSRTVFGNIAY---PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:COG3845 78 IALG--IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.02e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 169.55 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsaKELRKL 80
Cdd:PRK13648 7 IIVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHrVAVMEKGKVIEEGKLFDVF 229
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-223 |
2.11e-50 |
|
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: 167.09 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 30 KGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK-ELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLR 108
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 109 laKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNR 188
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 2050094043 189 EYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
3.82e-50 |
|
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: 166.39 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKL 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-287 |
4.52e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 168.75 E-value: 4.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakelRKL 80
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIG-----------MifqsfnlfnsrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG4152 70 RRRIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTteilNLLKKVNREYNL---TILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNV----ELLKDVIRELAAkgtTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 227 DVFTQPKTKTtqnFVRSVIND-----HLPESVLAKIQNGGqiYRLTFTGEETGQPVLSYIAKNYNV 287
Cdd:COG4152 215 EIRRQFGRNT---LRLEADGDagwlrALPGVTVVEEDGDG--AELKLEDGADAQELLRALLARGPV 275
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
5.61e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 167.95 E-value: 5.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItSLSAKELRKL 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFN--LFnSRTVFGNIAY-PLRLaKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK13639 77 RKTVGIVFQNPDdqLF-APTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-223 |
3.47e-49 |
|
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: 162.60 E-value: 3.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLrqrigmifqsfnlfnsrtvf 100
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 gnIAYplrlaklpkneikerVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:cd03214 75 --IAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-240 |
1.61e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 166.43 E-value: 1.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYesgGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsakelRKLRQR-I 84
Cdd:PRK11432 11 NITKRF---GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 85 GMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
3.07e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 163.65 E-value: 3.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITS-LSAKELRKLRQRIGMIFQ--SFNLFnS 96
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQfpEHQLF-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 97 RTVFGNIAY-PLRLAkLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:PRK13634 101 ETVEKDICFgPMNFG-VSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
4.69e-48 |
|
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: 158.95 E-value: 4.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 3 SFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLRQ 82
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIGMIFQsfnlfnsrtvfgniayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDIL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-225 |
4.80e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 161.52 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQR- 83
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 84 IGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEGKL 225
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-273 |
5.68e-48 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 170.42 E-value: 5.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKST----LLRLVNMlerpTAGTISIDDKDITSLSAKELRKLRQRIGMIFQS--F 91
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 92 NLFNSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGLE-DKANYYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 170 ALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV-IND- 247
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVpVADp 572
|
250 260
....*....|....*....|....*...
gi 2050094043 248 --HLPESVLAKIQNGGQIYRltfTGEET 273
Cdd:PRK10261 573 srQRPQRVLLSDDLPSNIHL---RGEEV 597
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
1.69e-47 |
|
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: 168.41 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:COG4987 334 LELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNiaypLRLAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG4987 409 RRIAVVPQRPHLFDT-TLREN----LRLARPDATD--EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKV--NReynlTILLITHEMHVVkEICHRVAVMEKGKVIEEGK 224
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGR----TVLLITHRLAGL-ERMDRILVLEDGRIVEQGT 552
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
2.65e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 161.17 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItSLSAKELRKLRQRIGMIFQS--FNLFnS 96
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDpdNQLF-S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 97 RTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETT 176
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 177 TEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-319 |
6.91e-47 |
|
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: 162.20 E-value: 6.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK-ELRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLAKLPKNEIK-ERVNELLkfvGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSVIN-----DHLPESVLA 255
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIegvvaEHDQHYGLT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 256 KIQNGGQIYRLTFTGEETGQPVLSYIAKNynvDV-------------NVLYGNIIELQNVLFGNLLVELQGEQKEIQ 319
Cdd:TIGR02142 252 ALRLGGGHLWVPENLGPTGARLRLRVPAR---DVslalqkpeatsirNILPARVVEIEDSDIGRVGVVLESGGKTLW 325
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-233 |
9.22e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 159.95 E-value: 9.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVH-AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA-KELRK 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQ--SFNLFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLE-DKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
1.04e-46 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 167.59 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK10535 84 RrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEiCHRVAVMEKGKVI 220
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-256 |
2.27e-46 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 159.91 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS----TLLRLVNMLERPTAGTISIDDKDITSLSAKE 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 77 LRKL-RQRIGMIFQ----SFNlfNSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGLEDKA---NYYPEQLSGGQKQ 147
Cdd:PRK11022 83 RRNLvGAEVAMIFQdpmtSLN--PCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFD 227
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260
....*....|....*....|....*....
gi 2050094043 228 VFTQPKTKTTQNFVRSvindhLPESVLAK 256
Cdd:PRK11022 241 IFRAPRHPYTQALLRA-----LPEFAQDK 264
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-255 |
6.79e-46 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 156.87 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKV--YESG---GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRK 79
Cdd:PRK15112 8 RNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQ-SFNLFNSRTVFGNIA-YPLRL-AKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK15112 85 RSQRIRMIFQdPSTSLNPRQRISQILdFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHE 244
|
250 260
....*....|....*....|
gi 2050094043 236 TTqnfvRSVINDHLPESVLA 255
Cdd:PRK15112 245 LT----KRLIAGHFGEALTA 260
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-224 |
8.14e-46 |
|
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: 155.28 E-value: 8.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELrkLRQRIGMIFQSFNLFNSR 97
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 TVFGNiaypLRLA--KLPKNEIKERVNELLK-FVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:cd03224 91 TVEEN----LLLGayARRRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2050094043 175 TTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:cd03224 167 IVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
1.15e-45 |
|
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: 154.68 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklR 81
Cdd:cd03268 1 LKTNDLTKTY--GKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKneikERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
1.56e-45 |
|
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: 163.01 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNsrtvfGNIAYPLRLAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG4988 411 RQIAWVPQNPYLFA-----GTIRENLRLGRPDASD--EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
4.43e-45 |
|
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: 153.93 E-value: 4.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNIAYplrlAKLPKNEikERVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVG 150
Cdd:cd03253 75 RAIGVVPQDTVLFND-TIGYNIRY----GRPDATD--EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-238 |
7.49e-45 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 160.64 E-value: 7.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKST----LLRLVNmlerpTAGTISIDDKDITSLSAKELRKLRQRIGMIFQSFN-L 93
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FNSR-TVFGNIAYPLRL--AKLPKNEIKERVNELLKFVGLEDKANY-YPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK15134 375 LNPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 170 ALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQ 238
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-291 |
9.71e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 155.63 E-value: 9.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVY-----ESGG------------QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIS 63
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 64 IDDKDITslsaKELRKLRQRIGMIF-------------QSFNLFnsRTVFGniayplrlakLPKNEIKERVNELLKFVGL 130
Cdd:COG4586 81 VLGYVPF----KRRKEFARRIGVVFgqrsqlwwdlpaiDSFRLL--KAIYR----------IPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 131 EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHR 210
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 211 VAVMEKGKVIEEG---KLFDVFTQPKTkttqnfVRSVINDHLPESVLAK----IQNGGQIYRLTFTGEETGQPVLSYIAK 283
Cdd:COG4586 225 VIVIDHGRIIYDGsleELKERFGPYKT------IVLELAEPVPPLELPRggevIEREGNRVRLEVDPRESLAEVLARLLA 298
|
....*....
gi 2050094043 284 NYNV-DVNV 291
Cdd:COG4586 299 RYPVrDLTI 307
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
1.83e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.03 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1129 4 LLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFNSRTVFGNIA---YPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:COG1129 80 --GIAIIHQELNLVPNLSVAENIFlgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 158 SPDILICDEATSALDPEtttEILNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG1129 158 DARVLILDEPTASLTER---EVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-223 |
2.22e-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: 151.28 E-value: 2.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakelrklR 81
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 162 LICDEATSALDPETTteilNLLKKVNREY---NLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03269 150 LILDEPFSGLDPVNV----ELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-250 |
3.14e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 152.98 E-value: 3.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA-KELRK 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQ--SFNLFnSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13649 83 IRKKVGLVFQfpESQLF-EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ----- 231
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfle 240
|
250 260
....*....|....*....|....*..
gi 2050094043 232 ------PK-TKTTQNFVRSVIN-DHLP 250
Cdd:PRK13649 241 ekqlgvPKiTKFAQRLADRGISfSSLP 267
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-253 |
9.49e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 151.88 E-value: 9.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:PRK13640 6 VEFKHVSFTYPD--SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEGKLFDVFtqPKTKTTQN- 239
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF--SKVEMLKEi 240
|
250 260
....*....|....*....|....*
gi 2050094043 240 -----FVRSVIND------HLPESV 253
Cdd:PRK13640 241 gldipFVYKLKNKlkekgiSVPQEI 265
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-245 |
9.58e-44 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 153.85 E-value: 9.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIK---GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqR-IGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK11650 76 --RdIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHE----MhvvkEICHRVAVMEKGkVIEE-GKLFDVFTQPKT 234
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqveaM----TLADRVVVMNGG-VAEQiGTPVEVYEKPAS 228
|
250
....*....|.
gi 2050094043 235 KttqnFVRSVI 245
Cdd:PRK11650 229 T----FVASFI 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-241 |
1.16e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 150.83 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSF 91
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRR---RVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 92 NLFNSRTVFGNIAYPLRLAKLPKN--EIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREynLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
3.14e-43 |
|
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: 146.80 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLR 81
Cdd:cd03216 1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQsfnlfnsrtvfgniayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-223 |
4.76e-43 |
|
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: 148.53 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLr 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qrIGMIFQSFNLFNSrTVFGNIAYPLRlaklpkNEIKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:cd03251 78 --IGLVSQDVFLFND-TVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-236 |
1.17e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 148.98 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakELRKL 80
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNL-FNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13644 76 RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITH---EMHVVKeichRVAVMEKGKVIEEGKLFDVFTQPKTKT 236
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHnleELHDAD----RIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-241 |
1.69e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 147.68 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKELRkLRQRIGMIFQSFNL 93
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FNSRTVFGNIAYPLRLAKL--PKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEA 167
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 168 TSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-233 |
1.87e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 148.82 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITS-LSAKELRK 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQ--SFNLFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
2.48e-42 |
|
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: 146.10 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklrQRIGMIFQSFNLFNSRTVFGN 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 103 IAyplrLAKLP----KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:cd03298 91 VG----LGLSPglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
3.35e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.41 E-value: 3.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakelRKLR 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
3.44e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 148.31 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSV-HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI---DDKDITSLSAKE- 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 77 -----------------LRKLRQRIGMIFQ--SFNLFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANY 136
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 137 YPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEK 216
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|..
gi 2050094043 217 GKVIEEGKLFDV 228
Cdd:PRK13651 241 GKIIKDGDTYDI 252
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-244 |
3.68e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 148.90 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLE---RPTAGTISIDDKDITSLSAKELRKL-RQRIGMIFQ--S 90
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKIiGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 91 FNLFNSRTVFGNI--AYPLRLAKLP----KNEIKERVNELLKFVGLED-KA--NYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:COG4170 100 SCLDPSAKIGDQLieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDhKDimNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259
|
...
gi 2050094043 242 RSV 244
Cdd:COG4170 260 RSM 262
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-233 |
5.94e-42 |
|
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: 145.69 E-value: 5.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELrklrqrigMIFQSFNLFNSRTVF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLR--LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV-FTQPK 233
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-232 |
7.40e-42 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 148.33 E-value: 7.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERP--TAGTISIDDKDITSLSAKELRKLR-QRIGMIFQ---- 89
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRaEQISMIFQdpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 90 SFNLFnsRTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLED---KANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:PRK09473 109 SLNPY--MRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
7.90e-42 |
|
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: 145.04 E-value: 7.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkLR 81
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNIAYPLRLAKlpkneiKERVNELLKFVGLEDKANYYP-----------EQLSGGQKQRVG 150
Cdd:cd03245 78 RNIGYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
8.19e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 148.07 E-value: 8.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVY-ESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI---------- 69
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 70 ---TSLSAKELRKLRQRIGMIFQ--SFNLFNSrTVFGNIAY-PLRLaKLPKNEIKERVNELLKFVGL-EDKANYYPEQLS 142
Cdd:PRK13631 101 tnpYSKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 143 GGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250 260
....*....|....*....|....*....
gi 2050094043 223 GKLFDVFTQP----KTKTTQNFVRSVIND 247
Cdd:PRK13631 258 GTPYEIFTDQhiinSTSIQVPRVIQVIND 286
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
9.23e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 145.17 E-value: 9.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:COG1137 3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGM--------IFQsfNLfnsrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIA 152
Cdd:COG1137 75 RARLGIgylpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTIlLITHemHVVKE---ICHRVAVMEKGKVIEEG 223
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGV-LITD--HNVREtlgICDRAYIISEGKVLAEG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
1.57e-41 |
|
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: 151.49 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSV-HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI---DD-KDITSLSAK 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEwVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 76 ELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLRLaKLPKNEIKERVNELLKFVGLEDKA-----NYYPEQLSGGQKQRVG 150
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-223 |
2.34e-41 |
|
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: 143.79 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL-LRLVNMLErPTAGTISIDDKDITSLSakeLRKL 80
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLlLALFRLVE-LSSGSILIDGVDISKIG---LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFnSRTVFGNIA----YP-------LRLAKLpkneiKERVNELLKfvGLEDKANYYPEQLSGGQKQRV 149
Cdd:cd03244 77 RSRISIIPQDPVLF-SGTIRSNLDpfgeYSdeelwqaLERVGL-----KEFVESLPG--GLDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLkkvnREY--NLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTI----REAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-235 |
6.18e-41 |
|
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: 143.07 E-value: 6.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklRQRIG 85
Cdd:cd03218 5 NLSKRY--GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIF--QSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
1.07e-40 |
|
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: 142.36 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFNLFnSRTVFGNIayplrlaKLPKNEIK-ERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRV 149
Cdd:cd03254 78 -MIGVVLQDTFLF-SGTIMENI-------RLGRPNATdEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-223 |
1.26e-40 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 143.37 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:PRK11831 104 NVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
1.63e-40 |
|
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: 141.91 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNMLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:cd03249 1 IEFKNVSFRYPSR-PDVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERfydPTSGEILLDGVDIRDLN---LR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQSFNLFNsRTVFGNIAYPLRLAKLPKNEIKERVNELLKFV-GLEDKanYYPE------QLSGGQKQRVGI 151
Cdd:cd03249 74 WLRSQIGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDG--YDTLvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
1.63e-40 |
|
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: 141.24 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 7 ISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslSAKELRKlrqRIGM 86
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRK---SIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 87 IFQS--FNLFnSRTVFGNiaypLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:cd03226 76 VMQDvdYQLF-TDSVREE----LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.70e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 143.40 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggqSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK13652 3 LIETRDLCYSYSG---SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqrIGMIFQSFN--LFnSRTVFGNIAY-PLRLAkLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK13652 80 ---VGLVFQNPDdqIF-SPTVEQDIAFgPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
1.85e-40 |
|
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: 141.85 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNsRTVFGNIAYPLRLAKLpkneikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:cd03252 76 RQVGVVLQENVLFN-RSIRDNIALADPGMSM------ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-223 |
2.07e-40 |
|
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: 141.66 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesgGQSvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLeRPTAGTISIDDKDITSLSAKELrk 79
Cdd:COG0410 3 MLEVENLHAGY---GGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQSFNLFNSRTVFGNI---AYPLRLAKLPKnEIKERVNELlkFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLllgAYARRDRAEVR-ADLERVYEL--FPRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-201 |
2.32e-40 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 142.15 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:PRK11248 1 MLQISHLYADY--GGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqriGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11248 73 ----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEM 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-243 |
2.48e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 148.31 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERP----TAGTISIDDKDITSLSAK 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 76 ELRKLR-QRIGMIFQ----SFNLFNsrTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLEDKA---NYYPEQLSGGQK 146
Cdd:PRK15134 85 TLRGVRgNKIAMIFQepmvSLNPLH--TLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*..
gi 2050094043 227 DVFTQPKTKTTQNFVRS 243
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNS 259
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
4.10e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 141.45 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKELrKLRQRIGMIFQSFNLF 94
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV-DLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 nSRTVFGNIAYPLRLAKLP-KNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK14239 99 -PMSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 170 ALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-224 |
4.71e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.87 E-value: 4.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYEsggqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrkl 80
Cdd:PRK10771 1 MLKLTDITWLYH------HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rQR-IGMIFQSFNLFNSRTVFGNIA---YP-LRLaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK10771 70 -RRpVSMLFQENNLFSHLTVAQNIGlglNPgLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-228 |
5.11e-40 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 140.99 E-value: 5.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVY------------------ESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTI 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 63 SIDDKdITSLSAkelrklrqrIGMIFQsfnlfNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKAN----YYp 138
Cdd:COG1134 84 EVNGR-VSALLE---------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 139 eqlSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|
gi 2050094043 219 VIEEGKLFDV 228
Cdd:COG1134 224 LVMDGDPEEV 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
1.23e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 140.61 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQS-VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelRK 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE---YK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQ------SFNLfnsrTVFGN--IAY------PLRLAKLPKN--EIKERVNEL-LkfvGLEDKANYYPEQLS 142
Cdd:COG1101 78 RAKYIGRVFQdpmmgtAPSM----TIEENlaLAYrrgkrrGLRRGLTKKRreLFRELLATLgL---GLENRLDTKVGLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 143 GGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-241 |
1.50e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 140.18 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYESGGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK------DITSLSAKelrK 79
Cdd:PRK14246 12 NISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAI---K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLP-KNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREynLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
....*..
gi 2050094043 235 KTTQNFV 241
Cdd:PRK14246 246 ELTEKYV 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
5.95e-39 |
|
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: 135.81 E-value: 5.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03246 76 DHVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-230 |
1.06e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 138.99 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITS--LSAKELR 78
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQ--SFNLFNSrTVFGNIAY-PLRLAKlPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGE-NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
1.34e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 139.97 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsakELRKLR 81
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV 228
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-224 |
1.84e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 137.43 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELrklrQRIGMI--FQSFNLFNSR 97
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI----ARMGVVrtFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 TVFGN--IAYPLR--------LAKLP-----KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDIL 162
Cdd:PRK11300 96 TVIENllVAQHQQlktglfsgLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-223 |
3.90e-38 |
|
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: 143.04 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLvnmLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:COG5265 358 VRFENVSFGYDPERPILK---GVSFEVPAGKTVAIVGPSGAGKSTLARL---LFRfydVTSGRILIDGQDIRDVT---QA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQSFNLFNSrTVFGNIAYP------------LRLA-------KLPK---NEIKERvnellkfvGLedkany 136
Cdd:COG5265 429 SLRAAIGIVPQDTVLFND-TIAYNIAYGrpdaseeeveaaARAAqihdfieSLPDgydTRVGER--------GL------ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 137 ypeQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEK 216
Cdd:COG5265 494 ---KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEA 567
|
....*..
gi 2050094043 217 GKVIEEG 223
Cdd:COG5265 568 GRIVERG 574
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-223 |
4.27e-38 |
|
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: 143.56 E-value: 4.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIA--YPLRLaklpkneikERVNELLKFVGLEDKANYYP-----------EQLSGGQKQR 148
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAggAPLTL---------DEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQR 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 149 VGIARALATSPDILICDEATSALDPETTTEILNLLKKVnreyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-222 |
7.77e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 134.91 E-value: 7.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEE 222
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-223 |
2.42e-37 |
|
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: 140.62 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNMLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYT---LA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQSFNLFNSrTVFGNIAYPlRLAKLPKNEIKERVNE--LLKFV-----GLEDKANYYPEQLSGGQKQRVGI 151
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAAayAQDFVdklplGLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-229 |
2.73e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 134.84 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKLRQRIGMIFQS-FNLFNS 96
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 97 RTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETT 176
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 177 TEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKLFDVF 229
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
3.01e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 134.06 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK- 79
Cdd:COG4604 1 MIEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 ---LRQRigmifqsfNLFNSR-TV-----FGNiaYPL---RLAKlpknEIKERVNELLKFVGLEDKANYYPEQLSGGQKQ 147
Cdd:COG4604 77 laiLRQE--------NHINSRlTVrelvaFGR--FPYskgRLTA----EDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFD 227
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
...
gi 2050094043 228 VFT 230
Cdd:COG4604 223 IIT 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-231 |
3.52e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 134.86 E-value: 3.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA-KELR 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQ--SFNLFnSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKA-NYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLF-EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNrEYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-255 |
3.80e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 136.70 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklr 81
Cdd:PRK11000 4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:PRK11000 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 162 LICDEATSALDP----ETTTEILNLLKKVNReynlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTT 237
Cdd:PRK11000 155 FLLDEPLSNLDAalrvQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFV 230
|
250
....*....|....*...
gi 2050094043 238 QNFVRSVINDHLPESVLA 255
Cdd:PRK11000 231 AGFIGSPKMNFLPVKVTA 248
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-223 |
4.35e-37 |
|
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: 133.03 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYESGGQSvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklRQRIG 85
Cdd:TIGR03410 2 EVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIF--QSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELlkFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:TIGR03410 77 IAYvpQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYEL--FPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
4.91e-37 |
|
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: 131.83 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKL 80
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEikERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKvNREYNLTILLITHE 200
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-227 |
5.00e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 140.10 E-value: 5.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNMLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:PRK13657 335 VEFDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVT---RA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 KLRQRIGMIFQSFNLFNsRTVFGNIayplRLAKlpKNEIKERVNELLK------FVglEDKANYYP-------EQLSGGQ 145
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFN-RSIEDNI----RVGR--PDATDEEMRAAAEraqahdFI--ERKPDGYDtvvgergRQLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 146 KQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKl 225
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS- 552
|
..
gi 2050094043 226 FD 227
Cdd:PRK13657 553 FD 554
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-231 |
5.12e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 133.36 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RqriGMIFQSFNL---FNSRTVFGNIAYPLRLAKLPKNEIkerVNELLKFVGLEDKAN-YYPeQLSGGQKQRVGIARALA 156
Cdd:PRK13548 78 R---AVLPQHSSLsfpFTVEEVVAMGRAPHGLSRAEDDAL---VAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 157 ------TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
.
gi 2050094043 231 Q 231
Cdd:PRK13548 231 P 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
5.60e-37 |
|
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: 133.29 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAG-TISIDDKDITSLSakeLRK 79
Cdd:COG1119 3 LLELRNVTVRR--GGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQSFNLFNSRTV----------FGNIAYPLRlaklPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG1119 76 LRKRIGLVSPALQLRFPRDEtvldvvlsgfFDSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMH-VVKEIcHRVAVMEKGKVIEEGKLFDV 228
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAAGPKEEV 230
|
..
gi 2050094043 229 FT 230
Cdd:COG1119 231 LT 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
6.23e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 133.71 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:PRK13647 5 IEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFN--LFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13647 80 -KVGLVFQDPDdqVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 160 DILICDEATSALDP---ETTTEILNLLKKVNReynlTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK13647 158 DVIVLDEPMAYLDPrgqETLMEILDRLHNQGK----TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-225 |
1.44e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 132.49 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditsLS-AKELRKLRQR 83
Cdd:PRK11247 16 NAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAgTAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 84 IGMIFQSFNLFNSRTVFGNIAYPLrlaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYNLTILLITHEmhvVKEichRVAVMEKGKVIEEGKL 225
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD---VSE---AVAMADRVLLIEEGKI 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-199 |
1.55e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 130.68 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERP--TAGTISIDDKDITSLSAkELRklrqRIGMIFQSFNLFNSR 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPA-EQR----RIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 TVFGNIAYPLRlAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:COG4136 92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180
....*....|....*....|..
gi 2050094043 178 EILNLLKKVNREYNLTILLITH 199
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTH 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-232 |
6.85e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 137.55 E-value: 6.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:TIGR00958 479 IEFQDVSFSYPNR-PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIAYPLRlaKLPKNEIKERVNELL--KFVGlEDKANYYPE------QLSGGQKQRVGIAR 153
Cdd:TIGR00958 555 RQVALVGQEPVLF-SGSVRENIAYGLT--DTPDEEIMAAAKAANahDFIM-EFPNGYDTEvgekgsQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDpettTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-244 |
8.35e-36 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 136.91 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERpTAGTISIDDK----------DI 69
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 70 TSLSAKELRKLR-QRIGMIFQ----SFN-LFnsrTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLEDKA---NYYPE 139
Cdd:PRK10261 91 SEQSAAQMRHVRgADMAMIFQepmtSLNpVF---TVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 140 QLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260
....*....|....*....|....*
gi 2050094043 220 IEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-223 |
9.90e-36 |
|
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: 129.37 E-value: 9.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 16 QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditsLSAKELRKLRQRIGMIF-QSFNLF 94
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-241 |
1.75e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 129.43 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLE---RPTAGTISIDDKDItslSAKELRKlrQRIGMIFQsfnlfNS 96
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPV---APCALRG--RKIATIMQ-----NP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 97 RTVFGniayPLR---------LAKLPKNEIKERVNELLKFVGLEDKA---NYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:PRK10418 89 RSAFN----PLHtmhtharetCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-223 |
2.41e-35 |
|
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: 128.03 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQS------------------VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIS 63
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 64 IdDKDITSLSAkelrklrqrIGMIFQsfnlfNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSG 143
Cdd:cd03220 81 V-RGRVSSLLG---------LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-244 |
1.08e-34 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 129.15 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLE----RPTAGTISIDDKDITSLSAKELRKL- 80
Cdd:PRK15093 8 NLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKLv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQ--------SFNLfnSRTVFGNI---AYPLRLAKLpKNEIKERVNELLKFVGLEDKANY---YPEQLSGGQK 146
Cdd:PRK15093 88 GHNVSMIFQepqscldpSERV--GRQLMQNIpgwTYKGRWWQR-FGWRKRRAIELLHRVGIKDHKDAmrsFPYELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSK 244
|
250
....*....|....*...
gi 2050094043 227 DVFTQPKTKTTQNFVRSV 244
Cdd:PRK15093 245 ELVTTPHHPYTQALIRAI 262
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-241 |
5.02e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 125.66 E-value: 5.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLER--PTA---GTISIDDKDITSlSAKELRKLRQRIGMIFQSFNLF 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 nSRTVFGNIAYPLRLAKLpKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK14243 104 -PKSIYDNIAYGARINGY-KGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 171 LDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVA-----VMEKGKVIEEGKLFD----VFTQPKTKTTQNFV 241
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAffnveLTEGGGRYGYLVEFDrtekIFNSPQQQATRDYV 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
6.94e-34 |
|
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: 130.31 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLE--RPTAG------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 61 -----------TISIDDKDITSLSAKELRKLRQRIGMIFQ-SFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFV 128
Cdd:TIGR03269 77 kvgepcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 129 GLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*
gi 2050094043 209 HRVAVMEKGKVIEEG 223
Cdd:TIGR03269 237 DKAIWLENGEIKEEG 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-228 |
7.70e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 127.30 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK-----ELRklrqRIGMIFQSFNLFNSR 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEKR----RIGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 TVFGNIAYPLrlaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK11144 92 KVRGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 178 EILNLLKKVNREYNLTILLITHEMhvvKEICH---RVAVMEKGKVIEEGKLFDV 228
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSL---DEILRladRVVVLEQGKVKAFGPLEEV 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
1.04e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.84 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK- 79
Cdd:COG4559 1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 ---LRQRIGMIFQsfnlFNSRTV--FGniAYPLRLAKLPKNEIKERVNELlkfVGLEDKAN-YYPeQLSGGQKQRVGIAR 153
Cdd:COG4559 77 ravLPQHSSLAFP----FTVEEVvaLG--RAPHGSSAAQDRQIVREALAL---VGLAHLAGrSYQ-TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALA-------TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
....*.
gi 2050094043 227 DVFTQP 232
Cdd:COG4559 226 EVLTDE 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-235 |
1.30e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 124.24 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYEsgGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIG 85
Cdd:PRK10895 8 NLAKAYK--GRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIFQSFNLFNSRTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 165 DEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
4.03e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.79 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNiaypLRLAKLPKNEikERVNELLKFVGLEDKANYYP----------EQLSGGQKQRVGI 151
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVkEICHRVAVMEKGKVIEEGK 224
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL-EQFDRICVMDNGQIIEQGT 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-243 |
5.35e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 123.22 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKe 76
Cdd:PRK14258 8 IKVNNLSFYYDT--QKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 77 LRKLRQRIGMIFQSFNLFnSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGLED----KANYYPEQLSGGQKQRVGI 151
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEK-----GKVIEEGKLF 226
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
250
....*....|....*..
gi 2050094043 227 DVFTQPKTKTTQNFVRS 243
Cdd:PRK14258 242 KIFNSPHDSRTREYVLS 258
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-225 |
1.35e-32 |
|
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: 120.97 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYesGGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakelRKLRQRIG 85
Cdd:TIGR03740 5 NLSKRF--GKQ--TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDLHKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIkervNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKL 225
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
2.51e-32 |
|
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: 118.69 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL--------RQRIGmifqsf 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 92 nLFNSRTVFGNIAYPLrlaklpkneikervnellkfvgledkanyypeQLSGGQKQRVGIARALATSPDILICDEATSAL 171
Cdd:cd03215 89 -LVLDLSVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2050094043 172 DPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03215 136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-244 |
2.91e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.80 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK-----DITSLSAK 75
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 76 ELRKL-RQRIGMIFQsfnlfNSR-------TVFGNIAYPLrLAKLPKN--EIKERVNELLKFVGLE-DKANYYPEQLSGG 144
Cdd:PRK11701 82 ERRRLlRTEWGFVHQ-----HPRdglrmqvSAGGNIGERL-MAVGARHygDIRATAGDWLERVEIDaARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 145 QKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGk 224
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG- 234
|
250 260
....*....|....*....|.
gi 2050094043 225 LFD-VFTQPKTKTTQNFVRSV 244
Cdd:PRK11701 235 LTDqVLDDPQHPYTQLLVSSV 255
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-219 |
3.68e-32 |
|
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: 119.88 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESggQSVHAV-EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslSAKELRKL 80
Cdd:cd03248 12 VKFQNVTFAYPT--RPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFnSRTVFGNIAYPLrlAKLPKNEIKErvnellkfvgLEDKAN-----------YYPE------QLSG 143
Cdd:cd03248 87 HSKVSLVGQEPVLF-ARSLQDNIAYGL--QSCSFECVKE----------AAQKAHahsfiselasgYDTEvgekgsQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.05e-31 |
|
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: 124.32 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qRIGMIFQSFNLFNsrtvfGNIAYPLRLAKL--PKNEIKE--RVNELLKFV-----GLEDKANYYPEQLSGGQKQRVGIA 152
Cdd:TIGR02857 397 -QIAWVPQHPFLFA-----GTIAENIRLARPdaSDAEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVkEICHRVAVM 214
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
4.26e-31 |
|
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: 117.15 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISK---VYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK----DITSLS 73
Cdd:COG4778 4 LLEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 74 AKELRKLRQR-IGMIFQsfnlF-------NSRTVfgnIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGG 144
Cdd:COG4778 84 PREILALRRRtIGYVSQ----FlrviprvSALDV---VAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 145 QKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKG 217
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-223 |
6.81e-31 |
|
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: 115.97 E-value: 6.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIAyplrlaklPKNEIKERvnELLKFVGLEDKANyypeQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03369 82 SSLTIIPQDPTLF-SGTIRSNLD--------PFDEYSDE--EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 162 LICDEATSALDPETTTEIlnllKKVNRE--YNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:cd03369 147 LVLDEATASIDYATDALI----QKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-223 |
1.01e-30 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 122.93 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTI-----SIDDKDITSlsakelrklRQRIGMIFQSFNLF 94
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT---------RRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASD 479
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
1.10e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.43 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK09700 5 YISMAGIGKSF--GP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFNSRTVFGNiaypLRLAKLPK-----------NEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLEN----LYIGRHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV 228
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
2.53e-30 |
|
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: 113.56 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrkLR 81
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNIAyplrlaklpkneikervnellkfvgledkanyypEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
2.90e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.88 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGgQSVHAVEdvtLSVEKGEIFGIIGFSGAGKSTLLRLVNML---ERPTAGTISIDDKDITSLS--AK 75
Cdd:PRK09984 4 IIRVEKLAKTFNQH-QALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 76 ELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPlRLAKLP---------KNEIKERVNELLKFVGLEDKANYYPEQLSGGQK 146
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-219 |
7.68e-30 |
|
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: 119.47 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 10 VYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLeRPTAGTISIDDKDITSLSAKElrkLRQRIGMIF 88
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARlLVGVW-PPTAGSVRLDGADLSQWDREE---LGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 QSFNLFNSrTVFGNIAyplRLAKLPKNEIKE-----RVNEL-LKF-------VGlEDKANyypeqLSGGQKQRVGIARAL 155
Cdd:COG4618 413 QDVELFDG-TIAENIA---RFGDADPEKVVAaaklaGVHEMiLRLpdgydtrIG-EGGAR-----LSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDGRV 544
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
7.77e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 117.64 E-value: 7.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkL 80
Cdd:PRK09536 3 MIDVSDLS--VEFGDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQ----SFNlFNSRTV--FGNIAYPLRLAklPKNEIKER-VNELLKFVGLEDKANYYPEQLSGGQKQRVGIAR 153
Cdd:PRK09536 76 SRRVASVPQdtslSFE-FDVRQVveMGRTPHRSRFD--TWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-247 |
9.65e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.81 E-value: 9.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 14 GGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA---KELRKLRQRIGMIFQS 90
Cdd:PRK14271 32 AGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIfnyRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 91 FNLFnSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:PRK14271 110 PNPF-PMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREynLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSVI 245
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLS 266
|
..
gi 2050094043 246 ND 247
Cdd:PRK14271 267 GD 268
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-223 |
1.98e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 118.58 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:PRK11176 342 IEFRNVTFTYP--GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNIAYPlRLAKLPKNEIKE--RVNELLKFV-----GLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK11176 417 NQVALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 155 LATSPDILICDEATSALDPETTTEI---LNLLKKvnreyNLTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIqaaLDELQK-----NRTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
5.67e-29 |
|
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: 116.69 E-value: 5.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSFNLFNSrTV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR---RVSVCAQDAHLFDT-TV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 100 FGNiaypLRLAKlpKNEIKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:TIGR02868 426 REN----LRLAR--PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 2050094043 169 SALDPETTTEILNLLKKVNREYnlTILLITH 199
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGR--TVVLITH 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-231 |
5.78e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.33 E-value: 5.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKl 80
Cdd:PRK11231 2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFNSRTVFGNIAY---P-LRL-AKLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK11231 77 --RLALLPQHHLTPEGITVRELVAYgrsPwLSLwGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-222 |
1.02e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIGMI---FQSFNLFN 95
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGIAYVpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 96 SRTVFGNIAYPL--RLAK---LPKNEIKERVNEL-----LKFVGLEDKANyypeQLSGGQKQRVGIARALATSPDILICD 165
Cdd:COG1129 344 DLSIRENITLASldRLSRgglLDRRRERALAEEYikrlrIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-209 |
2.79e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 11 YESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklrQRIGMIFQS 90
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 91 FNLFNSrTVFGNIAYPLRLAKlPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2050094043 171 LDPETTTEILNLLKKVNREYNLTILLITHEMHvvkEICH 209
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKD---EINH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-221 |
1.22e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 110.00 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 3 SFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQ 82
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIGMIFQSFNLFNSRTVFGNI---AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 160 DILICDEATSALdpeTTTEILNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:PRK11288 160 RVIAFDEPTSSL---SAREIEQLFRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-223 |
9.68e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.91 E-value: 9.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSFNLFNSRTVFG 101
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIA---YPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK10253 101 LVArgrYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2050094043 178 EILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-223 |
1.24e-25 |
|
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: 102.35 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV-NMLERP--TAGTISIDDKDitsLSAKELRKlrqRIGMIFQSF 91
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQP---RKPDQFQK---CVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 92 NLFNSRTVFGNIAY--PLRLAKLPKNEIKERVNE--LLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEA 167
Cdd:cd03234 91 ILLPGLTVRETLTYtaILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 168 TSALDPETTTEILNLLKKVNREyNLTILLITH----EMHvvkEICHRVAVMEKGKVIEEG 223
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARR-NRIVILTIHqprsDLF---RLFDRILLLSSGEIVYSG 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-223 |
1.35e-25 |
|
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: 107.52 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:TIGR01193 474 IVINDVSYSY---GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNsrtvfGNIAYPLRLAKLPKNEIKErVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:TIGR01193 548 QFINYLPQEPYIFS-----GSILENLLLGAKENVSQDE-IWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREynlTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-234 |
1.54e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.16 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 16 QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItSLSAKELRKLRQRIGMIFQSFN--L 93
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPEqqI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVgledKANYYPEQ----LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK13638 91 FYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLV----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 170 ALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-223 |
1.16e-24 |
|
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: 98.78 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNI-----SKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTA--GTISIDDKDItslsa 74
Cdd:cd03213 4 LSFRNLtvtvkSSPSKSGKQLLK---NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 75 kELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLRLaklpkneikervnellkfvgledkanyypEQLSGGQKQRVGIARA 154
Cdd:cd03213 76 -DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITH----EMHvvkEICHRVAVMEKGKVIEEG 223
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHqpssEIF---ELFDKLLLLSQGRVIYFG 194
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
2.13e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.57 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelRKL 80
Cdd:PRK11614 5 MLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIK-ERVNELlkFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERiKWVYEL--FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-223 |
2.60e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.86 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSFNLFNSRTVFGNI 103
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---KVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 104 A---YPLR--LAKLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:PRK10575 107 AigrYPWHgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-222 |
3.91e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL--------RQRIGMIfQ 89
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLV-P 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 90 SFNLF-NsrTVFGNIAYPlRLAKLP---KNEIKERVNELL-----KFVGLEDKAnyypEQLSGGQKQRVGIARALATSPD 160
Cdd:COG3845 350 DMSVAeN--LILGRYRRP-PFSRGGfldRKAIRAFAEELIeefdvRTPGPDTPA----RSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-223 |
5.31e-24 |
|
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: 103.17 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI-TSLSAkelrkL 80
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA-----V 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
8.72e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 4 FNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIdDKDItslsakelrklrqR 83
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGL-------------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 84 IGMIFQSFNLFNSRTVFGNI-------------------------AYPLRLAKLpKNEIKE--------RVNELLKFVGL 130
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVldgdaelraleaeleeleaklaepdEDLERLAEL-QEEFEAlggweaeaRAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 131 EDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKvnreYNLTILLITHEMHVVKEICH 209
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHDRYFLDRVAT 217
|
250
....*....|.
gi 2050094043 210 RVAVMEKGKVI 220
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-279 |
1.05e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.58 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYeSGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK15439 11 LLCARSISKQY-SG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFNSRTVFGNIAYplRLAKLPKNeiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK15439 87 --GIYLVPQEPLLFPNLSVKENILF--GLPKRQAS--MQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTeilNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVftqPKTKTTQ 238
Cdd:PRK15439 161 ILILDEPTASLTPAETE---RLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL---STDDIIQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2050094043 239 NFVRSVINDHLPESvlakiqnggQIYRLTFTG----EETGQPVLS 279
Cdd:PRK15439 235 AITPAAREKSLSAS---------QKLWLELPGnrrqQAAGAPVLT 270
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-222 |
1.62e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 93.87 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSlsakelrklrqrigmifqsfnlfnS 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGR------------------------E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 97 RTVFGNIAyplrlaklPKNEIKERVnELLKFVGLEDKANYY--PEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:COG2401 100 ASLIDAIG--------RKGDFKDAV-ELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVKEIC-HRVAVMEKGKVIEE 222
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-223 |
7.24e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.32 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLRQRIGMIFQSFNLF 94
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 nSRTVFGNIAyplrLAKlpKNEIKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK10789 402 -SDTVANNIA----LGR--PDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-223 |
7.61e-22 |
|
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: 91.43 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSLSAKElrKLRQRIGMIFQsfnlfnsrt 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 99 vfgniaYPLRLAKLpkneikeRVNELLKFVGledkanyypEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:cd03217 85 ------YPPEIPGV-------KNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2050094043 179 ILNLLKKVnREYNLTILLITHEMHVVKEI-CHRVAVMEKGKVIEEG 223
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
260-334 |
9.34e-22 |
|
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: 87.57 E-value: 9.34e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 260 GGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKEIQKALQHLR-LQVQLKEV 334
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLReQGVEVEVL 76
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
2.19e-21 |
|
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: 88.66 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrklr 81
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGmifqsfnlfnsrtvfgniayplrlaklpkneikervnellkfvgledkanYYPeQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03221 63 VKIG--------------------------------------------------YFE-QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
2.55e-21 |
|
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: 95.47 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI-TSLSakelrK 79
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS-----D 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKG 217
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-220 |
7.01e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.07 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDDKDITSLSAKELRklR 81
Cdd:PRK13549 9 KNITKTF--GG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNIRDTE--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSRTVFGNI---AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATS 158
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 159 PDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-199 |
7.79e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISkVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI-DDKDITSLSakelrk 79
Cdd:COG4178 362 ALALEDLT-LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 lrQRIGMIFQSFnlfnsRTVfgnIAYPLRLAKLPKneikERVNELLKFVGLEDKANYYPEQ------LSGGQKQRVGIAR 153
Cdd:COG4178 433 --QRPYLPLGTL-----REA---LLYPATAEAFSD----AELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKvnREYNLTILLITH 199
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-230 |
1.41e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditsLSAKELRKLR 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-------LGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QR-IGMIFQS------FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK15056 77 KNlVAYVPQSeevdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHrVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
2.60e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 91.70 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelRKLR 81
Cdd:PRK10790 341 IDIDNVSFAYRDD-NLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIAyplrlakLPKNEIKERVNELLKFVGLEDKANYYP--------EQ---LSGGQKQRVG 150
Cdd:PRK10790 415 QGVAMVQQDPVVL-ADTFLANVT-------LGRDISEEQVWQALETVQLAELARSLPdglytplgEQgnnLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVnREyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-RE-HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-204 |
2.62e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesgGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakeLRKL 80
Cdd:PRK09544 4 LVSLENVSVSF---GQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLfnsrtvfgNIAYPL---RLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK09544 66 KLRIGYVPQKLYL--------DTTLPLtvnRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVV 204
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
262-326 |
2.79e-20 |
|
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: 83.27 E-value: 2.79e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 262 QIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKEIQKALQHLR 326
Cdd:pfam09383 1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLR 65
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
3.43e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.19 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKLR 81
Cdd:PRK10522 323 LELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNsrtvfgniayplRLAKlPKNEIK--ERVNELLKFVGLEDKANYYPE-----QLSGGQKQRVGIARA 154
Cdd:PRK10522 397 KLFSAVFTDFHLFD------------QLLG-PEGKPAnpALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 155 LATSPDILICDEATSALDP----ETTTEILNLLkkvnREYNLTILLITHEMHVVkEICHRVAVMEKGKVIE 221
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPhfrrEFYQVLLPLL----QEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
3.69e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditslsAKELrkl 80
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqRIGMIFQSFNLFN-SRTVFGNIAyplRLAklpKNEIKERVNELLK---FVGleDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:COG0488 379 --KIGYFDQHQEELDpDKTVLDELR---DGA---PGGTEQEVRGYLGrflFSG--DDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD----DFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
1.12e-19 |
|
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: 85.60 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHAV-EDVTLSVEKGEIFGIIGFSGAGKSTLLR--LVNMleRPTAGTISIDDkditslsakelr 78
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSalLGEL--EKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 79 klrqRIGMIFQSFNLFNsRTVFGNIayplrLAKLPKNEikERVNELLKFVGLEDKANYYPEQ-----------LSGGQKQ 147
Cdd:cd03250 67 ----SIAYVSQEPWIQN-GTIRENI-----LFGKPFDE--ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEI-----LNLLKKvNReynlTILLITHEMHVVKEiCHRVAVMEKGK 218
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN-NK----TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-245 |
2.76e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLL-----RLVNMLERptAGTISIDDKDItslsakELRKLRQRIGMIFQSFNL 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPI------DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FNSRTVFGNIAYPLRL---AKLPKNEIKERVNELLKFVGLEDKANY---YPEQ---LSGGQKQRVGIARALATSPDILIC 164
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK---LFDVFTQ-----PKTKT 236
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSpdqAVPFFSDlghpcPENYN 270
|
....*....
gi 2050094043 237 TQNFVRSVI 245
Cdd:TIGR00955 271 PADFYVQVL 279
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-230 |
3.08e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLL-RLVNMLerPTAGTISIDDKDITSLSAKELRKLRqriGMIFQ----SFNLfnsrT 98
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHR---AYLSQqqspPFAM----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 99 VFgniAYpLRL---AKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL-----ATSPD--ILICDEAT 168
Cdd:COG4138 86 VF---QY-LALhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 169 SALDPETTTEILNLLKKVnREYNLTILLITHEM-HVVKEiCHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:COG4138 162 NSLDVAQQAALDRLLREL-CQQGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAEVMT 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-221 |
4.93e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 88.26 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLRQRIGMIFQSFNLFnSRTVFGNI 103
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLF-SGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 104 AyplrlaklPKNEIK--------ERVNelLKFV------GLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PLN03130 1334 D--------PFNEHNdadlweslERAH--LKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 170 ALDPETTTeilnLLKKVNRE--YNLTILLITHEMHVVKEiCHRVAVMEKGKVIE 221
Cdd:PLN03130 1404 AVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
13-231 |
9.20e-19 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 86.87 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 13 SGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditslsakelrklRQRIGMIFQSFN 92
Cdd:PRK13545 32 KDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI----------------KGSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 93 LFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALD 172
Cdd:PRK13545 96 LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 173 PETTTEIlnlLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13545 176 QTFTKKC---LDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-231 |
2.59e-18 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 83.33 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrklrqrIGMIFQSFNLF 94
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 175 TTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13546 178 FAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-173 |
4.55e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslSAKELRKLRQRIGMIFQSF--NLF 94
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAYMPQGLgkNLY 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:NF033858 91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
6.46e-18 |
|
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: 84.49 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDDKDITSLSAKEL 77
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RklRQRIGMIFQSFNLFNSRTVFGNI----AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIA 152
Cdd:TIGR02633 76 E--RAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVNReYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-231 |
7.08e-18 |
|
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: 85.00 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL-LRLVNMLErPTAGTISIDDKDITSLSakeLRKL 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINE-SAEGEIIIDGLNIAKIG---LHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRtvfgniaypLRLAKLPKNEIKER-------VNELLKFV-GLEDKANYY----PEQLSGGQKQR 148
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGS---------LRMNLDPFSQYSDEevwwaleLAHLKTFVsALPDKLDHEcaegGENLSVGQRQL 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 149 VGIARALATSPDILICDEATSALDPETTteilNLLKKVNREY--NLTILLITHEMHVVKEIChRVAVMEKGKVIEEGKLF 226
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPS 1504
|
....*
gi 2050094043 227 DVFTQ 231
Cdd:TIGR00957 1505 NLLQQ 1509
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-222 |
8.92e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrQRIGMIFQSFNLFNSR 97
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 TVFGNI----AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALdp 173
Cdd:PRK10762 95 TIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL-- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 174 eTTTEILNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK10762 173 -TDTETESLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-232 |
1.15e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.13 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLL-RLVNMLerPTAGTISIDDKDITSLSAKELRklRQRIGMIFQSFNLFNSrTVFGN 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELA--RHRAYLSQQQTPPFAM-PVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 103 IAypLRL-AKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA-LATSPDI------LICDEATSALDPE 174
Cdd:PRK03695 90 LT--LHQpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREyNLTILLITHEM-HVVKEiCHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK03695 168 QQAALDRLLSELCQQ-GIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-277 |
1.19e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 84.26 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rqrIGMIFQSFNLFnSRTVFGNIAyPLR-------LAKLPKNEIKERVNEllKFVGLEDKANYYPEQLSGGQKQRVGIAR 153
Cdd:PLN03232 1312 ---LSIIPQSPVLF-SGTVRFNID-PFSehndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDPETTTeilnLLKKVNRE--YNLTILLITHEMHVVKEiCHRVAVMEKGKVIEegklFDVFTQ 231
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE----YDSPQE 1455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2050094043 232 PKTKTTQNFVRsVINDHLPEsvlakiqNGGQIYRLTFTGEETGQPV 277
Cdd:PLN03232 1456 LLSRDTSAFFR-MVHSTGPA-------NAQYLSNLVFERRENGMSL 1493
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-220 |
1.81e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.85 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIG 85
Cdd:PRK10982 3 NISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 86 MIFQSFNLFNSRTVFGNI---AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDIL 162
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-174 |
2.37e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.94 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakELRKLRQR-IGMIFQSFNLFNSRT 98
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHEnILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 99 VFGNIAYPLRLAKLPKNEIkervNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-199 |
2.38e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakELRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLaklpKNEIKERVNELLKFVGLED----KANYypeqLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK13539 93 NLEFWAAF----LGGEELDIAAALEAVGLAPlahlPFGY----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 2050094043 178 EILNLLkKVNREYNLTILLITH 199
Cdd:PRK13539 165 LFAELI-RAHLAQGGIVIAATH 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-205 |
3.00e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitSLSAKELRKLR 81
Cdd:PTZ00265 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFnSRTVFGNIAYPLRLAK---LPKNEIKER------------------------------VNELL--- 125
Cdd:PTZ00265 460 SKIGVVSQDPLLF-SNSIKNNIKYSLYSLKdleALSNYYNEDgndsqenknkrnscrakcagdlndmsnttdSNELIemr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 126 ---------------KFVGLEDKANYYPE-----------QLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEI 179
Cdd:PTZ00265 539 knyqtikdsevvdvsKKVLIHDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|....*.
gi 2050094043 180 LNLLKKVNREYNLTILLITHEMHVVK 205
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-223 |
3.58e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.20 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLLrlvNMLE--RPTAGTISIDDKDITSLsakELRKLRQRIGMIFQSFNLFNSrTVFG 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAyplrLAKLPKNEikERVNELLK------FVGLEDKANYYP--EQ---LSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK11174 442 NVL----LGNPDASD--EQLQQALEnawvseFLPLLPQGLDTPigDQaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 171 LDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PRK11174 516 LDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-219 |
3.73e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklRQRIGMIF-----QSFNLF--- 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 -----NSRTVFGNIAYPLRLAKlpKNEIKERVNELL--KFVGLEDKAnyypEQLSGGQKQRVGIARALATSPDILICDEA 167
Cdd:PRK15439 357 plawnVCALTHNRRGFWIKPAR--ENAVLERYRRALniKFNHAEQAA----RTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 168 TSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-221 |
5.68e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.37 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDD-----KDItslSAKElrklRQRIGMIFQ 89
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGevcrfKDI---RDSE----ALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 90 SF----------NLF--NSRTVFGNIAYplrlaklpkNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:NF040905 86 ELalipylsiaeNIFlgNERAKRGVIDW---------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-221 |
7.19e-17 |
|
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: 81.38 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYES-GGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKL 80
Cdd:COG4615 328 LELRGVTYRYPGeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNsrtvfgniayplRLAKLPKNEIKERVNELLKFVGLEDKANYypE-------QLSGGQKQRVGIAR 153
Cdd:COG4615 405 RQLFSAVFSDFHLFD------------RLLGLDGEADPARARELLERLELDHKVSV--EdgrfsttDLSQGQRKRLALLV 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 154 ALATSPDILICDEATSALDPET----TTEILNLLKKVNReynlTILLITHE---MHVvkeiCHRVAVMEKGKVIE 221
Cdd:COG4615 471 ALLEDRPILVFDEWAADQDPEFrrvfYTELLPELKARGK----TVIAISHDdryFDL----ADRVLKMDYGKLVE 537
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-230 |
1.21e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERPTA-------GTISIDDKDITSLSAKELRKLRQRIGMIFQSFN 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 93 LFNSRTVFGNIAYP-LRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA---------TSPDIL 162
Cdd:PRK13547 97 AFSAREIVLLGRYPhARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-238 |
1.75e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.39 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlRLVNMLERPTAGTisiDDKDITSLSAKElRKLRQRIG----MIFQSFNL 93
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANR-RALRRTIG*hrpVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 94 FNSRTvfgNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:NF000106 101 FSGRE---NLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 174 ETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQ 238
Cdd:NF000106 178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-219 |
6.12e-16 |
|
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: 76.82 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL----LRLVNmlerpTAGTISIDDKDITSLSakeL 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKLRQRIGMIFQSFNLFNSrtvfgniayPLRLAKLPKNEIKERvnELLKF---VGLEDKANYYPEQL-----------SG 143
Cdd:cd03289 73 QKWRKAFGVIPQKVFIFSG---------TFRKNLDPYGKWSDE--EIWKVaeeVGLKSVIEQFPGQLdfvlvdggcvlSH 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKV 219
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-175 |
7.60e-16 |
|
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: 78.44 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrklr 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSF-NLFNSRTVFGNIAYPLRLAKLPKNEIKERV---------NELLKFVGledkanyypeQLSGGQKQRVGI 151
Cdd:TIGR03719 385 VKLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHL 454
|
170 180
....*....|....*....|....
gi 2050094043 152 ARALATSPDILICDEATSALDPET 175
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-242 |
9.94e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakELRKLRQRIGMIFQS---FNLFNSR 97
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVKKGMAYITESrrdNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 TVFGNIAYP--LRLAKL--------PKNEIK--ERVNELL--KFVGLEDKANyypeQLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK09700 357 SIAQNMAISrsLKDGGYkgamglfhEVDEQRtaENQRELLalKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMekgkviEEGKLFDVFTQPKTKTTQNFVR 242
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF------CEGRLTQILTNRDDMSEEEIMA 504
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-219 |
1.11e-15 |
|
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: 78.41 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 5 NNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLL----RLVNmlerpTAGTISIDDKDITSLSakeLRKL 80
Cdd:TIGR01271 1221 QGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLS-----TEGEIQIDGVSWNSVT---LQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFnSRTVFGNIAyplRLAKLPKNEIKERVNEllkfVGLEDKANYYPEQL-----------SGGQKQRV 149
Cdd:TIGR01271 1291 RKAFGVIPQKVFIF-SGTFRKNLD---PYEQWSDEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLM 1362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKV 219
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLE-CQQFLVIEGSSV 1429
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
1.57e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKE--------LRKLRQRIGMIF---- 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 -QSFNLfNSRTVFGNIAYPLRLAklpkneikERVNELLKFVGLEDKANYYPEQ----LSGGQKQRVGIARALATSPDILI 163
Cdd:PRK10762 348 kENMSL-TALRYFSRAGGSLKHA--------DEQQAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-199 |
2.10e-15 |
|
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: 72.96 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISkVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI-DDKDITSLSakelrkl 80
Cdd:cd03223 1 IELENLS-LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rQRIGMIFQSFnlfnsRTVfgnIAYPLRlaklpkneikervnellkfvgledkanyypEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03223 71 -QRPYLPLGTL-----REQ---LIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITH 199
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-222 |
2.93e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakeLRKLRQRI--GMIF-----QSFNLF 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIraGIMLcpedrKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 NSRTVFGNIAYPLRLAKLPK----NEIKERVNELLKFVGLEDKANyYPEQ----LSGGQKQRVGIARALATSPDILICDE 166
Cdd:PRK11288 344 PVHSVADNINISARRHHLRAgcliNNRWEAENADRFIRSLNIKTP-SREQlimnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 167 ATSALDPETTTEILNLLkkvnreYNL-----TILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVI------YELaaqgvAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-215 |
9.60e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 72.83 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKG-----EIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDIT----SLSAKE---LRKLRQRIGMIFQS 90
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYegtVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 91 FNLFNSrtvfgNIAYPLRLAKLPKNEIKErvnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:cd03237 92 HPYFKT-----EIAKPLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2050094043 171 LDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVME 215
Cdd:cd03237 146 LDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-200 |
1.03e-14 |
|
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: 74.97 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 3 SFNNISKVYESGGqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVnmlerptAGTisidDKDItslSAKELRKLRQ 82
Cdd:TIGR03719 6 TMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV----DKDF---NGEARPQPGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIGMIFQSFNLFNSRTVFGNIAYPLR-----LAKLpkNEIKER-------VNELLKFVG-LEDK---------------- 133
Cdd:TIGR03719 69 KVGYLPQEPQLDPTKTVRENVEEGVAeikdaLDRF--NEISAKyaepdadFDKLAAEQAeLQEIidaadawdldsqleia 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 134 --ANYYP------EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHE 200
Cdd:TIGR03719 147 mdALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHD 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-223 |
1.62e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKST-LLRLVNMLErPTAGTISIDDKDITSLSakeLRKLRQRIGMIFQSFNLFNSrTVFGN 102
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTlLLTFMRMVE-VCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 103 I-----AYPLRL-AKLPKNEIKERV---NELLKFVGLEDKANYypeqlSGGQKQRVGIARALAT--SPDILIcDEATSAL 171
Cdd:PTZ00243 1404 VdpfleASSAEVwAALELVGLRERVaseSEGIDSRVLEGGSNY-----SVGQRQLMCMARALLKkgSGFILM-DEATANI 1477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 172 DPETTTEILNLLKKVNREYnlTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PTZ00243 1478 DPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-205 |
2.86e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 59 AGTISIDDKDITSLSAKELRKLrqrIGMIFQSFNLFNsRTVFGNIAYPlrlaklPKNEIKERVNELLKFVGLEDKANYYP 138
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLFN-MSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 139 EQ-----------LSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVK 205
Cdd:PTZ00265 1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-243 |
2.94e-14 |
|
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: 71.48 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL----LRLVNMLErptaGTISIDDKDITSLSakeL 77
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKLRQRIGMIFQSFNLFNSRTVFG----------NIAYPLRLAKLpKNEIKERVNellkfvGLEDKANYYPEQLSGGQKQ 147
Cdd:cd03288 91 HTLRSRLSIILQDPILFSGSIRFNldpeckctddRLWEALEIAQL-KNMVKSLPG------GLDAVVTEGGENFSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTteilNLLKKV--NREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKL 225
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATE----NILQKVvmTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
|
250
....*....|....*...
gi 2050094043 226 FDVFTQpKTKTTQNFVRS 243
Cdd:cd03288 239 ENLLAQ-EDGVFASLVRT 255
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-223 |
1.59e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV------NMLErptaGTISIDDKDITSLSAKElrklRQRIGmIFQSFN-- 92
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESILDLEPEE----RAHLG-IFLAFQyp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 93 -----LFNSRtvFGNIAYPLRLAKLPKNEIK-----ERVNELLKFVGLEDK--ANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:CHL00131 94 ieipgVSNAD--FLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPSflSRNVNEGFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEIC-HRVAVMEKGKVIEEG 223
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-219 |
3.73e-13 |
|
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: 69.85 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERPTAGTISIDDKDITSLSAkeLRKLRQRIGMIFQSFNLFNSRTV 99
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNP--AQAIRAGIAMVPEDRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 100 FGnIAYPLRLAKLPKNEIKERVNEL---------LKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:TIGR02633 354 LG-VGKNITLSVLKSFCFKMRIDAAaelqiigsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2050094043 170 ALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-224 |
4.51e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYEsggqsvhaveDVTLSVE-----KGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK--------- 67
Cdd:COG1245 342 VEYPDLTKSYG----------GFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqyis 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 68 DITSLSAKELrkLRQRIGMIFQSfNLFNSRtvfgnIAYPLRLAKLPKNEIKErvnellkfvgledkanyypeqLSGGQKQ 147
Cdd:COG1245 412 PDYDGTVEEF--LRSANTDDFGS-SYYKTE-----IIKPLGLEKLLDKNVKD---------------------LSGGELQ 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEkGKVIEEGK 224
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGH 538
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
7.09e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDkditslSAKelrklr 81
Cdd:PRK11819 325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE------TVK------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 qrIGMIFQSF-NLFNSRTVFGNIAYPLRLAKLPKNEIKERV---------NELLKFVGledkanyypeQLSGGQKQRVGI 151
Cdd:PRK11819 389 --LAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVG----------VLSGGERNRLHL 456
|
170 180
....*....|....*....|....
gi 2050094043 152 ARALATSPDILICDEATSALDPET 175
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-227 |
7.69e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITslsakelRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPT-------KQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAY------PLRLAKLPKNEIKERVNELLKFVGLEDK--ANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 174 ETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFD 227
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-220 |
3.92e-12 |
|
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: 64.59 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLE---RPTaGTISIDDKDitslSAKEL 77
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKaLANRTEgnvSVE-GDIHYNGIP----YKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 RKLRQRIGMIFQSFNLFNSRTVFgniayplrlaklpkneikervnELLKFVgLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPTLTVR----------------------ETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHvvKEICH---RVAVMEKGKVI 220
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAS--DEIYDlfdKVLVLYEGRQI 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-172 |
4.88e-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: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 12 ESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKLRQRIGMIFQSF 91
Cdd:cd03231 9 ERDGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 92 NLFNSRTVFGNIAYPLRLAKlpkneiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSAL 171
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
.
gi 2050094043 172 D 172
Cdd:cd03231 157 D 157
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-200 |
5.95e-12 |
|
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: 63.80 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNmlERPTAGTISiddKDITsLSAKELRK-L 80
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVIT---GEIL-INGRPLDKnF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 RQRIGMIFQSFNLFNSRTVfgniayplrlaklpkneikervNELLKFvgledKANYypEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTV----------------------REALRF-----SALL--RGLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHE 200
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQ 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-219 |
7.93e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKE-------LRKLRQRIGMIFQSFN 92
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfaLVTEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 93 L-FNSrtVFGNI-AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK10982 343 IgFNS--LISNIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2050094043 170 ALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-215 |
2.73e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYEsggqsvhaveDVTLSVE-----KGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISID---------- 65
Cdd:PRK13409 340 LVEYPDLTKKLG----------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 66 --DKDITslsakeLRKLRQRIGMIFQSfNLFNSrtvfgNIAYPLRLAKLPKNEIKErvnellkfvgledkanyypeqLSG 143
Cdd:PRK13409 410 kpDYDGT------VEDLLRSITDDLGS-SYYKS-----EIIKPLQLERLLDKNVKD---------------------LSG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVME 215
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-199 |
8.34e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 3 SFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLvnMlerptAGTisidDKDIT-----SLSAKel 77
Cdd:PRK11819 8 TMNRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRI--M-----AGV----DKEFEgearpAPGIK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 78 rklrqrIGMIFQSFNLFNSRTVFGNIAYPLR--LAKLPK-NEIKER-------VNELLKFVG-LEDK---ANYY------ 137
Cdd:PRK11819 72 ------VGYLPQEPQLDPEKTVRENVEEGVAevKAALDRfNEIYAAyaepdadFDALAAEQGeLQEIidaADAWdldsql 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 138 ---------P------EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTteilNLLKKVNREYNLTILLITH 199
Cdd:PRK11819 146 eiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLEQFLHDYPGTVVAVTH 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-229 |
1.09e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLvnML-ERPTAGTISIDdkditslsakelrkLRQRIGMIFQSFNLFNSrTVFG 101
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISA--MLgELSHAETSSVV--------------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLAKlpkneikERVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PLN03232 698 NILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 171 LDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEGKLFDVF 229
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-172 |
1.58e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakelRKLRQRigmiFQSfNLF------- 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRDE----YHQ-DLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 -NSR-TVFGNIAYPLRLAKLPKNeikERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALD 172
Cdd:PRK13538 85 iKTElTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-185 |
2.00e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 28 VEKGEIFGIIGFSGAGKSTLLrlvNML-ERPTAGTISIDDKDItslSAKELRKLRQR-IGMIFQSFNLFNSRTVFGNIAY 105
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLL---NVLaERVTTGVITGGDRLV---NGRPLDSSFQRsIGYVQQQDLHLPTSTVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 106 PLRL---AKLPKNEIKERVNELLKFVGLEDKANYY----PEQLSGGQKQRVGIARALATSPDILI-CDEATSALDPETTT 177
Cdd:TIGR00956 860 SAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939
|
....*...
gi 2050094043 178 EILNLLKK 185
Cdd:TIGR00956 940 SICKLMRK 947
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-199 |
2.45e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.69 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrkl 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDV---LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK------------- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 81 rQRIGMIFQSfNLFNSRTVFGNIAYPLRLAKLPKNEIKERV-NELLKFVGLE---------DKANYYPEQLSGGQKQRVG 150
Cdd:TIGR00954 515 -GKLFYVPQR-PYMTLGTLRDQIIYPDSSEDMKRRGLSDKDlEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLkkvnREYNLTILLITH 199
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-219 |
3.12e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIGMIFQSFNLFNSRTV 99
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDRKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 100 FGnIAYPLRLAKLPKNEIKERVNELLKFVGLED-------KANYyPEQ----LSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:PRK13549 356 MG-VGKNITLAALDRFTGGSRIDDAAELKTILEsiqrlkvKTAS-PELaiarLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 169 SALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-219 |
3.57e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRlvnmlerptagtisiddkdiTSLSAKELRKLR----QRIGMIFQSFNLFNSrT 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISEGRvwaeRSIAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 99 VFGNIAY-----PLRLAKLPkneikeRVNELLKFV-----GLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:PTZ00243 737 VRGNILFfdeedAARLADAV------RVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 169 SALDP---ETTTE--ILNLLKKVNReynltiLLITHEMHVVKEICHRVAvMEKGKV 219
Cdd:PTZ00243 811 SALDAhvgERVVEecFLGALAGKTR------VLATHQVHVVPRADYVVA-LGDGRV 859
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-223 |
6.65e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 2 ISFNNISKVYESGGQSvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditslsakelrkLR 81
Cdd:PLN03130 615 ISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 82 QRIGMIFQSFNLFNSrTVFGNIAY-----PLR-------------LAKLP---KNEIKER-VNellkfvgledkanyype 139
Cdd:PLN03130 679 GTVAYVPQVSWIFNA-TVRDNILFgspfdPERyeraidvtalqhdLDLLPggdLTEIGERgVN----------------- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 140 qLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNllKKVNREY-NLTILLITHEMHVVKEIcHRVAVMEKGK 218
Cdd:PLN03130 741 -ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGM 816
|
....*
gi 2050094043 219 VIEEG 223
Cdd:PLN03130 817 IKEEG 821
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-202 |
8.42e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.11 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 11 YESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLrLVNMLERPT-AGTISIDDKDITSLSAKELRKL-RQRIGMIF 88
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLL-LAILGEMQTlEGKVHWSNKNESEPSFEATRSRnRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 QSFNLFNSrTVFGNIAYplrlaKLPKNeiKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVGIARALAT 157
Cdd:cd03290 86 QKPWLLNA-TVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTE-----ILNLLKKVNReynlTILLITHEMH 202
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHlmqegILKFLQDDKR----TLVLVTHKLQ 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
1.50e-09 |
|
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: 55.84 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 30 KGEIFGIIGFSGAGKSTLLR-LVNMLERPTAGTISIDDKDITSLSAKELRKLRQRIGmifqsfnlfnsrtvfgniayplr 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 109 laklpkneikervnellkfvgledkanyyPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL-----NLL 183
Cdd:smart00382 58 -----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLL 108
|
170 180
....*....|....*....|...
gi 2050094043 184 KKVNREYNLTILLITHEMHVVKE 206
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-218 |
2.21e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLErPTAGTISIDDKDitslsakELRK 79
Cdd:PRK15064 1 MLSTANITMQF--GAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKiLGGDLE-PSAGNVSLDPNE-------RLGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRiGMIFQSFNLFNsrTV-FGNI-------------AYP-------LRLAKLpknEIK----------ERVNELLKFV 128
Cdd:PRK15064 69 LRQD-QFAFEEFTVLD--TViMGHTelwevkqerdriyALPemseedgMKVADL---EVKfaemdgytaeARAGELLLGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 129 GLEDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATSALDPETtteiLNLLKKVNREYNLTILLITHEMHVVKEI 207
Cdd:PRK15064 143 GIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDRHFLNSV 218
|
250
....*....|.
gi 2050094043 208 CHRVAVMEKGK 218
Cdd:PRK15064 219 CTHMADLDYGE 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-246 |
2.61e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 28 VEKGEIFGIIGFSGAGKSTLLRLV----NMLERPTAGTISIDdkditSLSAKELRK-LRQRIGMIFQSFNLFNSRTVFGN 102
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYD-----GITPEEIKKhYRGDVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 103 IAYPLRLaKLPKNEIK-----ERVNELLKFV----GLEDK-----ANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:TIGR00956 159 LDFAARC-KTPQNRPDgvsreEYAKHIADVYmatyGLSHTrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 169 SALDPETTTEILNLLKKVNREYNLTILL-ITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV--------FTQPKTKTTQN 239
Cdd:TIGR00956 238 RGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDRQTTAD 317
|
....*..
gi 2050094043 240 FVRSVIN 246
Cdd:TIGR00956 318 FLTSLTS 324
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-177 |
2.87e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 28 VEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLS-AKELRKLRQRIGMIFQSFNLFNSRtvFGNIAYP 106
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRFMAYLGHLPGLKADLSTLENLH--FLCGLHG 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 107 LRLAKLPKNEikervnelLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK13543 112 RRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT 174
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-220 |
4.20e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 26 LSVEKGEIFGIIGFSGAGKSTLLRLVnmlerptAGTISIDDKDItslsakelrklrqrigmIFQSfNLFNSR-------- 97
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRI-----------------IYEQ-DLIVARlqqdpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 98 ---TVFGNIAYPL---------------------------RLAKLpkNEIKE---------RVNELLKFVGLEdkANYYP 138
Cdd:PRK11147 79 vegTVYDFVAEGIeeqaeylkryhdishlvetdpseknlnELAKL--QEQLDhhnlwqlenRINEVLAQLGLD--PDAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 139 EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
..
gi 2050094043 219 VI 220
Cdd:PRK11147 231 LV 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
4.44e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLRQRIGMIFQSFNLFNSRTVF 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAklpknEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:PRK13540 93 ENCLYDIHFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170 180
....*....|....*....|
gi 2050094043 181 NLLKKvNREYNLTILLITHE 200
Cdd:PRK13540 168 TKIQE-HRAKGGAVLLTSHQ 186
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-249 |
6.62e-08 |
|
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: 52.75 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 27 SVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGtiSIDDKD-----ITSLSAKELR----KLRQ---RIGMIFQSFNLF 94
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeiLDEFRGSELQnyftKLLEgdvKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 95 nSRTVFGNIayplrLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:cd03236 100 -PKAVKGKV-----GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 175 TTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMekgkvIEEGKLFDVFTQPKTkttqnfVRSVINDHL 249
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL-----YGEPGAYGVVTLPKS------VREGINEFL 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-206 |
1.17e-07 |
|
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: 53.38 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakelrKLRQRIGMIFQsFNLFNSRTVF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQ-TSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAKLpkneikeRVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:TIGR01271 505 DNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190
....*....|....*....|....*....|....*....
gi 2050094043 170 ALDPETTTEILN--LLKKVNreyNLTILLITHEMHVVKE 206
Cdd:TIGR01271 578 HLDVVTEKEIFEscLCKLMS---NKTRILVTSKLEHLKK 613
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-223 |
1.97e-07 |
|
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: 52.64 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 24 VTLSVEKGEIFGIIGFSGAGKSTLLrlvnmlerptagtisiddkdiTSLSAkELRKLRQRIGMIfqsfnlfnsrtvfGNI 103
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLL---------------------SALLA-EMDKVEGHVHMK-------------GSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 104 AYPLRLAKLPKNEIKERVnellkFVGLEDKANYYPE---------------------------QLSGGQKQRVGIARALA 156
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENI-----LFGKALNEKYYQQvleacallpdleilpsgdrteigekgvNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 157 TSPDILICDEATSALDPETTTEIL-NLLKKVNREYNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-222 |
2.57e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSLS-----------AKELRKlrqRIGMi 87
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTvsdaidaglayVTEDRK---GYGL- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 88 fqsfNLFNsrTVFGNIAyplrLAKLPK-------NEIKE-RVNE------LLKFVGLEDKAnyypEQLSGGQKQRVGIAR 153
Cdd:NF040905 352 ----NLID--DIKRNIT----LANLGKvsrrgviDENEEiKVAEeyrkkmNIKTPSVFQKV----GNLSGGNQQKVVLSK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-179 |
4.86e-07 |
|
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: 50.63 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakelrKLRQRIGMIFQsFNLFNSRTVF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISFSSQ-FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAKLpkneikeRVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:cd03291 116 ENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170
....*....|
gi 2050094043 170 ALDPETTTEI 179
Cdd:cd03291 189 YLDVFTEKEI 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-231 |
6.15e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 26 LSVEKGEIFGIIGFSGAGKSTLLR-LVNMLErPTAGTISIDDKDITSLSakeLRKLRQRIGMIFQSFN---LFNSRTVFG 101
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARaLAGELP-LLSGERQSQFSHITRLS---FEQLQKLVSDEWQRNNtdmLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAyplrlAKLPKNEIK--ERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEI 179
Cdd:PRK10938 100 RTT-----AEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 180 LNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK10938 175 AELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-206 |
9.14e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 11 YESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR--LVNMLERPTAGTISIDDKDITsLSAKELRKLrqrigmif 88
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNegLYASGKARLISFLPKFSRNKL-IFIDQLQFL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 qsfnlfnsrtvfgniayplrlaklpkneikerVNELLKFVGLEDKANyypeQLSGGQKQRVGIARALATSPD--ILICDE 166
Cdd:cd03238 72 --------------------------------IDVGLGYLTLGQKLS----TLSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2050094043 167 ATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKE 206
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSS 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-249 |
9.34e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 28 VEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAG-TISIDDKD--------------ITSLSAKELRKLR--QRIGMIfqs 90
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdYEEEPSWDevlkrfrgtelqnyFKKLYNGEIKVVHkpQYVDLI--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 91 fnlfnSRTVFGNIAYPLRlaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK13409 173 -----PKVFKGKVRELLK-----KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 171 LDpetTTEILNLLKKVnREY--NLTILLITHEMHVVKEICHRVAVM--EKGkvieegkLFDVFTQPKTkttqnfVRSVIN 246
Cdd:PRK13409 243 LD---IRQRLNVARLI-RELaeGKYVLVVEHDLAVLDYLADNVHIAygEPG-------AYGVVSKPKG------VRVGIN 305
|
...
gi 2050094043 247 DHL 249
Cdd:PRK13409 306 EYL 308
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-172 |
1.26e-06 |
|
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: 49.78 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 29 EKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISID-DKDitslsaKELRKLRqriGMIFQSF--NLFNsrtvfGNI-- 103
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpSWD------EVLKRFR---GTELQDYfkKLAN-----GEIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 104 AY-PLRLAKLPKnEIKERVNELLKFVGLEDKANYYPEQ-------------LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:COG1245 163 AHkPQYVDLIPK-VFKGTVRELLEKVDERGKLDELAEKlglenildrdiseLSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
...
gi 2050094043 170 ALD 172
Cdd:COG1245 242 YLD 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-220 |
1.30e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 6 NISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLErPTAGTISIDDKditslsakelrklrQRI 84
Cdd:PRK15064 324 NLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELE-PDSGTVKWSEN--------------ANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 85 GMIFQ--SFNLFNSRTVFGNIAYpLRLAKLPKNEIKERVNELLkFVGleDKANYYPEQLSGGQKQRVGIARALATSPDIL 162
Cdd:PRK15064 385 GYYAQdhAYDFENDLTLFDWMSQ-WRQEGDDEQAVRGTLGRLL-FSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 163 ICDEATSALDPEtTTEILNL-LKKvnreYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:PRK15064 461 VMDEPTNHMDME-SIESLNMaLEK----YEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-173 |
1.39e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLV---------NML-----ERPTAGTISiddkDItslsakelrklRQRIGMIF 88
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgrRRGSGETIW----DI-----------KKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 QSFNL-----FNSRTV-----FGNI----AYPLRLAKLpkneikerVNELLKFVGLEDKANYYPEQ-LSGGQKQRVGIAR 153
Cdd:PRK10938 343 SSLHLdyrvsTSVRNVilsgfFDSIgiyqAVSDRQQKL--------AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVR 414
|
170 180
....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDP 173
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDP 434
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
15-206 |
1.43e-06 |
|
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: 48.41 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTL----------LRLVN-----------MLERPT-------AGTISIDD 66
Cdd:cd03270 5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVEslsayarqflgQMDKPDvdsieglSPAIAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 67 KDITslsakelRKLRQRIGMIFQSFNLFnsRTVFGNIAyplrlaklpkneIKERVNELLKfVGLE----DKANyypEQLS 142
Cdd:cd03270 85 KTTS-------RNPRSTVGTVTEIYDYL--RLLFARVG------------IRERLGFLVD-VGLGyltlSRSA---PTLS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 143 GGQKQRVGIARALATSPD--ILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKE 206
Cdd:cd03270 140 GGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
7-200 |
1.58e-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: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 7 ISKVYESGGQSVHAVEDVTLsveKGEIFGIIGFSGAGKSTLLRLVNM----LERPTAGTISIDDKDITSLSAK---ELRk 79
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEF---FSPLTLIVGQNGAGKTTIIEALKYaltgELPPNSKGGAHDPKLIREGEVRaqvKLA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 80 LRQRIG---MIFQSFNLFnsrtvfgniayplrlaklpKNEIKERVNELLKFVGLEdkanyyPEQLSGGQKQ------RVG 150
Cdd:cd03240 77 FENANGkkyTITRSLAIL-------------------ENVIFCHQGESNWPLLDM------RGRCSGGEKVlasliiRLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTE-ILNLLKKVNREYNLTILLITHE 200
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-200 |
2.00e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 11 YESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLvnMLE--RPTAGTISIDdkdiTSLSAKELRKLRQrigmif 88
Cdd:PRK11147 327 YQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHCG----TKLEVAYFDQHRA------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 89 qsfNLFNSRTVFGNIAYPlrlaklpKNEIKerVNELLKFV--GLED------------KAnyypeqLSGGQKQRVGIARA 154
Cdd:PRK11147 393 ---ELDPEKTVMDNLAEG-------KQEVM--VNGRPRHVlgYLQDflfhpkramtpvKA------LSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2050094043 155 LATSPDILICDEATSALDPETtteiLNLLKKVNREYNLTILLITHE 200
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-223 |
4.08e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 26 LSVEKGEIFGIIGFSGAGKSTLLRLVNMLE--RPTAGTISIDDKDITSLSAKElrKLRQRIGMIFQ--------SFNLFN 95
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQypveipgvSNQFFL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 96 SRTVFGNIAY----PL-------------RLAKLPKNEIKERVNellkfVGLedkanyypeqlSGGQKQRVGIARALATS 158
Cdd:PRK09580 100 QTALNAVRSYrgqePLdrfdfqdlmeekiALLKMPEDLLTRSVN-----VGF-----------SGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 159 PDILICDEATSALDPE---TTTEILNLLKKVNREYnltiLLITHEMHVVKEI-CHRVAVMEKGKVIEEG 223
Cdd:PRK09580 164 PELCILDESDSGLDIDalkIVADGVNSLRDGKRSF----IIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
27-199 |
5.04e-06 |
|
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: 46.88 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 27 SVEKGEIFGIIGFSGAGKSTLLRLVNML---ERPTAGTiSIDDKDITSLSAKELR-----KLRQRIGMIFQSFNLfNSRT 98
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITYAlygKTPRYGR-QENLRSVFAPGEDTAEvsftfQLGGKKYRVERSRGL-DYDQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 99 vFGNIAYplrlakLPKNEIKERvneLLKFVgledkanyypEQLSGGQKQRVGIARALATSP----------DILICDEAT 168
Cdd:cd03279 102 -FTRIVL------LPQGEFDRF---LARPV----------STLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGF 161
|
170 180 190
....*....|....*....|....*....|.
gi 2050094043 169 SALDPETTTEILNLLKKVNREyNLTILLITH 199
Cdd:cd03279 162 GTLDPEALEAVATALELIRTE-NRMVGVISH 191
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-233 |
8.87e-06 |
|
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: 45.64 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 28 VEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakelrklrqrigmifqsfnlfnsrtvfgniaypl 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 108 rlaklpkneikervnellkfvgledkanYYPE--QLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKK 185
Cdd:cd03222 65 ----------------------------YKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2050094043 186 VNREYNLTILLITHEMHVVKEICHRVAVMEKgkvieEGKLFDVFTQPK 233
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEG-----EPGVYGIASQPK 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-172 |
9.16e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 14 GGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNM--------------LERPTAGTisiddkDITSL-----SA 74
Cdd:PLN03073 188 GGRDL--IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGD------DTTALqcvlnTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 75 KELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLRlAKLPKNEIKERVNELLKFVGL------EDKA-------NYYPE-- 139
Cdd:PLN03073 260 IERTQLLEEEAQLVAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEIYKRLELidaytaEARAasilaglSFTPEmq 338
|
170 180 190
....*....|....*....|....*....|....*...
gi 2050094043 140 -----QLSGGQKQRVGIARALATSPDILICDEATSALD 172
Cdd:PLN03073 339 vkatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-219 |
3.22e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 36 IIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakeLRKLRQRIGMIFQ----SFNLFNSRTVFGNIAYPlrlaK 111
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQhhvdGLDLSSNPLLYMMRCFP----G 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 112 LPKNEIKERVNELLKFVGLEDKANYypeQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKvnreYN 191
Cdd:PLN03073 602 VPEQKLRAHLGSFGVTGNLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL----FQ 674
|
170 180
....*....|....*....|....*...
gi 2050094043 192 LTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PLN03073 675 GGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-183 |
5.24e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 36 IIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakelrklRQRIGMIFQSFNLFNSRTVFGNIAYplrlaklpKN 115
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLEMTVFENLKF--------WS 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 116 EIKERVNEL------LKFVGLEDKANYypeQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLL 183
Cdd:PRK13541 96 EIYNSAETLyaaihyFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-221 |
5.46e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISID--------DKDITSLSA----------KELRKLRQ 82
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvNQETPALPQpaleyvidgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIgmifQSFNLFNSrtvfGNIAYPL--RLAKLPKNEIKERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSP 159
Cdd:PRK10636 97 QL----HDANERND----GHAIATIhgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 160 DILICDEATSALDPETTTeilnLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:PRK10636 169 DLLLLDEPTNHLDLDAVI----WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
141-205 |
7.68e-05 |
|
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: 43.76 E-value: 7.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 141 LSGGQKQRVGIARAL---ATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVK 205
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-205 |
7.82e-05 |
|
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: 44.62 E-value: 7.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 141 LSGGQKQRVGIARAL---ATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVK 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 896
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-199 |
8.08e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 33 IFGIIGFSGAGKSTLLRLV----------------NMLERPTAGT--------------ISIDDKDITSLSAKELRKLRQ 82
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIryalygkarsrsklrsDLINVGSEEAsvelefehggkryrIERRQGEFAEFLEAKPSERKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 83 RIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELL-KFVGLEDkanyyPEQLSGGQKQRVGIARALAtspdi 161
Cdd:COG0419 105 ALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILaQLSGLDP-----IETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 2050094043 162 LICDeaTSALDPETTTEILNLLKKvnreynltILLITH 199
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE--------LAIITH 202
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
140-185 |
1.58e-04 |
|
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: 39.91 E-value: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 140 QLSGGQKQ-------------RVGIARALATSPDILICDEATSALDPETTTEILNLLKK 185
Cdd:pfam13558 32 GLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
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| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
33-76 |
6.71e-04 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 40.21 E-value: 6.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2050094043 33 IFGIIGFSGAGKSTLL-RLVNMLERPTAGTISIDD--KDITSLSAKE 76
Cdd:COG0572 9 IIGIAGPSGSGKTTFArRLAEQLGADKVVVISLDDyyKDREHLPLDE 55
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| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
17-205 |
3.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR--LVNMLERPTAG----TISIDDKDITSL------------------ 72
Cdd:PRK00635 607 TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQgfcsNLSIQWGAISRLvhitrdlpgrsqrsiplt 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 73 ---SAKELRKL------RQRIGMI---FqSFNL----------FNSRTVFGN---IAYPLRLAKLPKNEIKE------RV 121
Cdd:PRK00635 687 yikAFDDLRELfaeqprSKRLGLTkshF-SFNTplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVLEvrykgkNI 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 122 NELLKFVGLEDKA--------------------NYYP-----EQLSGGQKQRVGIARAL---ATSPDILICDEATSALDP 173
Cdd:PRK00635 766 ADILEMTAYEAEKffldepsihekihalcslglDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHT 845
|
250 260 270
....*....|....*....|....*....|..
gi 2050094043 174 ETTTEILNLLKKVNREYNlTILLITHEMHVVK 205
Cdd:PRK00635 846 HDIKALIYVLQSLTHQGH-TVVIIEHNMHVVK 876
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-199 |
4.13e-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: 4.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 140 QLSGGQKQRVGIARALA---TSPDILIC-DEATSALDPETTTEILNLLKKvNREYNLTILLITH 199
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITH 139
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-211 |
4.65e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 4.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 141 LSGGQKQRVGIARALAT--SPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVkEICHRV 211
Cdd:PRK00635 477 LSGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRI 547
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