|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-257 |
3.20e-161 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 450.30 E-value: 3.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSL 238
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260
....*....|....*....|....*
gi 1610668340 239 LHD------PQAERDFLARHGLHGR 257
Cdd:COG1135 241 LPTvlndelPEELLARLREAAGGGR 265
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-257 |
5.35e-141 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 399.56 E-value: 5.35e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:PRK11153 1 MIELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSL 238
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260
....*....|....*....|....*
gi 1610668340 239 LHD------PQAERDFLARHGLHGR 257
Cdd:PRK11153 241 IQStlhldlPEDYLARLQAEPTTGS 265
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
2.94e-140 |
|
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: 393.49 E-value: 2.94e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGR--PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-239 |
2.22e-102 |
|
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: 301.42 E-value: 2.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSL 238
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
.
gi 1610668340 239 L 239
Cdd:TIGR02314 241 I 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-251 |
2.54e-94 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 277.26 E-value: 2.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrMDKSALREYRL 80
Cdd:COG1126 1 MIEIENLHKSFGDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAV-PLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGriadllvAPwsrlrQSLL 239
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG-------PP-----EEFF 224
|
250
....*....|....
gi 1610668340 240 HDPQAER--DFLAR 251
Cdd:COG1126 225 ENPQHERtrAFLSK 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
1.11e-91 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 269.99 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYA--GTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRT-GMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:COG1136 84 RRRHiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKtLCDHAALLEHGEIIESGR 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSDER 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
6.31e-90 |
|
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: 275.24 E-value: 6.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGR---PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALRE 77
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRLRTGMIFQH----FNllHARSVADNVAVPLEIAKV-PKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIAR 151
Cdd:COG1123 340 LRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPW 231
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*...
gi 1610668340 232 SRLRQSLL 239
Cdd:COG1123 498 HPYTRALL 505
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
2.29e-88 |
|
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: 262.22 E-value: 2.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:COG1127 5 MIEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPL-EIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQ 236
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQ 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
4.36e-88 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 260.50 E-value: 4.36e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGR--PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYR 79
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 LRT-GMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03255 81 RRHiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKtLCDHAALLEHGEI 217
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
8.46e-86 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 254.98 E-value: 8.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYaGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:COG2884 1 MIRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQkLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGR 222
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
5.22e-82 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 245.13 E-value: 5.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmDKSALREYRLR 81
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAV-PLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
3.64e-81 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 244.20 E-value: 3.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:COG3638 2 MLELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNV------AVPLE---IAKVPKAARQaRVAELLELVGLADKAAAFPSQLSGGQKQRVGIAR 151
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgRTSTWrslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-230 |
1.82e-80 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 246.94 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKT--YAGTGR-PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRT 82
Cdd:COG4175 27 GKSKDeiLEKTGQtVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 -GMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:COG4175 107 mSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPettasvL------NLLADINQKLNLTIVLITHEL-EVVKtLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:COG4175 187 MDEAFSALDP------LirremqDELLELQAKLKKTIVFITHDLdEALR-LGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
1.64e-79 |
|
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: 239.70 E-value: 1.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY--AGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksALREY 78
Cdd:COG1124 1 MLEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR---RRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQH-FNLLHAR-SVADNVAVPLEIAKVPkaARQARVAELLELVGLADKAAA-FPSQLSGGQKQRVGIARALAA 155
Cdd:COG1124 78 RRRVQMVFQDpYASLHPRhTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDrYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 156 RPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-221 |
2.46e-77 |
|
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: 233.55 E-value: 2.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQH-FNLLHAR-SVADNVAVPLEIAKVP--KAARQARVAELLELVGLADKAA-AFPSQLSGGQKQRVGIARAL 153
Cdd:cd03257 81 RKEIQMVFQDpMSSLNPRmTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEEVLnRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 154 AARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-226 |
9.70e-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: 232.46 E-value: 9.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYaGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLR 81
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAK---------VPKAARQaRVAELLELVGLADKAAAFPSQLSGGQKQRVGIARA 152
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-230 |
6.75e-76 |
|
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: 231.38 E-value: 6.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRT-GMIFQHFNLLHAR 95
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKiSMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTA 175
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 176 SVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-243 |
7.65e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 231.13 E-value: 7.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY--AGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalrey 78
Cdd:COG1116 7 ALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:COG1116 81 --DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHEL-EVVkTLCDHAALLEHGeiieSGRIADLLVAPWSRLR-Q 236
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdEAV-FLADRVVVLSAR----PGRIVEEIDVDLPRPRdR 233
|
....*..
gi 1610668340 237 SLLHDPQ 243
Cdd:COG1116 234 ELRTSPE 240
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
1.53e-75 |
|
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: 229.14 E-value: 1.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRLR 81
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:COG1122 77 VGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
1.09e-74 |
|
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: 229.94 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRC-LNLLERP--TAGRIIVNGNDITRMDKSAL 75
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAiLGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 76 REYRLRT-GMIFQH-FNLLHAR-SVADNVAVPLEI-AKVPKAARQARVAELLELVGLADKAA---AFPSQLSGGQKQRVG 148
Cdd:COG0444 81 RKIRGREiQMIFQDpMTSLNPVmTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 149 IARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLV 228
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
..
gi 1610668340 229 AP 230
Cdd:COG0444 241 NP 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-236 |
2.07e-74 |
|
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: 226.61 E-value: 2.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLR 81
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPL-EIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQ 236
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQ 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
4.90e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 229.60 E-value: 4.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksaLREYRL 80
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLL-HaRSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:COG3842 78 NVGMVFQDYALFpH-LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-221 |
1.26e-73 |
|
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: 223.55 E-value: 1.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalreYRLR 81
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-----ERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-227 |
2.83e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 223.40 E-value: 2.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrlR 81
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-230 |
7.92e-73 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 225.77 E-value: 7.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTG----RP-----ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDK 72
Cdd:COG4608 8 LEVRDLKKHFPVRGglfgRTvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 73 SALREYRLRTGMIFQH-FNLLHAR-SVADNVAVPLEIAKV-PKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVG 148
Cdd:COG4608 88 RELRPLRRRMQMVFQDpYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 149 IARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLV 228
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYA 247
|
..
gi 1610668340 229 AP 230
Cdd:COG4608 248 RP 249
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
7.31e-72 |
|
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: 220.25 E-value: 7.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYaGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:TIGR02315 1 MLEVENLSKVY-PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAK---------VPKAARQaRVAELLELVGLADKAAAFPSQLSGGQKQRVGIAR 151
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgrFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEII 218
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-216 |
3.04e-70 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 215.02 E-value: 3.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 3 EIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYRLRT 82
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT---KLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 GMIFQHFNL-LHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGE 216
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-227 |
1.95e-68 |
|
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: 210.79 E-value: 1.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalreyr 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 lRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:cd03293 74 -DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEhgeiIESGRIADLL 227
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS----ARPGRIVAEV 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-230 |
5.44e-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: 210.23 E-value: 5.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR---K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADK--AAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
1.59e-66 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 207.35 E-value: 1.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDItRM---------- 70
Cdd:COG4598 8 ALEVRDLHKSFGD--LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLkpdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 71 -DKSALREYRLRTGMIFQHFNLLHARSVADNV-AVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVG 148
Cdd:COG4598 85 aDRRQLQRIRTRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 149 IARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNlTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLV 228
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
250
....*....|.
gi 1610668340 229 APWS-RLRQSL 238
Cdd:COG4598 244 NPKSeRLRQFL 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
1.75e-66 |
|
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: 204.34 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSaLREYRLR 81
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLeiakvpkaarqarvaellelvgladkaaafpsqlSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGE 216
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-221 |
1.83e-65 |
|
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: 203.57 E-value: 1.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL-----ERPTAGRIIVNGNDITRMDKSALr 76
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 77 EYRLRTGMIFQHFNLLHArSVADNVAVPLEIAKV-PKAARQARVAELLELVGLADKAA--AFPSQLSGGQKQRVGIARAL 153
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 154 AARPDVLLCDEATSALDPETTASVLNLLADINQKlnLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
2.07e-65 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 203.71 E-value: 2.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDI---TRMDKSALREY 78
Cdd:COG4161 3 IQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADN-VAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-230 |
2.20e-65 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 207.31 E-value: 2.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdkSALREYRLR 81
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
5.69e-65 |
|
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: 210.92 E-value: 5.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTA---GRIIVNGNDITRMDKSALRE 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 yrlRTGMIFQHF-NLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAAR 156
Cdd:COG1123 84 ---RIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-246 |
2.23e-64 |
|
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: 201.89 E-value: 2.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDitRMDKSALREYRLR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLLVAPwSRLRQSLLH 240
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQV-ELLKEIGLD 236
|
....*.
gi 1610668340 241 DPQAER 246
Cdd:TIGR04520 237 VPFITE 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-217 |
2.57e-64 |
|
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: 199.94 E-value: 2.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLR 81
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-240 |
4.83e-63 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 197.62 E-value: 4.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDItRMDKSALREYRL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAV-PLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWS-RLRQSL 238
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSqRLQEFL 236
|
..
gi 1610668340 239 LH 240
Cdd:PRK09493 237 QH 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-238 |
2.22e-62 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 196.51 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNgnDIT-------RMDKS 73
Cdd:PRK11264 3 AIEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITidtarslSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 74 ALREYRLRTGMIFQHFNLLHARSVADNVAV-PLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARA 152
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPW- 231
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQq 237
|
....*..
gi 1610668340 232 SRLRQSL 238
Cdd:PRK11264 238 PRTRQFL 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-221 |
5.76e-61 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 192.54 E-value: 5.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDI---TRMDKSALREY 78
Cdd:PRK11124 3 IQLNGINCFYGAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADN-VAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-233 |
9.68e-60 |
|
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: 188.98 E-value: 9.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksaLREYRLR 81
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSR 233
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-230 |
1.66e-59 |
|
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: 196.83 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRC-LNLLerPTAGRIIVNGNDITRMDKSALREYRLRTGMIFQH-FNLLHAR 95
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLAlLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFGSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 -SVADNVAVPLEIAKVP--KAARQARVAELLELVGLaDKAAA--FPSQLSGGQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:COG4172 379 mTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGL-DPAARhrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 171 PETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:COG4172 458 VSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-217 |
1.29e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 189.90 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSAlreyRl 80
Cdd:COG3839 3 SLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----R- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-255 |
2.52e-58 |
|
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: 186.89 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYA-GTG--RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQhF--NLLHARSVADNVA-------VPLEIAKvpkaarqARVAELLELVGL----ADKAaafPSQLSGGQKQ 145
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAfgpknlgLSEEEAE-------ERVKEALELVGLdeeyLERS---PFELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 146 RVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
250 260 270
....*....|....*....|....*....|
gi 1610668340 226 LLvapwsrlrqsllhdpqAERDFLARHGLH 255
Cdd:TIGR04521 230 VF----------------SDVDELEKIGLD 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
4.12e-58 |
|
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: 184.94 E-value: 4.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLR-TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARvaELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKtLCDHAALLEHGEIIESGR 222
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTA 229
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
19-239 |
8.45e-58 |
|
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: 184.65 E-value: 8.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRM----------DKSALREYRLRTGMIFQH 88
Cdd:TIGR03005 16 LDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMpgrngplvpaDEKHLRQMRNKIGMVFQS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 89 FNLLHARSVADNVA-VPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATS 167
Cdd:TIGR03005 96 FNLFPHKTVLDNVTeAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 168 ALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSLL 239
Cdd:TIGR03005 176 ALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFL 247
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-230 |
3.09e-57 |
|
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: 182.92 E-value: 3.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRLr 81
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tGMIFQHFNLLHARSVADNVAVPLEIAKV----PKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:cd03296 77 -GFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-238 |
6.58e-56 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 180.16 E-value: 6.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRM----------DKSALREYRLRTGMIFQH 88
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 89 FNLLHARSVADNV-AVPLEIAKVPKAARQARVAELLELVGLADKA-AAFPSQLSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:PRK10619 101 FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 167 SALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWS-RLRQSL 238
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSpRLQQFL 252
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
7.34e-56 |
|
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: 176.82 E-value: 7.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksALREYRLR 81
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVavpleiakvpkaarqarvaellelvgladkaaafpsQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-230 |
1.66e-55 |
|
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: 186.43 E-value: 1.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGR--PALNDVSLHVPGGAVYGILGRSGAGKS-TLIRCLNLLERPTA---GRIIVNGNDITRMDKSA 74
Cdd:COG4172 6 LLSVEDLSVAFGQGGGtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 75 LREYR-LRTGMIFQH----FNLLHarSVADNVAVPLEI-AKVPKAARQARVAELLELVGLAD---KAAAFPSQLSGGQKQ 145
Cdd:COG4172 86 LRRIRgNRIAMIFQEpmtsLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 146 RVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
....*
gi 1610668340 226 LLVAP 230
Cdd:COG4172 244 LFAAP 248
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
1.80e-55 |
|
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: 178.69 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksalREYRL 80
Cdd:COG0411 4 LLEVRGLTKRFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-----PPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 -RTGMI--FQHFNLLHARSVADNVAVPLE----------IAKVPKAARQ-----ARVAELLELVGLADKAAAFPSQLSGG 142
Cdd:COG0411 77 aRLGIArtFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRARREerearERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 143 QKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGR 222
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
...
gi 1610668340 223 IAD 225
Cdd:COG0411 237 PAE 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
4.51e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 178.13 E-value: 4.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTG--RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmDKSALRey 78
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlrtGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELE 200
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
4.66e-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: 188.12 E-value: 4.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR---Q 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHfNLLHARSVADNVAVPLEiakvpkAARQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:COG2274 551 IGVVLQD-VFLFSGTIRENITLGDP------DATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKtLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELL 697
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-227 |
7.29e-54 |
|
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: 174.46 E-value: 7.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRL 80
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS---RRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAV---P-LEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAAR 156
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
2.68e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.54 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSktYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRLR 81
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHArSVADNVAVPLEIAKvpKAARQARVAELLELVGLADKAAAFP-SQLSGGQKQRVGIARALAARPDVL 160
Cdd:COG4619 76 VAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-225 |
2.96e-53 |
|
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: 172.62 E-value: 2.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdkSALREYRLR 81
Cdd:cd03219 1 LEVRGLTKRFGGL--VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL--PPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEI--------AKVPKAARQAR--VAELLELVGLADKAAAFPSQLSGGQKQRVGIAR 151
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVMVAAQArtgsglllARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-227 |
2.99e-53 |
|
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: 172.73 E-value: 2.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrl 80
Cdd:COG4555 1 MIEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINqKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
2.49e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.27 E-value: 2.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksalreyRL 80
Cdd:COG1121 6 AIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLlhAR----SVADNVA----VPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARA 152
Cdd:COG1121 76 RIGYVPQRAEV--DWdfpiTVRDVVLmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGeIIESGRIADLL 227
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVL 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-226 |
7.49e-52 |
|
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: 168.32 E-value: 7.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksALREYRLR 81
Cdd:cd03265 1 IEVENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-227 |
1.11e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 168.39 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrpALNdVSLHVPGGAVYGILGRSGAGKSTLircLNLL---ERPTAGRIIVNGNDITRMDKSAlre 77
Cdd:COG3840 1 MLRLDDLTYRYGDF---PLR-FDLTIAAGERVAILGPSGAGKSTL---LNLIagfLPPDSGRILWNGQDLTALPPAE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 yRLRTgMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:COG3840 71 -RPVS-MLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-230 |
2.18e-51 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 168.29 E-value: 2.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL--ERPTA---GRIIVNGNDI--TRMDKSA 74
Cdd:COG1117 12 IEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 75 LReyrLRTGMIFQHFNLLhARSVADNVAVPLEIAKV-PKAARQARVAELLELVGLAD------KAAAFpsQLSGGQKQRV 147
Cdd:COG1117 90 LR---RRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevkdrlKKSAL--GLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADInqKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
...
gi 1610668340 228 VAP 230
Cdd:COG1117 242 TNP 244
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
2.26e-51 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 169.04 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGndiTRMDKSALREYRLR 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHEL-EVVKTlcDHAALLEHGEIIESG 221
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLdEAAQA--DRVIVMNKGEILEEG 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
2.53e-50 |
|
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: 162.94 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK---N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHArSVADNVavpleiakvpkaarqarvaellelvgladkaaafpsqLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKtLCDHAALLEHGE 216
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-202 |
2.92e-50 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 164.28 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:PRK10908 1 MIRFEHVSKAYLG-GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINqKLNLTIVLITHELEVV 202
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLI 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-227 |
1.15e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.50 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIrclNLLER---PTAGRIIVNGNDITRMDKSALREy 78
Cdd:COG1132 340 IEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLV---NLLLRfydPTSGRILIDGVDIRDLTLESLRR- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlRTGMIFQHFNLLHaRSVADNVAvpleIAKvPKAARqARVAELLELVGLADKAAAFP-----------SQLSGGQKQRV 147
Cdd:COG1132 415 --QIGVVPQDTFLFS-GTIRENIR----YGR-PDATD-EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-226 |
3.37e-49 |
|
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: 161.52 E-value: 3.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrlR 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQ----S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 162 CDEATSALDPETTASVLNLLADInqKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-237 |
3.44e-49 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 162.93 E-value: 3.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGTG-------RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY 78
Cdd:PRK10419 8 GLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQH----FNLLHarSVADNVAVPLE-IAKVPKAARQARVAELLELVGLADK-AAAFPSQLSGGQKQRVGIARA 152
Cdd:PRK10419 88 RRDIQMVFQDsisaVNPRK--TVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLV--AP 230
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTfsSP 245
|
....*..
gi 1610668340 231 WSRLRQS 237
Cdd:PRK10419 246 AGRVLQN 252
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-254 |
3.55e-49 |
|
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: 165.66 E-value: 3.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGN---DITRmdKSALREYRLRTGMIFQHFNLLHARSV 97
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSAR--GIFLPPHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNvavpLE--IAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTA 175
Cdd:COG4148 95 RGN----LLygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 176 SVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL----VAPWSRLRQ--SLLHDPQAERDfl 249
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLsrpdLLPLAGGEEagSVLEATVAAHD-- 248
|
....*
gi 1610668340 250 ARHGL 254
Cdd:COG4148 249 PDYGL 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-233 |
2.34e-48 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 163.33 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdkSAlREYRLr 81
Cdd:PRK10851 3 IEIANIKKSFGRT--QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HA-RDRKV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tGMIFQHFNLLHARSVADNVAVPLEIakVPK------AARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAA 155
Cdd:PRK10851 77 -GFVFQHYALFRHMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 156 RPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSR 233
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-221 |
2.54e-48 |
|
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: 158.96 E-value: 2.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksaLREYRLR 81
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD-----LPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARV---AELLELVGLADKaaaFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVrevAELLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-239 |
3.54e-48 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 162.06 E-value: 3.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYA---GTGRP-----ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKS 73
Cdd:PRK11308 6 LQAIDLKKHYPvkrGLFKPerlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 74 ALREYRLRTGMIFQH-FNLLHAR-SVADNVAVPLEI-AKVPKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGI 149
Cdd:PRK11308 86 AQKLLRQKIQIVFQNpYGSLNPRkKVGQILEEPLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 150 ARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVA 229
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
250
....*....|
gi 1610668340 230 PWSRLRQSLL 239
Cdd:PRK11308 246 PRHPYTQALL 255
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-221 |
4.17e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 158.47 E-value: 4.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksalreyRLRTGMIFQHF 89
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 90 NLLHAR--SVADNVAVPLEIAKV----PKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCD 163
Cdd:cd03235 78 SIDRDFpiSVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 164 EATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHgEIIESG 221
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
5.75e-48 |
|
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: 158.13 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGaVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksalREYRLR 81
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP----QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNL---LHARSVADNVAVpleIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03264 74 IGYLPQEFGVypnFTVREFLDYIAW---LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-234 |
1.71e-47 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 161.93 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalreYRL 80
Cdd:PRK11607 19 LLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-----YQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRL 234
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.95e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 158.23 E-value: 2.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDItrmDKSALREYRL 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-242 |
3.07e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 158.36 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY-AGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYR 79
Cdd:PRK13650 4 IIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 LRTGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVkTLCDHAALLEHGEiIESGRIADLLVAPWSRLRQSL 238
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ-VESTSTPRELFSRGNDLLQLG 238
|
....
gi 1610668340 239 LHDP 242
Cdd:PRK13650 239 LDIP 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-167 |
3.84e-47 |
|
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: 153.96 E-value: 3.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRLRTGMIFQHFNLLHARSVA 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 99 DNVAVPLEIAKVPKAARQARVAELLELVGLADKAA----AFPSQLSGGQKQRVGIARALAARPDVLLCDEATS 167
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-230 |
4.42e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 161.35 E-value: 4.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRT-GMIFQHFNLLHARS 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKiAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 97 VADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTAS 176
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 177 VLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
6.57e-47 |
|
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: 154.52 E-value: 6.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 3 EIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksalreyrlrt 82
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 gmifqhfnllhARSVADNVAVpleiakVPKAarqarvaelLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLC 162
Cdd:cd03214 68 -----------PKELARKIAY------VPQA---------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 163 DEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
8.13e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 160.11 E-value: 8.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalrEYR-L 80
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA----ENRhV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTgmIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK09452 89 NT--VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
9.76e-47 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 153.17 E-value: 9.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 3 EIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRLRT 82
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 GMIFQhfnllharsvadnvavpleiakvpkaarqarvaellelvgladkaaafpsqLSGGQKQRVGIARALAARPDVLLC 162
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 163 DEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGE 216
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
1.63e-46 |
|
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: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:COG4988 337 IELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR---Q 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHArSVADNVAvpleIAKvpKAARQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:COG4988 413 IAWVPQNPYLFAG-TIRENLR----LGR--PDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKtLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
1.82e-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: 151.60 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmDKSALReyrlR 81
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALR----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKaarqARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-230 |
4.30e-45 |
|
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: 151.33 E-value: 4.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYagtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalrEYRlR 81
Cdd:cd03299 1 LKVENLSKDW---KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP----EKR-D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-240 |
4.67e-45 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 152.30 E-value: 4.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYA-GTG------RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSa 74
Cdd:COG4167 5 LEVRNLSKTFKyRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 75 LREYRLRtgMIFQHFNL-LHARS-VADNVAVPLEIA-KVPKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIA 150
Cdd:COG4167 84 YRCKHIR--MIFQDPNTsLNPRLnIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
250
....*....|
gi 1610668340 231 WSRLRQSLLH 240
Cdd:COG4167 242 QHEVTKRLIE 251
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-221 |
5.01e-45 |
|
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: 150.52 E-value: 5.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVyGILGRSGAGKSTLIRCLNLLERPTAGRIIVNG---NDiTRMdKSALREYRLRTGMIFQHFNLLHARSV 97
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFD-SRK-KINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAVPLEiaKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASV 177
Cdd:cd03297 93 RENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1610668340 178 LNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-254 |
5.41e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 152.21 E-value: 5.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYrl 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 rTGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK13648 85 -IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHEL-EVVKTlcDHAALLEHGEIIESGRIADL-----------L 227
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAMEA--DHVIVMNKGTVYKEGTPTEIfdhaeeltrigL 241
|
250 260
....*....|....*....|....*...
gi 1610668340 228 VAPWS-RLRQSLLHDPqaerDFLARHGL 254
Cdd:PRK13648 242 DLPFPiKINQMLGHQT----SFLTYEGL 265
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
1.48e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 150.18 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITR--MDKsalrey 78
Cdd:COG1137 3 TLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGM--------IFQhfNLlharSVADNVAVPLEIAKVPKAARQARVAELLE---LVGLADKAAafpSQLSGGQKQRV 147
Cdd:COG1137 75 RARLGIgylpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEefgITHLRKSKA---YSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPettASVlnllADInQKL--NLT---I-VLIT-HelEVVKTL--CDHAALLEHGEII 218
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDP---IAV----ADI-QKIirHLKergIgVLITdH--NVRETLgiCDRAYIISEGKVL 215
|
....*....
gi 1610668340 219 ESGRIADLL 227
Cdd:COG1137 216 AEGTPEEIL 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.54e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 151.38 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAgTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDItRMDKSALREYRL 80
Cdd:PRK13639 1 ILETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHF-NLLHARSVADNVAV-PLEIaKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:PRK13639 79 TVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-221 |
1.90e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 151.39 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYA----GTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmDKSALR 76
Cdd:PRK13633 4 MIKCKNVSYKYEsneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 77 EYRLRTGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAA 155
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 156 RPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHEL-EVVKTlcDHAALLEHGEIIESG 221
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
1.97e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.33 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:COG1129 4 LLEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 rtGMIFQHFNLLHARSVADNVAVPLEIAK---VPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:COG1129 82 --AIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
3.50e-44 |
|
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: 156.85 E-value: 3.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLLER---PTAGRIIVNGNDITRMDKSALREy 78
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL---LALLLRfldPQSGSITLGGVDLRDLDEDDLRR- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlRTGMIFQHFNLLHArSVADNvavpLEIAKvpKAARQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRV 147
Cdd:COG4987 410 --RIAVVPQRPHLFDT-TLREN----LRLAR--PDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELL 557
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-221 |
3.51e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 150.72 E-value: 3.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTA---GRIIVNGNDITRMDKSALREy 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlRTGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:PRK13640 85 --KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVkTLCDHAALLEHGEIIESG 221
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-233 |
9.84e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 148.69 E-value: 9.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmDKSALReyrl 80
Cdd:PRK11248 1 MLQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 rtGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK11248 73 --GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGeiieSGRIADLLVAPWSR 233
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG----PGRVVERLPLNFAR 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-225 |
3.07e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 148.27 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTY-AGT--GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmDKSA-LRE 77
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVkLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRLRTGMIFQHFNL-LHARSVADNVAVPLEIAKVPKAARQARVAELLELVGL-----ADKAaafPSQLSGGQKQRVGIAR 151
Cdd:PRK13637 81 IRKKVGLVFQYPEYqLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
7.37e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 146.21 E-value: 7.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL-----ERPTAGRIIVNGNDITRMDKSALR 76
Cdd:PRK14247 4 IEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 77 EyrlRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAAR--QARVAELLELVGL----ADKAAAFPSQLSGGQKQRVGIA 150
Cdd:PRK14247 82 R---RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADInqKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-217 |
2.60e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 145.21 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 4 IVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVnGNditrmdkSALREYRLRTG 83
Cdd:PRK11247 15 LNAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GT-------APLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 84 MIFQHFNLLHARSVADNVAVPLEiAKVPKAARQArvaelLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCD 163
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLK-GQWRDAALQA-----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 164 EATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-247 |
4.57e-42 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 146.39 E-value: 4.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRTGMIFQH-FNLLHAR- 95
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDpLASLNPRm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEI--AKVPKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPE 172
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 173 TTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSLLH-----DPQAERD 247
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSavpipDPDLERN 275
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-226 |
4.86e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 145.25 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA---LRE 77
Cdd:COG4152 1 MLELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigyLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YR-LRTGMifqhfnllharSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAAR 156
Cdd:COG4152 79 ERgLYPKM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-227 |
6.77e-42 |
|
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: 142.96 E-value: 6.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsalrEYRLR 81
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP----HERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIF--QHFNLLHARSVADNVAVPLEIAKvpKAARQARVAELLELV-GLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03224 75 AGIGYvpEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-227 |
7.32e-42 |
|
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: 143.40 E-value: 7.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHfNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELV-----GLADKAAAFPSQLSGGQKQRVGIARALAAR 156
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-238 |
7.96e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 144.14 E-value: 7.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSktYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPL-EIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSL 238
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFL 243
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-227 |
3.62e-41 |
|
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: 141.52 E-value: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTlirCLNLLER---PTAGRIIVNGNDITRMdksALREYRLRTGMIFQHFNLLh 93
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDL---NLRWLRSQIGLVSQEPVLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAVPLEIAKVPKAARQARVAELLELV-GLADK----AAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSA 168
Cdd:cd03249 90 DGTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 169 LDPETTASVLNLLADInqKLNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:cd03249 170 LDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-225 |
4.32e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.48 E-value: 4.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGnditrmdksalREYRL 80
Cdd:COG3845 5 ALELRGITKRFGGV--VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----------KPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RT---------GMIFQHFNLLHARSVADNVAVPLEIAKVP----KAARqARVAELLELVGLADKAAAFPSQLSGGQKQRV 147
Cdd:COG3845 72 RSprdaialgiGMVHQHFMLVPNLTVAENIVLGLEPTKGGrldrKAAR-ARIRELSERYGLDVDPDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-205 |
8.57e-41 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 140.34 E-value: 8.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRT-GMIFQHFNLLHARSV 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKlGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASV 177
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180
....*....|....*....|....*...
gi 1610668340 178 LNLLADINQKLNLTIVLITHELEVVKTL 205
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-241 |
1.24e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 143.32 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYRLrtGMIFQHFNLLHARSVA 98
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQRDI--CMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 99 DNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVL 178
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 179 NLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSLLHD 241
Cdd:PRK11432 177 EKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-227 |
2.36e-40 |
|
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: 139.29 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIrclNLLER---PTAGRIIVNGNDITRMDKSALREY 78
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLV---NLIPRfydVDSGRILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlrTGMIFQHFNLLHArSVADNVAVPLEIAKVPKAARQARVAELLELV-----GLADKAAAFPSQLSGGQKQRVGIARAL 153
Cdd:cd03251 78 ---IGLVSQDVFLFND-TVAENIAYGRPGATREEVEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 154 AARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-243 |
9.17e-40 |
|
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: 137.60 E-value: 9.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALreyrlrtgMIFQHFNLLHARSVA 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 99 DNVAVPLE--IAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTAS 176
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 177 VLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVaPWSRLRQSLLHDPQ 243
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPF-PRPRDRLEVVEDPS 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
1.24e-39 |
|
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: 137.29 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITR--MDKsalreyR 79
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHK------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 LRTGMIF--QHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:cd03218 73 ARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKlNLTiVLIT-HELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-201 |
1.54e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 144.87 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY-AGTGRPA-LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSAL--- 75
Cdd:PRK10535 4 LLELKDIRRSYpSGEEQVEvLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 76 -REYrlrTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALA 154
Cdd:PRK10535 84 rREH---FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1610668340 155 ARPDVLLCDEATSALDPETTASVLNLLADINQKLNlTIVLITHELEV 201
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQV 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-227 |
1.57e-39 |
|
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: 136.98 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlRTGMIFQHFNLLH 93
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR---AIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ArSVADNVAVPLEIA---KVPKAARQARVAELLElvgladkaaAFPSQ-----------LSGGQKQRVGIARALAARPDV 159
Cdd:cd03253 89 D-TIGYNIRYGRPDAtdeEVIEAAKAAQIHDKIM---------RFPDGydtivgerglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-244 |
8.31e-39 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 138.32 E-value: 8.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA-LREYRLRTGMIFQHFNLLHARSVAD 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIfLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 100 NVAVPLEIAKVPKaaRQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLN 179
Cdd:TIGR02142 95 NLRYGMKRARPSE--RRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 180 LLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLlvapWSRLRQSLLHDPQA 244
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV----WASPDLPWLAREDQ 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-236 |
1.03e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.95 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL------ERPTAGRIIVNGNDITRMDKSALREyrlRTGMIFQHFNLL 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRK---EVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 HARSVADNVAVPLEIAKVpKAARQAR--VAELLELVGL----ADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGI-KEKREIKkiVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 167 SALDPETTASVLNLLADInqKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQ 236
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-218 |
1.08e-38 |
|
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: 133.92 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 3 EIVGLSKTYAGTGRpALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksalREYRLRT 82
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 GMIFQHFNL-LHARSVADNVAVPLEIAkvpkAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03226 74 GYVMQDVDYqLFTDSVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 162 CDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEII 218
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-218 |
3.90e-38 |
|
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: 131.40 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGnditrmdksalREYRLR 81
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------KEVSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TgmifqhfnllharsvadnvavpleiakvPKAARQARVAelleLVgladkaaafpSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03216 68 S----------------------------PRDARRAGIA----MV----------YQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 162 CDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEII 218
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-221 |
7.72e-38 |
|
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: 132.73 E-value: 7.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlRTGMIFQHfNLLHA 94
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS---MIGVVLQD-TFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 95 RSVADNVAVPLEIAKVPKAARQARVAELLELV-----GLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSAL 169
Cdd:cd03254 91 GTIMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 170 DPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESG 221
Cdd:cd03254 171 DTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-239 |
1.42e-37 |
|
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: 132.03 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdkSAlrEYRL 80
Cdd:COG0410 3 MLEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL--PP--HRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGM--------IFQHFnllharSVADNVAVPLEIAKvPKAARQARVAELLELvgladkaaaFP----------SQLSGG 142
Cdd:COG0410 77 RLGIgyvpegrrIFPSL------TVEENLLLGAYARR-DRAEVRADLERVYEL---------FPrlkerrrqraGTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 143 QKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGR 222
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
250
....*....|....*..
gi 1610668340 223 IADLLVAPwsRLRQSLL 239
Cdd:COG0410 220 AAELLADP--EVREAYL 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
1.93e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.22 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTY-AGT--GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA-LRE 77
Cdd:PRK13634 3 ITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRLRTGMIFQhF--NLLHARSVADNVAV-PLEIAkVPKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIARAL 153
Cdd:PRK13634 83 LRKKVGIVFQ-FpeHQLFEETVEKDICFgPMNFG-VSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 154 AARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-230 |
4.01e-37 |
|
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: 138.55 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR---Q 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHArSVADNVA--VPLEIAKVPKAARqarvaelleLVGLADKAAAFP-----------SQLSGGQKQRVG 148
Cdd:TIGR03797 529 LGVVLQNGRLMSG-SIFENIAggAPLTLDEAWEAAR---------MAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 149 IARALAARPDVLLCDEATSALDPETTASVLNLLAdinqKLNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLV 228
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
..
gi 1610668340 229 AP 230
Cdd:TIGR03797 674 RE 675
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
4.73e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.12 E-value: 4.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLsKTYAGTGRpALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL-----ERPTAGRIIVNGNDITRMDKSALr 76
Cdd:PRK14267 5 IETVNL-RVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 77 EYRLRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARqarvaELLELVGLADKAAA-----------FPSQLSGGQKQ 145
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKK-----ELDERVEWALKKAAlwdevkdrlndYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 146 RVGIARALAARPDVLLCDEATSALDPETTASVLNLLADInqKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-208 |
5.37e-37 |
|
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: 130.25 E-value: 5.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYA-----GTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGN----DITRMD 71
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 72 KS---ALREYRLrtGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADK-AAAFPSQLSGGQKQRV 147
Cdd:COG4778 84 PReilALRRRTI--GYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDH 208
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADR 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-221 |
8.80e-37 |
|
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: 129.54 E-value: 8.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSalreyRLRTGMIFQHFNLLHARSVADN 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 101 VAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNL 180
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1610668340 181 LADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
2.76e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.97 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKsALREYRLRTGMIFQH-FNLLH 93
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK-GLMKLRESVGMVFQDpDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPET 173
Cdd:PRK13636 97 SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 174 TASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-217 |
5.46e-36 |
|
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: 126.18 E-value: 5.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDksaLREYRLR 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLhARSVADNVavpleiakvpkaarqarvaellelvgladkaaafpsqLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVkTLCDHAALLEHGEI 217
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
6.29e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 129.15 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYRL 80
Cdd:PRK13652 3 LIETRDLCYSYSGS-KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFN-LLHARSVADNVAV-PLEIAkVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:PRK13652 79 FVGLVFQNPDdQIFSPTVEQDIAFgPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-229 |
8.38e-36 |
|
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: 134.07 E-value: 8.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIrclNLLER---PTAGRIIVNGNDITRMdksALREY 78
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV---NLIPRfyePDSGQILLDGHDLADY---TLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHArSVADNVAVPlEIAKVPKA--ARQARVAELLELVGLADKAAAFP-----SQLSGGQKQRVGIAR 151
Cdd:TIGR02203 405 RRQVALVSQDVVLFND-TIANNIAYG-RTEQADRAeiERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLVA 229
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-221 |
9.57e-36 |
|
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: 133.39 E-value: 9.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLE--RPTAGRIIVN---------------- 63
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 64 -------GN-------DITRMDKSALREYRLRTGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGL 128
Cdd:TIGR03269 79 gepcpvcGGtlepeevDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 129 ADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDH 208
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|...
gi 1610668340 209 AALLEHGEIIESG 221
Cdd:TIGR03269 239 AIWLENGEIKEEG 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-226 |
1.17e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 128.32 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTY-AGT--GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA-LRE 77
Cdd:PRK13649 3 INLQNVSYTYqAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRLRTGMIFQhF--NLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKA-AAFPSQLSGGQKQRVGIARALA 154
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 155 ARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-239 |
1.60e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.91 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 12 AGTGRPALNDVSLHVPGGAVYGILGRSGAGKS-TLIRCLNLLERP----TAGRIIVNGNDITRMDKSALREYR-LRTGMI 85
Cdd:PRK15134 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 FQH----FNLLHARSVADNVAVPLEIAKVPKAARqARVAELLELVGL---ADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:PRK15134 98 FQEpmvsLNPLHTLEKQLYEVLSLHRGMRREAAR-GEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSL 238
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKL 256
|
.
gi 1610668340 239 L 239
Cdd:PRK15134 257 L 257
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-221 |
5.02e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 126.28 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL---ERPTAGRIIVNGNDITRMDKSA--L 75
Cdd:PRK09984 4 IIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLArdI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 76 REYRLRTGMIFQHFNLLHARSVADNVAVPlEIAKVP---------KAARQARVAELLELVGLADKAAAFPSQLSGGQKQR 146
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 147 VGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-239 |
5.34e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 126.44 E-value: 5.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY---AGTGR----PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKS 73
Cdd:PRK15112 4 LLEVRNLSKTFryrTGWFRrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 74 aLREYRLRtgMIFQH-FNLLHARS-VADNVAVPLEI-AKVPKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGI 149
Cdd:PRK15112 84 -YRSQRIR--MIFQDpSTSLNPRQrISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 150 ARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVA 229
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|
gi 1610668340 230 PWSRLRQSLL 239
Cdd:PRK15112 241 PLHELTKRLI 250
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-205 |
6.71e-35 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 124.13 E-value: 6.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksALREYRL 80
Cdd:COG4133 2 MLEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLEIAKVPkaARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlNLTIVLITH---ELEVVKTL 205
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHqplELAAARVL 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-221 |
8.84e-35 |
|
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: 123.93 E-value: 8.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA---LREY 78
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RlrtgmifqhfNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03269 79 R----------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 159 VLLCDEATSALDP---ETTASVLNLLADINQklnlTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03269 149 LLILDEPFSGLDPvnvELLKDVIRELARAGK----TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-227 |
1.24e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 124.88 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRl 80
Cdd:PRK13548 2 MLEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 rtGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALA------ 154
Cdd:PRK13548 79 --AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 155 ARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-239 |
2.85e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 129.44 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKST----LIRCLNllerpTAGRIIVNGNDITRMDKSALREYRLRTGMIFQHFN-LL 92
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 HAR-SVADNVAVPLEI--AKVPKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSA 168
Cdd:PRK15134 376 NPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 169 LDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSLL 239
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-239 |
3.16e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 125.62 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 7 LSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKS-TLIRCLNLLERP---TAGRIIVNGNDITRMDKsalREYRL 80
Cdd:PRK11022 9 LSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE---KERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTG----MIFQH--FNLLHARSVADNVavpLEIAKV----PKAARQARVAELLELVGLADKAA---AFPSQLSGGQKQRV 147
Cdd:PRK11022 86 LVGaevaMIFQDpmTSLNPCYTVGFQI---MEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250
....*....|..
gi 1610668340 228 VAPWSRLRQSLL 239
Cdd:PRK11022 243 RAPRHPYTQALL 254
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-223 |
5.09e-34 |
|
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: 122.51 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALreyrlr 81
Cdd:TIGR03740 1 LETKNLSKRFGK--QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKI------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tGMIFQHFNLLHARSVADNVAVPLEIAKVPKAarqaRVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRI 223
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-227 |
5.60e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.93 E-value: 5.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 11 YAGTgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIrclNLLER---PTAGRIIVNGNDITRMDKSALREYrlrTGMIFQ 87
Cdd:PRK13657 344 YDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRvfdPQSGRILIDGTDIRTVTRASLRRN---IAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 HfNLLHARSVADNVAVPLEIA---KVPKAARQARVAELLE--LVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLC 162
Cdd:PRK13657 417 D-AGLFNRSIEDNIRVGRPDAtdeEMRAAAERAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 163 DEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELV 557
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-230 |
6.60e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 123.56 E-value: 6.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAgTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmDKSALREYRL 80
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNL-LHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK13644 78 LVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-254 |
7.67e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 123.74 E-value: 7.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA-LREYRLRTGMIFQhfnLLHARS 96
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKRIGMVFQ---FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 97 VADNVAVPLEIA----KVPKAARQARVAELLELVGLA-DKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDP 171
Cdd:PRK13646 99 FEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 172 ETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLvAPWSRLRQSLLHDP---QAERDF 248
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF-KDKKKLADWHIGLPeivQLQYDF 257
|
....*.
gi 1610668340 249 LARHGL 254
Cdd:PRK13646 258 EQKYQT 263
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-227 |
9.74e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.53 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYR- 79
Cdd:COG4559 1 MLEAENLSVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 -LRtgmifQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALA---- 154
Cdd:COG4559 79 vLP-----QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 155 ---ARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 |
1.45e-33 |
|
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: 121.06 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHfNLLHARSVADNVAvPLEIAKvpkaarQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSNLD-PFGEYS------DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLladINQKL-NLTIVLITHELEVVKTlCDHAALLEHGEIIESG 221
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-200 |
1.99e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.12 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKT-YAGTG--RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksalRE 77
Cdd:COG1101 1 MLELKNLSKTfNPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-----PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRlRTGMI---FQH------FNLlharSVADNVAV--------PLEIAKvpKAARQARVAELLELV--GLADKAAAFPSQ 138
Cdd:COG1101 76 YK-RAKYIgrvFQDpmmgtaPSM----TIEENLALayrrgkrrGLRRGL--TKKRRELFRELLATLglGLENRLDTKVGL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 139 LSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELE 200
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
2.72e-33 |
|
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: 126.63 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:TIGR02857 322 LEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---Q 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHfNLLHARSVADNVAvpleIAKvpKAARQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:TIGR02857 398 IAWVPQH-PFLFAGTIAENIR----LAR--PDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVkTLCDH 208
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADR 525
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-227 |
2.88e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 127.06 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIrclNLLER---PTAGRIIVNGNDitrmdksaLREY 78
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA---NLLTRfydIDEGEILLDGHD--------LRDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRT-----GMIFQHFNLLHaRSVADNVAVPLE----IAKVPKAARQARVAELLELV--GLADKAAAFPSQLSGGQKQRV 147
Cdd:PRK11176 411 TLASlrnqvALVSQNVHLFN-DTIANNIAYARTeqysREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADInQKlNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL-QK-NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
3.12e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY--------------AGTGRP------ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRI 60
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkellLRRRRTrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 61 IVNGnditRMdkSALreyrLRTGMIFqHFNLlharSVADNVAVPLEIAKVPKAARQARVAELLELVGLADkaaaFPSQ-- 138
Cdd:COG1134 84 EVNG----RV--SAL----LELGAGF-HPEL----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGD----FIDQpv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 139 --LSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGE 216
Cdd:COG1134 145 ktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*....
gi 1610668340 217 IIESGRIAD 225
Cdd:COG1134 224 LVMDGDPEE 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-230 |
4.81e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 121.36 E-value: 4.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 4 IVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAG-----RIIVNGNDItrMDKSALREY 78
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLhARSVADNVAVPLEIAK-VPK----AARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARAL 153
Cdd:PRK14271 100 RRRVGMLFQRPNPF-PMSIMDNVLAGVRAHKlVPRkefrGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 154 AARPDVLLCDEATSALDPETTASVLNLLADINQKlnLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 |
4.89e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.50 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTY---------AGTGR----------PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRII 61
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 62 VNGNDITRMDKsalrEYRLRTGMIF-QhfnllhaRS-------VADNVAVPLEIAKVPKAARQARVAELLELVGLADKAA 133
Cdd:COG4586 81 VLGYVPFKRRK----EFARRIGVVFgQ-------RSqlwwdlpAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 134 AFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLE 213
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
250
....*....|....
gi 1610668340 214 HGEIIESGRIADLL 227
Cdd:COG4586 230 HGRIIYDGSLEELK 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-227 |
5.75e-33 |
|
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: 125.69 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGR---PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVN-GNDITRMDKSALR 76
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 77 EyRLRT----GMIFQHFNLLHARSVADNV--AVPLEIakvPKAARQARVAELLELVGLADKAAA-----FPSQLSGGQKQ 145
Cdd:TIGR03269 359 G-RGRAkryiGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKAEeildkYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 146 RVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
..
gi 1610668340 226 LL 227
Cdd:TIGR03269 515 IV 516
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-240 |
7.62e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 122.32 E-value: 7.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIvglsKTYAGTGRpALNDVSLHVPGGAVYGILGRSGAGKSTLIRC-LNLLE---RPTAGRIIVNGNDITRMDKSALRE 77
Cdd:COG4170 11 IEI----DTPQGRVK-AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKdnwHVTADRFRWNGIDLLKLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRLR-TGMIFQHFN--LLHARSVADNV--AVPLEIAKVP----KAARQARVAELLELVGLADKAA---AFPSQLSGGQKQ 145
Cdd:COG4170 86 IIGReIAMIFQEPSscLDPSAKIGDQLieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 146 RVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIAD 225
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
250
....*....|....*
gi 1610668340 226 LLVAPWSRLRQSLLH 240
Cdd:COG4170 246 ILKSPHHPYTKALLR 260
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-227 |
8.01e-33 |
|
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: 125.70 E-value: 8.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRclnLLER---PTAGRIIVNGNDITRMDKSALREYrlrTGMIFQ----- 87
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDIRDVTQASLRAA---IGIVPQdtvlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 ----HFNLLHARSVADNvavpleiAKVPKAARQARVAELLE--------LVG---LadkaaafpsQLSGGQKQRVGIARA 152
Cdd:COG5265 445 ndtiAYNIAYGRPDASE-------EEVEAAARAAQIHDFIEslpdgydtRVGergL---------KLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTI-VDADEILVLEAGRIVERGTHAELL 580
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-243 |
1.01e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 122.83 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNG---NDITRMDKSalreyrlrT 82
Cdd:PRK11000 8 NVTKAYGDV--VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVPPAERG--------V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 GMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARV---AELLELVGLADKAaafPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQSLL 239
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
....
gi 1610668340 240 HDPQ 243
Cdd:PRK11000 235 GSPK 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-254 |
1.43e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.61 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSA-LREYRLRTGMIFQH-FNLLHAR 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEIAKVPKAARQARVAELLELVGLADKA-AAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETT 174
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 175 ASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLvapwsrlrqsllhdpqAERDFLARHGL 254
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF----------------QEVDFLKAHEL 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-221 |
2.03e-32 |
|
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: 118.08 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR---N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHArSVADNVAVPLEIAKvpkaarQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVL-NLLADINQKlnlTIVLITHELEVVkTLCDHAALLEHGEIIESG 221
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKeRLRQLLGDK---TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
3.20e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 120.71 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSAlreyRLR 81
Cdd:PRK13536 42 IDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA----RAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-221 |
3.30e-32 |
|
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: 117.47 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksALREY 78
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-227 |
1.52e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.22 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 23 SLHVPGGAVYGILGRSGAGKSTLircLNLLE---RPTAGRIIVNGNDITRMDKSalreyRLRTGMIFQHFNLLHARSVAD 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL---LNLIAgflTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 100 NVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLN 179
Cdd:PRK10771 91 NIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610668340 180 LLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-226 |
1.54e-31 |
|
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: 116.09 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 3 EIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSAlreyRLRT 82
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 GMIF-----QHFNLLharSVADNVAVPLEIAKvpkAARQARVAELLELvgladkaaaFP----------SQLSGGQKQRV 147
Cdd:TIGR03410 76 GIAYvpqgrEIFPRL---TVEENLLTGLAALP---RRSRKIPDEIYEL---------FPvlkemlgrrgGDLSGGQQQQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:TIGR03410 141 AIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-227 |
1.85e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.50 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlRTGMIFQH-FNLLHARSV 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR---KIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASV 177
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1610668340 178 LNLLADINQKLNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-227 |
1.86e-31 |
|
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: 116.34 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAG-RIIVNGNDITRMDksaLREYRLRTGMIFQHfnlLH 93
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---VWELRKRIGLVSPA---LQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 AR-----SVADNV-----AVpLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCD 163
Cdd:COG1119 89 LRfprdeTVLDVVlsgffDS-IGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 164 EATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
1.88e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.88 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYaGTGRP----ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALRE 77
Cdd:PRK13651 3 IKVKNIVKIF-NKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 Y---------------------RLRTGMIFQ--HFNLLHARSVADNVAVPLEIAkVPKAARQARVAELLELVGLA----D 130
Cdd:PRK13651 82 KvleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG-VSKEEAKKRAAKYIELVGLDesylQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 131 KAaafPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAA 210
Cdd:PRK13651 161 RS---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*..
gi 1610668340 211 LLEHGEIIESGRIADLL 227
Cdd:PRK13651 237 FFKDGKIIKDGDTYDIL 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-219 |
3.43e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 115.26 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLR-TGMIFQHFNLLHARSV 97
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASV 177
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610668340 178 LNLLADINQKLNLTIVLITHELEVVKTlCDHAALLEHGEIIE 219
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-221 |
4.79e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.12 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRTGMIFQ--HFNLLHAR 95
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEIAKV-PKAARQARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPET 173
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610668340 174 TASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-227 |
5.71e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 120.31 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLLER---PTAGRIIVNGNDITRMDKSALREy 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL---LQLLTRawdPQQGEILLNGQPIADYSEAALRQ- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlRTGMIFQHFNLLHArSVADNvavpLEIAKvpKAARQARVAELLELVGLADKAAAFPS----------QLSGGQKQRVG 148
Cdd:PRK11160 415 --AISVVSQRVHLFSA-TLRDN----LLLAA--PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 149 IARALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTLcDHAALLEHGEIIESGRIADLL 227
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-227 |
6.04e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 115.65 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLER--PTA---GRIIVNGNDITRMDKSALrEYRLRTGMIFQHFNLL 92
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPDVDPV-EVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 hARSVADNVAVPLEIAK--------VPKAARQA----RVAELLELVGLAdkaaafpsqLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK14243 104 -PKSIYDNIAYGARINGykgdmdelVERSLRQAalwdEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlnLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLV 238
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-227 |
1.07e-30 |
|
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: 120.23 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYaGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrlr 81
Cdd:TIGR01193 474 IVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR----- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tgmifQHFNLL------HARSVADNVAV----PLEIAKVPKAARQARVAELLELV--GLADKAAAFPSQLSGGQKQRVGI 149
Cdd:TIGR01193 548 -----QFINYLpqepyiFSGSILENLLLgakeNVSQDEIWAACEIAEIKDDIENMplGYQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 150 ARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlnlTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-244 |
1.17e-30 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 114.41 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSktyAGTGRPALNDVSLHVPGGAVYGILGRSGAGKStlIRCLNLLE------RPTAGRIIVNGndiTRMDKSAL 75
Cdd:PRK10418 5 IELRNIA---LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDG---KPVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 76 REYRLRTgmIFQH----FNLLHarSVADNVAVPLeiAKVPKAARQARVAELLELVGLADKAA---AFPSQLSGGQKQRVG 148
Cdd:PRK10418 77 RGRKIAT--IMQNprsaFNPLH--TMHTHARETC--LALGKPADDATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 149 IARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLV 228
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250
....*....|....*.
gi 1610668340 229 APWSRLRQSLLHDPQA 244
Cdd:PRK10418 231 APKHAVTRSLVSAHLA 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-230 |
1.52e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.10 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL-----ERPTAGRIIVNGNDI--TRMDKSALREyrlRTGMIFQHFN 90
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysPRTDTVDLRK---EIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 91 LLhARSVADNVAVPLEIAKVPKAARQARVAELlELVG----------LADKAAAfpsqLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK14239 97 PF-PMSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGasiwdevkdrLHDSALG----LSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlnLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-217 |
2.50e-30 |
|
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: 112.95 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPA---LNDVSLHVPGGAVYGILGRSGAGKSTlirCLNLLER---PTAGRIIVNGNDITRMDKSALREyrlRTG 83
Cdd:cd03248 18 TFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHKYLHS---KVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 84 MIFQHfNLLHARSVADNVAVPL---EIAKVPKAARQARVAELLELV--GLADKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:cd03248 92 LVGQE-PVLFARSLQDNIAYGLqscSFECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEI 217
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-221 |
2.71e-30 |
|
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: 113.20 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYA---------GTGR----------PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIV 62
Cdd:cd03267 1 IEVSNLSKSYRvyskepgliGSLKslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 63 NGNDITRMDKsalrEYRLRTGMIF-QHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSG 141
Cdd:cd03267 81 AGLVPWKRRK----KFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 142 GQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
7.68e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDItrmdKSALREYRLR 81
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-246 |
9.53e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 114.20 E-value: 9.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNG---NDITRmdKSALREYRLRTGMIFQHFNLLHARSV 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEK--GICLPPEKRRIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAVPLeiakvpKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASV 177
Cdd:PRK11144 94 RGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 178 LNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL----LVAPWSRLRQ--SLLHDPQAER 246
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVwassAMRPWLPKEEqsSILKVTVLEH 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
4.19e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAgTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYRLR 81
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQH-FNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK13647 81 VGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-230 |
4.47e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 112.13 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKS-TLIRCLNLLERP--TAGRIIVNGNDITRMDKSALReyRLRT---GMIFQ---- 87
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELN--KLRAeqiSMIFQdpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 ------------------HFNLLHARSVADNVAVpLEIAKVPKAARQARVaellelvgladkaaaFPSQLSGGQKQRVGI 149
Cdd:PRK09473 109 slnpymrvgeqlmevlmlHKGMSKAEAFEESVRM-LDAVKMPEARKRMKM---------------YPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 150 ARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVA 229
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
.
gi 1610668340 230 P 230
Cdd:PRK09473 253 P 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
5.71e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.87 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRI----IVNGNDITRMDKSA---------LREYRLRTGM 84
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITnpyskkiknFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 IFQ--HFNLLHARSVADNVAVPLEIaKVPKAARQARVAELLELVGLADK-AAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 162 CDEATSALDPETTASVLNLLADiNQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-227 |
9.30e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.40 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrl 80
Cdd:COG4604 1 MIEIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHAR-SVADNVAV---PLEIAKvPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAAR 156
Cdd:COG4604 75 KRLAILRQENHINSRlTVRELVAFgrfPYSKGR-LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-170 |
9.62e-29 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 111.86 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksalrEYRL 80
Cdd:PRK11650 3 GLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------EPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 R-TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAE---LLELVGLADKAaafPSQLSGGQKQRVGIARALAAR 156
Cdd:PRK11650 76 RdIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 1610668340 157 PDVLLCDEATSALD 170
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-226 |
1.82e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 113.66 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrlRTGMIFQHFNLLHAR 95
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH----RQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPL---EIAKVPKAARQARVAELLELV--GLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:TIGR00958 570 SVRENIAYGLtdtPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 171 pettASVLNLLADINQKLNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADL 226
Cdd:TIGR00958 650 ----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-219 |
3.72e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 3.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDIT-RMDKSALREYRLRTGMIFQhF--NLLHAR 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQ-FpeAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAV-PLEIAKVPKAARQARVaELLELVGLADKAAA-FPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPET 173
Cdd:PRK13641 102 TVLKDVEFgPKNFGFSEDEAKEKAL-KWLKKVGLSEDLISkSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1610668340 174 TASVLNLLADInQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIE 219
Cdd:PRK13641 181 RKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-226 |
6.79e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.41 E-value: 6.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMD-KSAlreYR 79
Cdd:PRK09700 5 YISMAGIGKSFGPV--HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLA---AQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 LRTGMIFQHFNLLHARSVADNVAVPLEIAK-------VPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARA 152
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 153 LAARPDVLLCDEATSALdpeTTASVLNLLADINQ--KLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-221 |
1.13e-27 |
|
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: 106.08 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDitrmdkSALREyrLRTGMifqHFNLlhar 95
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLG--LGGGF---NPEL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTA 175
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1610668340 176 SVLNLLADINQKLNlTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:cd03220 180 KCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-221 |
1.59e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 110.61 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYrlr 81
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLhARSVADNVAVPLEI--AKVPKAARQARVAELLelVGLAD----KAAAFPSQLSGGQKQRVGIARALAA 155
Cdd:COG4618 408 IGYLPQDVELF-DGTIAENIARFGDAdpEKVVAAAKLAGVHEMI--LRLPDgydtRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 156 RPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKtLCDHAALLEHGEIIESG 221
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFG 548
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-239 |
1.94e-27 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 107.58 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTGRP--ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL------NLleRPTAGRIIVNGNDITRMdk 72
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNW--RVTADRMRFDDIDLLRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 73 sALREYRLRTG----MIFQHfnllhARSVAD---NVAVPLeIAKVPKAA-----------RQARVAELLELVGLADKAAA 134
Cdd:PRK15093 79 -SPRERRKLVGhnvsMIFQE-----PQSCLDpseRVGRQL-MQNIPGWTykgrwwqrfgwRKRRAIELLHRVGIKDHKDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 135 ---FPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAAL 211
Cdd:PRK15093 152 mrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
250 260
....*....|....*....|....*...
gi 1610668340 212 LEHGEIIESGRIADLLVAPWSRLRQSLL 239
Cdd:PRK15093 232 LYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-239 |
3.13e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.89 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLL-----ERPTAGRIIVNGNDITRMdKSALREYRLRTGMIFQHFNLLh 93
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYER-RVNLNRLRRQVSMVHPKPNLF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAV---------PLEIAKVPKAARQArvAELLELVGLADKAAAFpsQLSGGQKQRVGIARALAARPDVLLCDE 164
Cdd:PRK14258 101 PMSVYDNVAYgvkivgwrpKLEIDDIVESALKD--ADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 165 ATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEH-----GEIIESGRIADLLVAPW-SRLRQSL 238
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHdSRTREYV 256
|
.
gi 1610668340 239 L 239
Cdd:PRK14258 257 L 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-217 |
4.05e-27 |
|
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: 103.28 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALR--------EYRLRTGmi 85
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragiayvpEDRKREG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 fqhfnLLHARSVADNVAvpleiakvpkaarqarvaellelvgladkaaaFPSQLSGGQKQRVGIARALAARPDVLLCDEA 165
Cdd:cd03215 89 -----LVLDLSVAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 166 TSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-221 |
5.92e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.01 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRT--- 82
Cdd:PRK11701 11 GLTKLYGP--RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 83 ---GMIFQHF--NLLHARSVADNVAVPLEIAKVPKAAR-QARVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIARALAA 155
Cdd:PRK11701 89 tewGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 156 RPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-221 |
1.62e-26 |
|
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: 102.73 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 5 VGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTL---IRCLNLLERPTAGRIIVNGNDITRmdksalREYRLR 81
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRKP------DQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIA---KVPKAARQARVA-ELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILRlprKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHE--LEVVKTLcDHAALLEHGEIIESG 221
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQprSDLFRLF-DRILLLSSGEIVYSG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-218 |
3.49e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNditrmdksalreyrLRTGMI 85
Cdd:COG0488 3 NLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 FQHFNLLHARSVADNV--------AVPLEIAKVPKA------------------------ARQARVAELLELVGLADKAA 133
Cdd:COG0488 67 PQEPPLDDDLTVLDTVldgdaelrALEAELEELEAKlaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 134 AFP-SQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTAsvlnLLADINQKLNLTIVLITHELEVVKTLCDHAALL 212
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE----WLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
....*.
gi 1610668340 213 EHGEII 218
Cdd:COG0488 223 DRGKLT 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-222 |
3.52e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrl 80
Cdd:PRK11300 5 LLSVSGLMMRFGGL--LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMI--FQHFNLLHARSVADNVAVPLE----------IAKVP---KAARQA--RVAELLELVGLADKAAAFPSQLSGGQ 143
Cdd:PRK11300 79 RMGVVrtFQHVRLFREMTVIENLLVAQHqqlktglfsgLLKTPafrRAESEAldRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 144 KQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGR 222
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-230 |
2.10e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.02 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSAlreYRLRTGMIFQHFNLLHA 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 95 RSVADNVAvpleIAKVP--------KAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:PRK10575 100 MTVRELVA----IGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 167 SALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
2.38e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrl 80
Cdd:PRK09536 3 MIDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVavplEIAKVPKAAR--------QARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARA 152
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVV----EMGRTPHRSRfdtwtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-260 |
2.62e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYRL 80
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS---MLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVA------VPL-------EIAKVPKAARQARVAELlelvglADKAAafpSQLSGGQKQRV 147
Cdd:PRK11231 77 RLALLPQHHLTPEGITVRELVAygrspwLSLwgrlsaeDNARVNQAMEQTRINHL------ADRRL---TDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGriadll 227
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG------ 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 1610668340 228 vAPWSRLRQSLLH---DPQAErdfLARHGLHGRPLC 260
Cdd:PRK11231 221 -TPEEVMTPGLLRtvfDVEAE---IHPEPVSGTPMC 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-205 |
5.30e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 98.88 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL--NLLERPTAGRIIVNGNDITRmdksalreyrlrtgmifqhfnllh 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGR------------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAvpleIAKVPKAArqarvAELLELVGLADkAAAF---PSQLSGGQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:COG2401 99 EASLIDAIG----RKGDFKDA-----VELLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1610668340 171 PETTASVLNLLADINQKLNLTIVLITHELEVVKTL 205
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-222 |
1.17e-24 |
|
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: 97.48 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS---S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLhARSVADNVAVPLEIAKVpkaarqarvaELLElvglADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03369 84 LTIIPQDPTLF-SGTIRSNLDPFDEYSDE----------EIYG----ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGR 222
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-221 |
1.28e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLR--TGMIFQ--HFNLLH 93
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRkeIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAVPLEIAKVPKAARQaRVAELLELVGLA-DKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPE 172
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYK-KVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1610668340 173 TTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-229 |
2.84e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 101.33 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYaGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:PRK10790 341 IDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ---G 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLhARSVADNVAVPLEIAkvpkaarQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:PRK10790 417 VAMVQQDPVVL-ADTFLANVTLGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQKlnLTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLLVA 229
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTI-VEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-210 |
3.48e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 11 YAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALRE---YRLRTGMIFq 87
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQqvsYCAQTPTLF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 hfnllhARSVADNVAVPLEIAKvpKAARQARVAELLELVGLADKAAAFP-SQLSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:PRK10247 94 ------GDTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1610668340 167 SALDPETTASVLNLLADINQKLNLTIVLITHELEVVK------TLCDHAA 210
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINhadkviTLQPHAG 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-227 |
5.14e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 7 LSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksALREYRLR-TGMI 85
Cdd:PRK10895 9 LAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHARARRgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 FQHFNLLHARSVADNVAVPLEIAK-VPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDE 164
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 165 ATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-221 |
6.50e-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: 95.31 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 13 GTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLN--LLERPTAGRIIVNGNDITRmdksalREYRLRTGMIFQHfN 90
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK------RSFRKIIGYVPQD-D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 91 LLHArsvadnvavpleiakvpkaarQARVAELLELvgladkaAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:cd03213 92 ILHP---------------------TLTVRETLMF-------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 171 PETTASVLNLLADINQkLNLTIVLITHEL--EVVKtLCDHAALLEHGEIIESG 221
Cdd:cd03213 144 SSSALQVMSLLRRLAD-TGRTIICSIHQPssEIFE-LFDKLLLLSQGRVIYFG 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
6.61e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 100.13 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREyrlR 81
Cdd:TIGR02868 335 LELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR---R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHArSVADNvavpLEIAKvpKAARQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIA 150
Cdd:TIGR02868 411 VSVCAQDAHLFDT-TVREN----LRLAR--PDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHEL 199
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
1.42e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKS-TLIRCLNLLERPTA----GRIIV---NGNDITRMDKSALREYRLR---TGMI 85
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGlvqcDKMLLrrrSRQVIELSEQSAAQMRHVRgadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 FQH--FNLLHARSVADNVAVPLEI---AKVPKAARQARvaELLELVGLADKAAA---FPSQLSGGQKQRVGIARALAARP 157
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLhqgASREEAMVEAK--RMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSRLRQS 237
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRA 267
|
..
gi 1610668340 238 LL 239
Cdd:PRK10261 268 LL 269
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-221 |
2.04e-23 |
|
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: 99.32 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 7 LSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDItrmdKSALREYRLRTGMIF 86
Cdd:TIGR01257 934 LVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 87 QHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 167 SALDPETTASVLNLLadINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESG 221
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
6.77e-23 |
|
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: 90.97 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNditrmdksalreyrlr 81
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tgmifqhfnllharsvadnvavpLEIAKVPkaarqarvaellelvgladkaaafpsQLSGGQKQRVGIARALAARPDVLL 161
Cdd:cd03221 63 -----------------------VKIGYFE--------------------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQklnlTIVLITHELEVVKTLCDHAALLEHGE 216
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-221 |
1.04e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.79 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAgTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLR 81
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEhGEIIESG 221
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-221 |
2.49e-22 |
|
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: 90.45 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLLER---PTAGRIIVNGNDITRMDKsALREY 78
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL---LQLLTGdlkPQQGEITLDGVPVSDLEK-ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 rlrTGMIFQHFNLLHArsvadnvavpleiakvpkaarqarvaELLELVGLadkaaafpsQLSGGQKQRVGIARALAARPD 158
Cdd:cd03247 77 ---ISVLNQRPYLFDT--------------------------TLRNNLGR---------RFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTLcDHAALLEHGEIIESG 221
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-260 |
3.56e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.38 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrMDKSALREYRLRTGMIFQHFNL-LHAR 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQqIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEIAKVPKAARQARVAELLELVgladKAAAFPSQ----LSGGQKQRVGIARALAARPDVLLCDEATSALDP 171
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLV----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 172 ETTASVLNLLADINQKLNlTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLvAPWSRLRQSLLHDPQaerdFLAR 251
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF-ACTEAMEQAGLTQPW----LVKL 243
|
....*....
gi 1610668340 252 HGLHGRPLC 260
Cdd:PRK13638 244 HTQLGLPLC 252
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-197 |
4.49e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHV-PGGAVYgILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDitrmdksalreyrlrtGMIF--QHFNL 91
Cdd:COG4178 375 GRPLLEDLSLSLkPGERLL-ITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------------RVLFlpQRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 LHArSVADNVAVPLEIAKVPkaarQARVAELLELVGLA------DKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEA 165
Cdd:COG4178 438 PLG-TLREALLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|..
gi 1610668340 166 TSALDPETTASVLNLLADinQKLNLTIVLITH 197
Cdd:COG4178 513 TSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
4.75e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNditrmdksalreyrL 80
Cdd:COG0488 315 VLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------------V 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHA-RSVADnvavplEIAKVPKAARQARVAELLELVGLA-DKAAAFPSQLSGGQKQRVGIARALAARPD 158
Cdd:COG0488 379 KIGYFDQHQEELDPdKTVLD------ELRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADINQklnlTIVLITHELEVVKTLCDHAALLEHGEIIE 219
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-246 |
1.23e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLLE--RPTAGRIIVNGNDITRMDksaLREYRLRTGMIFQHFNLL 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSL---LNALLgfLPYQGSLKINGIELRELD---PESWRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 HArSVADNVA---VPLEIAKVPKAARQARVAELLELV--GLA----DKAAAfpsqLSGGQKQRVGIARALAARPDVLLCD 163
Cdd:PRK11174 436 HG-TLRDNVLlgnPDASDEQLQQALENAWVSEFLPLLpqGLDtpigDQAAG----LSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 164 EATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLVAPwsRLRQSLLHDPQ 243
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG--GLFATLLAHRQ 585
|
...
gi 1610668340 244 AER 246
Cdd:PRK11174 586 EEI 588
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-233 |
3.78e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.47 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLLERP---TAGRIIVNGNDITRMdksALREYRLRTGMIF 86
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL---LSLIQRHfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 87 QHfNLLHARSVADNVAVPLEIA---KVPKAARQARVAE-LLEL-VGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:PRK10789 396 QT-PFLFSDTVANNIALGRPDAtqqEIEHVARLASVHDdILRLpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKlnLTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLLVAP-WSR 233
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQSgWYR 544
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-244 |
2.28e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksALREYRLRTGMIFQHFNLLHARSVADN 100
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY---ASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 101 VA------VPLeIAKVPKAARQArVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETT 174
Cdd:PRK10253 102 VArgryphQPL-FTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 175 ASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAPWSR----LRQSLLHDPQA 244
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIEriygLRCMIIDDPVA 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-226 |
3.87e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLeRPTA---GRIIVNGNDITrmdKSALRE 77
Cdd:PRK13549 5 LLEMKNITKTFGGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQ---ASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRlRTGM--IFQHFNLLHARSVADNVAVPLEIAK---VPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARA 152
Cdd:PRK13549 79 TE-RAGIaiIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 153 LAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-222 |
8.07e-20 |
|
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: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERP---TAGRIIVNGndiTRMDKsalREYRLRTGMIFQHFNLLHAR 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG---MPIDA---KEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVAVPLEI---AKVPKAARQARVAELLELVGL---ADKAAAFPSQ---LSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:TIGR00955 115 TVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 167 SALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGR 222
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGS 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-218 |
1.23e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 87.57 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLeRPTA---GRIIVNGNDITrmdKSALRE 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGV--KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLK---ASNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YRlRTGM--IFQHFNLLHARSVADNVAVPLEI----AKVPKAARQARVAELLELVGLADKAAAFP-SQLSGGQKQRVGIA 150
Cdd:TIGR02633 75 TE-RAGIviIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEII 218
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-221 |
1.46e-19 |
|
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: 83.73 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL--NLLERPTAGRIIVNGNDITRMDKsalrEYRLRTG--MIFQHfn 90
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPP----EERARLGifLAFQY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 91 llharsvadnvavPLEIAKVpkaarqaRVAELLELVGLAdkaaafpsqLSGGQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:cd03217 86 -------------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 171 PETTASVLNLLADINQKlNLTIVLITHE---LEVVKTlcDHAALLEHGEIIESG 221
Cdd:cd03217 137 IDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIKP--DRVHVLYDGRIVKSG 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-226 |
2.20e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREY--------RLRTGMI- 85
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLVp 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 -FqhfnllharSVADNVAvpLEIAKVPKAAR---------QARVAELLE-----LVGLADKAAAfpsqLSGGQKQRVGIA 150
Cdd:COG3845 350 dM---------SVAENLI--LGRYRRPPFSRggfldrkaiRAFAEELIEefdvrTPGPDTPARS----LSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 151 RALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-216 |
2.23e-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: 83.29 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnLLE-RPTAGRIIVNGnditrmdksalreyrlRTGMIFQHFNLLHAr 95
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPG----------------SIAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNV--AVPLEiakvpkaarQARVAELLELVGLADKAAAFPSQ-----------LSGGQKQRVGIARALAARPDVLLC 162
Cdd:cd03250 81 TIRENIlfGKPFD---------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 163 DEATSALDPETTASVLNLLadINQKLNL--TIVLITHELEVVKtLCDHAALLEHGE 216
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENC--ILGLLLNnkTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-220 |
3.07e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGnditrmdksalREYRLRTGM- 84
Cdd:PRK11288 9 GIGKTFPGV--KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-----------QEMRFASTTa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 --------IFQHFNLLHARSVADNV---AVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARAL 153
Cdd:PRK11288 76 alaagvaiIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 154 AARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIES 220
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
9.13e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 9.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdkSALREYRL 80
Cdd:PRK15439 11 LLCARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL--TPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNVAVPLeiakvPK-AARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 160 LLCDEATSALDPETTAsvlNLLADIN--QKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:PRK15439 162 LILDEPTASLTPAETE---RLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-218 |
1.81e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMD-KSALR-------EYRLRTGmi 85
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRagiayvpEDRKGEG-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 fqhfnLLHARSVADNVAVPL--EIAK---VPKAARQARVAELLELVGLadKAAAfPSQ----LSGGQKQRVGIARALAAR 156
Cdd:COG1129 341 -----LVLDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRI--KTPS-PEQpvgnLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEII 218
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-250 |
2.26e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.45 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksALREYRLRTGMIFQHfNLLHARSVA 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRRQFSMIPQD-PVLFDGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 99 DNVAVPLEiakvpkaARQARVAELLELVGLADKAAAFP-----------SQLSGGQKQRVGIARALAAR-PDVLLCDEAT 166
Cdd:PTZ00243 1402 QNVDPFLE-------ASSAEVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKKgSGFILMDEAT 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 167 S----ALDPETTASVLNLLAdinqklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLVApwsrlRQSLLHD- 241
Cdd:PTZ00243 1475 AnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMN-----RQSIFHSm 1542
|
250
....*....|....
gi 1610668340 242 -----PQAERDFLA 250
Cdd:PTZ00243 1543 vealgRSEAKRFLQ 1556
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-226 |
2.71e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRL 80
Cdd:PRK10762 4 LLQLKGIDKAFPGV--KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 rtGMIFQHFNLLHARSVADNVAVPLEIAKV------PKAARQArvAELLELVGLADKAAAFPSQLSGGQKQRVGIARALA 154
Cdd:PRK10762 82 --GIIHQELNLIPQLTIAENIFLGREFVNRfgridwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 155 ARPDVLLCDEATSAL-DPETTA--SVLNLLADinqkLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESlfRVIRELKS----QGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-229 |
3.27e-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: 84.23 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksALREYRLRTGMIFQHfNLLHARSVA 98
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRFKITIIPQD-PVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 99 DNVAvPLeiakvpKAARQARVAELLELVGLADKAAAFPSQL-----------SGGQKQRVGIARALAARPDVLLCDEATS 167
Cdd:TIGR00957 1378 MNLD-PF------SQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 168 ALDPETTasvlNLL-ADINQKL-NLTIVLITHELevvKTLCDHA--ALLEHGEIIESGRIADLLVA 229
Cdd:TIGR00957 1451 AVDLETD----NLIqSTIRTQFeDCTVLTIAHRL---NTIMDYTrvIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-226 |
8.17e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRI-----IVNGNDItrmdksalrEYRLRTGMIFQHFNL- 91
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDI---------ATRRRVGYMSQAFSLy 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 ----------LHARsvadnvavpleIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLL 161
Cdd:NF033858 352 geltvrqnleLHAR-----------LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 162 CDEATSALDPETTASVLNLLADINQKLNLTIVLITH---ELEvvktLCDHAALLEHGEIIESGRIADL 226
Cdd:NF033858 421 LDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHfmnEAE----RCDRISLMHAGRVLASDTPAAL 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-226 |
1.31e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.70 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDIT-RMDKSALREyrlRTGM 84
Cdd:PRK10982 3 NISKSFPGV--KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALEN---GISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 IFQHFNLLHARSVADNvavpLEIAKVPKAA-----------RQARVAELLELVGLADKAAafpsQLSGGQKQRVGIARAL 153
Cdd:PRK10982 78 VHQELNLVLQRSVMDN----MWLGRYPTKGmfvdqdkmyrdTKAIFDELDIDIDPRAKVA----TLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 154 AARPDVLLCDEATSALdpetTASVLNLLADINQKLN---LTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:PRK10982 150 SYNAKIVIMDEPTSSL----TEKEVNHLFTIIRKLKergCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-218 |
1.41e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSalREYRLRTGMIFQHFNLLHARSV 97
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAVPLEIAKvpKAARQARVAELLELVG-LADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTAS 176
Cdd:PRK11614 98 EENLAMGGFFAE--RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610668340 177 VLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEII 218
Cdd:PRK11614 176 IFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-197 |
2.03e-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: 77.78 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmdksaLREYRLRTGMIFQHF 89
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 90 NLLHAR-SVADNVAVPLEIAkvpkAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSA 168
Cdd:TIGR01189 82 PGLKPElSALENLHFWAAIH----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 1610668340 169 LDPETTASVLNLLADINQKLNLTIvLITH 197
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVL-LTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-182 |
2.97e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYrlrtgmiFQHFNLLH- 93
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-------LGHRNAMKp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAVPLEIakvpKAARQARVAELLELVGLADkAAAFPSQ-LSGGQKQRVGIARALAARPDVLLCDEATSALDPE 172
Cdd:PRK13539 87 ALTVAENLEFWAAF----LGGEELDIAAALEAVGLAP-LAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170
....*....|
gi 1610668340 173 TTASVLNLLA 182
Cdd:PRK13539 162 AVALFAELIR 171
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-214 |
6.71e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTG-RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIvngnditrmdksalREYR 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGqRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 LRTGMIFQHFNLlharsvadNVAVPLEIAK---VPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAAR 156
Cdd:PRK09544 67 LRIGYVPQKLYL--------DTTLPLTVNRflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEH 214
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-203 |
1.70e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.92 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNgnDITRMDKSALREYRLRTGMIFQHfNLLHARSVADN 100
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 101 VAVPL---------------------------------------------------EIAKVPKAARQARVAELLELVGLA 129
Cdd:PTZ00265 480 IKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIKDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 130 DKAAAFP-----------SQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHE 198
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
....*
gi 1610668340 199 LEVVK 203
Cdd:PTZ00265 640 LSTIR 644
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-227 |
2.84e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLErPTAGRIIVNGNDITRMDKSALREYRlrtGMIFQHFNLLHARSVA 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 99 DNVAVPLEiAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARAL-----AARPD--VLLCDEATSALDP 171
Cdd:COG4138 88 QYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 172 ETTASVLNLLADINQkLNLTIVLITHELEvvKTL--CDHAALLEHGEIIESGRIADLL 227
Cdd:COG4138 167 AQQAALDRLLRELCQ-QGITVVMSSHDLN--HTLrhADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-171 |
1.18e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLL---ERPTAGRIIVNGNDITrmDKSALREY 78
Cdd:NF033858 2 ARLEGVSHRYGKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSL---LSLIagaRKIQQGRVEVLGGDMA--DARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGMIFQHF--NLLHARSVADNVAVpleIAKV---PKAARQARVAELLELVGLA---DKAAAfpsQLSGGQKQRVGIA 150
Cdd:NF033858 75 CPRIAYMPQGLgkNLYPTLSVFENLDF---FGRLfgqDAAERRRRIDELLRATGLApfaDRPAG---KLSGGMKQKLGLC 148
|
170 180
....*....|....*....|.
gi 1610668340 151 RALAARPDVLLCDEATSALDP 171
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDP 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-203 |
2.32e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 57 AGRIIVNGNDITRMDksaLREYRLRTGMIFQH---FNLlharSVADNVAVPLEIAKVPKAARQARVAELLELV-GLADK- 131
Cdd:PTZ00265 1276 SGKILLDGVDICDYN---LKDLRNLFSIVSQEpmlFNM----SIYENIKFGKEDATREDVKRACKFAAIDEFIeSLPNKy 1348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 132 ---AAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVK 203
Cdd:PTZ00265 1349 dtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-198 |
3.27e-15 |
|
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: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 4 IVGLSKTYAGtGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnllerptAGriivngnditrMDKSALREYRL--- 80
Cdd:TIGR03719 7 MNRVSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG-----------VDKDFNGEARPqpg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 -RTGMIFQHFNLLHARSVADNV--AVPlEIAKVPK-------------------AARQARVAELLELVGL---------A 129
Cdd:TIGR03719 68 iKVGYLPQEPQLDPTKTVRENVeeGVA-EIKDALDrfneisakyaepdadfdklAAEQAELQEIIDAADAwdldsqleiA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 130 DKAAAFP------SQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQklnlTIVLITHE 198
Cdd:TIGR03719 147 MDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-226 |
4.69e-15 |
|
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: 74.66 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 7 LSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdkSALREYRLRTGMIF 86
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQNMGYCP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 87 QHFNLLHARSVADNVAVPLEIAKVPkAARQARVAEL-LELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEA 165
Cdd:TIGR01257 2019 QFDAIDDLLTGREHLYLYARLRGVP-AEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 166 TSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-227 |
7.33e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.00 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMdksALREYRLRTGMIFQ--------- 87
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLGIIPQapvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 HFNL--LHARSVADnVAVPLEIAKVPKAARQ------ARVAELLElvgladkaaafpsQLSGGQKQRVGIARALAARPDV 159
Cdd:PLN03130 1330 RFNLdpFNEHNDAD-LWESLERAHLKDVIRRnslgldAEVSEAGE-------------NFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 160 LLCDEATSALDPETTASVlnlladinQKL------NLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL 227
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALI--------QKTireefkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-237 |
8.61e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.86 E-value: 8.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrlRTGMIFQHFNLLHARS 96
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR----RVLSIIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 97 VADNVAVPLE--IAKVPKAARQARVAELLEL--VGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPE 172
Cdd:PLN03232 1326 VRFNIDPFSEhnDADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 173 TTASVLNLLADinQKLNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLL---VAPWSRLRQS 237
Cdd:PLN03232 1406 TDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLsrdTSAFFRMVHS 1470
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-217 |
1.58e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.62 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL-NLLErPTAGRIIVNGND---ITRMDKSALREYRLRTGMIFQHFNL 91
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILgGDLE-PSAGNVSLDPNErlgKLRQDQFAFEEFTVLDTVIMGHTEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 LHARSVADNV-AVP------------LEI--AKVPKAARQARVAELLELVGLADKAAAFP-SQLSGGQKQRVGIARALAA 155
Cdd:PRK15064 93 WEVKQERDRIyALPemseedgmkvadLEVkfAEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 156 RPDVLLCDEATSALDPETtasvLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK15064 173 NPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-220 |
1.83e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLeRPTA---GRIIVNGNditrmdksaLRE 77
Cdd:NF040905 1 ILEMRGITKTFPGV--KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGE---------VCR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YR-LRTG------MIFQHFNLLHARSVADNVAVPLEIAK---VPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRV 147
Cdd:NF040905 69 FKdIRDSealgivIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIES 220
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-192 |
2.23e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNllERPTAGRI-----IVNGNDItrmDKSALReyrlRTGMIFQhfN 90
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVItggdrLVNGRPL---DSSFQR----SIGYVQQ--Q 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 91 LLHARSVADNVAV--------PLEIAKVPKAARQARVAELLELVGLADKAAAFPSQ-LSGGQKQRVGIARALAARPDVLL 161
Cdd:TIGR00956 845 DLHLPTSTVRESLrfsaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190
....*....|....*....|....*....|....*
gi 1610668340 162 -CDEATSALDPETTASVLNL---LADINQKLNLTI 192
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLmrkLADHGQAILCTI 959
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-197 |
2.99e-14 |
|
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: 68.72 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLHV-PGGAVYgILGRSGAGKSTLIRCLNLLERPTAGRIIvngnditrmdksalreYRLRTGMIFqhfnll 92
Cdd:cd03223 12 DGRVLLKDLSFEIkPGDRLL-ITGPSGTGKSSLFRALAGLWPWGSGRIG----------------MPEGEDLLF------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 harsvadnvavpleIAKVPKaarqarvaelLELVGLADkAAAFPSQ--LSGGQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:cd03223 69 --------------LPQRPY----------LPLGTLRE-QLIYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*..
gi 1610668340 171 PETTASVLNLLadinQKLNLTIVLITH 197
Cdd:cd03223 124 EESEDRLYQLL----KELGITVISVGH 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-173 |
7.31e-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: 70.73 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGN-DITRMDKSalREyrl 80
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVDQS--RD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 rtgmifqhfNLLHARSVADNVAVPLEIAKVPKAARQARV---------AELLELVGladkaaafpsQLSGGQKQRVGIAR 151
Cdd:TIGR03719 396 ---------ALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHLAK 456
|
170 180
....*....|....*....|..
gi 1610668340 152 ALAARPDVLLCDEATSALDPET 173
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVET 478
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-217 |
7.67e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 21 DVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSAlreyRLRTGMIF-----QHFNLLHAR 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 96 SVADNVaVPLEIAKVPKAARQARVAELLE----LVGL----ADKAAafpSQLSGGQKQRVGIARALAARPDVLLCDEATS 167
Cdd:PRK15439 357 PLAWNV-CALTHNRRGFWIKPARENAVLEryrrALNIkfnhAEQAA---RTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1610668340 168 ALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-197 |
9.17e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 5 VGLSKTYaGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnllerptAGriivngnditrMDKSALREYRL---- 80
Cdd:PRK11819 10 NRVSKVV-PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG-----------VDKEFEGEARPapgi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFNLLHARSVADNV--AVPLEIAKVPK------------------AARQARVAELLELVGLAD------KAA- 133
Cdd:PRK11819 71 KVGYLPQEPQLDPEKTVRENVeeGVAEVKAALDRfneiyaayaepdadfdalAAEQGELQEIIDAADAWDldsqleIAMd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 134 --------AFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQklnlTIVLITH 197
Cdd:PRK11819 151 alrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTH 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-227 |
1.35e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL-NLLERPTA-------GRIIVNGNDITRMDksALREYRLR 81
Cdd:PRK13547 8 HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGAprgarvtGDVTLNGEPLAAID--APRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tGMIFQHFNLLHARSVADNVAvpleIAKVPKAARQARVA--------ELLELVGLADKAAAFPSQLSGGQKQRVGIARAL 153
Cdd:PRK13547 86 -AVLPQAAQPAFAFSAREIVL----LGRYPHARRAGALThrdgeiawQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 154 A---------ARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIA 224
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
...
gi 1610668340 225 DLL 227
Cdd:PRK13547 241 DVL 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-240 |
1.78e-13 |
|
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: 69.94 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 6 GLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRC-LNLLErpTAGRIIVNGndiTRMDKSALREYRLRTGM 84
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAlLRLLS--TEGEIQIDG---VSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 IFQHFNLLHA--RSVADNVA--VPLEIAKVPkaarqarvaellELVGLADKAAAFPSQ-----------LSGGQKQRVGI 149
Cdd:TIGR01271 1297 IPQKVFIFSGtfRKNLDPYEqwSDEEIWKVA------------EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 150 ARALAARPDVLLCDEATSALDPETTASVLNLLADINQklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLVA 229
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNE 1441
|
250
....*....|.
gi 1610668340 230 PwSRLRQSLLH 240
Cdd:TIGR01271 1442 T-SLFKQAMSA 1451
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-227 |
2.09e-13 |
|
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: 68.01 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTL----IRCLNLLErptaGRIIVNGNDITRMDKSALRE 77
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 yrlRTGMIFQ---------HFNLLHARSVADNvavpleiakvpkaarqaRVAELLELVGLADKAAAFPSQL--------- 139
Cdd:cd03288 96 ---RLSIILQdpilfsgsiRFNLDPECKCTDD-----------------RLWEALEIAQLKNMVKSLPGGLdavvtegge 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 140 --SGGQKQRVGIARALAARPDVLLCDEATSALDPET----TASVLNLLADinqklnLTIVLITHELEVVKTlCDHAALLE 213
Cdd:cd03288 156 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLS 228
|
250
....*....|....
gi 1610668340 214 HGEIIESGRIADLL 227
Cdd:cd03288 229 RGILVECDTPENLL 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-227 |
2.53e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.59 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRTGMIFQH- 88
Cdd:TIGR00957 645 TWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKa 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 89 FNLLHARSVADNVAVPLEIAKVPKAARQArvaellelvgLADKAAafpsQLSGGQKQRVGIARALAARPDVLLCDEATSA 168
Cdd:TIGR00957 725 LNEKYYQQVLEACALLPDLEILPSGDRTE----------IGEKGV----NLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 169 LDPETTASVL-NLLADINQKLNLTIVLITHELEVVKTLcDHAALLEHGEIIESGRIADLL 227
Cdd:TIGR00957 791 VDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-227 |
3.26e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.76 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRlrTGMifqhfnllharsv 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL--TGI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 aDNVavplEIAKVPKAARQARVAELL-ELVGLADkAAAFPSQ----LSGGQKQRVGIARALAARPDVLLCDEATSALDPE 172
Cdd:PRK13545 104 -ENI----ELKGLMMGLTKEKIKEIIpEIIEFAD-IGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 173 TTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13545 178 FTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-226 |
3.51e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnLLERPT--AGRIIVNGNditrmdksalREYRLRTGMIFQhfnllh 93
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPPrsDASVVIRGT----------VAYVPQVSWIFN------ 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 aRSVADNV--AVPLEIAKVPKAARQARVAELLELVGLAD--KAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSAL 169
Cdd:PLN03130 693 -ATVRDNIlfGSPFDPERYERAIDVTALQHDLDLLPGGDltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 170 DPETTASVLN--LLADINQKlnlTIVLITHELEVVKTLcDHAALLEHGEIIESGRIADL 226
Cdd:PLN03130 772 DAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEEL 826
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-219 |
5.25e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 20 NDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDIT-RMDKSALR-------EYRLRTGMiFQHFnl 91
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKkgmayitESRRDNGF-FPNF-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 lharSVADNVAVpleiakvpkaARQARVAELLELVGL---------ADKAAAFPS-----------QLSGGQKQRVGIAR 151
Cdd:PRK09700 357 ----SIAQNMAI----------SRSLKDGGYKGAMGLfhevdeqrtAENQRELLAlkchsvnqnitELSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610668340 152 ALAARPDVLLCDEATSALDPETTASVLNL---LADINQklnlTIVLITHELEVVKTLCDHAALLEHGEIIE 219
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVmrqLADDGK----VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-221 |
5.57e-13 |
|
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: 65.75 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLerpTAGRIIVNGnDITrmdksalreYRlrtGMIFQHFNLLHA 94
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEG-DIH---------YN---GIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 95 RSVADNVAVPLEIAkvpkaarQARVAELLELVGLAdKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETT 174
Cdd:cd03233 83 GEIIYVSEEDVHFP-------TLTVRETLDFALRC-KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1610668340 175 ASVLNLLADINQKLNLTIVLITHE--LEVVKtLCDHAALLEHGEIIESG 221
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFVSLYQasDEIYD-LFDKVLVLYEGRQIYYG 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-230 |
1.14e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNgNDITRMDKSA-LREYRLRTGMIFqhFNLLHARSV 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAwIMNATVRGNILF--FDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 ADNVAV-PLEiakvpkaarqARVAELLElvGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTAS 176
Cdd:PTZ00243 753 ADAVRVsQLE----------ADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 177 VLN--LLADINQKlnlTIVLITHELEVVkTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PTZ00243 821 VVEecFLGALAGK---TRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-207 |
2.39e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.08 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLH---VPG-GAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDK---SALREY--RLRTGM 84
Cdd:cd03236 7 VHRYGPNSFKLHrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEfrgSELQNYftKLLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 IF-----QHFNLLhARSVADNVAVPLEiaKVPKAARQARVAELLELVGLADKAAafpSQLSGGQKQRVGIARALAARPDV 159
Cdd:cd03236 87 VKvivkpQYVDLI-PKAVKGKVGELLK--KKDERGKLDELVDQLELRHVLDRNI---DQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610668340 160 LLCDEATSALDPETTASVLNLLADINQKLNLTIVlITHELEVVKTLCD 207
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSD 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-216 |
3.16e-12 |
|
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: 65.96 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 29 GAVYGILGRSGAGKSTLIRCLnllerptAGRIIVNGNDITRM---DKsALREYRlrtGM-IFQHFnllhaRSVADN---V 101
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKIL-------SGELKPNLGDYDEEpswDE-VLKRFR---GTeLQDYF-----KKLANGeikV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 102 AV-PLEIAKVPKAARqARVAELLELV---GLADKAAAF----------PSQLSGGQKQRVGIARALAARPDVLLCDEATS 167
Cdd:COG1245 163 AHkPQYVDLIPKVFK-GTVRELLEKVderGKLDELAEKlglenildrdISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 168 ALDPE---TTASVLNLLADINQklnlTIVLITHELEVVKTLCDHAALLeHGE 216
Cdd:COG1245 242 YLDIYqrlNVARLIRELAEEGK----YVLVVEHDLAILDYLADYVHIL-YGE 288
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-221 |
4.69e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL------NLLErptaGRIIVNGNDITRMDKsalrEYRLRTGmIFQHF 89
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESILDLEP----EERAHLG-IFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 90 NLlharsvadnvavPLEIAKVP-----KAARQAR-----------------VAELLELVGLadkAAAFPSQ-----LSGG 142
Cdd:CHL00131 91 QY------------PIEIPGVSnadflRLAYNSKrkfqglpeldplefleiINEKLKLVGM---DPSFLSRnvnegFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 143 QKQRVGIARALAARPDVLLCDEATSALDPE---TTASVLNLLADINQklnlTIVLITHE---LEVVKTlcDHAALLEHGE 216
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYqrlLDYIKP--DYVHVMQNGK 229
|
....*
gi 1610668340 217 IIESG 221
Cdd:CHL00131 230 IIKTG 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-226 |
9.33e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTgrPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLErPTAGRIIVNGNDITrMDKSALReyrlR 81
Cdd:NF000106 14 VEVRGLVKHFGEV--KAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*TWC-ANRRALR----R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TgmIFQHFNLLHAR----SVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARP 157
Cdd:NF000106 86 T--IG*HRPVR*GRresfSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADL 226
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-227 |
9.42e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.30 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGnDITRMDKSALREYRLrTGMifqhfnllharsv 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQL-TGI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 aDNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASV 177
Cdd:PRK13546 104 -ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1610668340 178 LNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK13546 183 LDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-172 |
9.56e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 10 TYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRTGMIFQ-- 87
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKAdl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 ------HF-NLLHARSVadnvavpleiAKVPKAArqarvaelLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK13543 98 stlenlHFlCGLHGRRA----------KQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|..
gi 1610668340 161 LCDEATSALDPE 172
Cdd:PRK13543 160 LLDEPYANLDLE 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-240 |
1.77e-11 |
|
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: 62.95 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRC-LNLLErpTAGRIIVNGndiTRMDKSALREYRL 80
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLN--TEGDIQIDG---VSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGMIFQHFnLLHARSVADNvavpLEIAKVPKAARQARVAellELVGLADKAAAFPSQ-----------LSGGQKQRVGI 149
Cdd:cd03289 78 AFGVIPQKV-FIFSGTFRKN----LDPYGKWSDEEIWKVA---EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 150 ARALAARPDVLLCDEATSALDPETTASVLNLLAdiNQKLNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADLLvA 229
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLL-N 225
|
250
....*....|.
gi 1610668340 230 PWSRLRQSLLH 240
Cdd:cd03289 226 EKSHFKQAISP 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-197 |
1.91e-11 |
|
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: 61.74 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYrlrtgMIFQHFNLLHA 94
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-----LYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 95 R-SVADNVAVPLEIAKvpkaarQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPET 173
Cdd:cd03231 87 TlSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....
gi 1610668340 174 TASVLNLLADINQKLNLtIVLITH 197
Cdd:cd03231 161 VARFAEAMAGHCARGGM-VVLTTH 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-226 |
2.90e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnLLERPTAgriivngnDITRMDKSALREYRLRTGMIFQhfnllh 93
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHA--------ETSSVVIRGSVAYVPQVSWIFN------ 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 aRSVADNV--AVPLEIAKVPKAARQARVAELLELVGLADKAAAFPS--QLSGGQKQRVGIARALAARPDVLLCDEATSAL 169
Cdd:PLN03232 693 -ATVRENIlfGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 170 DPETTASVLNllADINQKLN-LTIVLITHELEVVKtLCDHAALLEHGEIIESGRIADL 226
Cdd:PLN03232 772 DAHVAHQVFD--SCMKDELKgKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-198 |
3.61e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLN---LLERptaGRIIVNGNDI-TRMDKSALREyrlRTGMIFQHfnll 92
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQDLIvARLQQDPPRN---VEGTVYDF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 harsVADNVAvplEIAKVPKAARQ---------------------------------ARVAELLELVGL-ADKAAafpSQ 138
Cdd:PRK11147 87 ----VAEGIE---EQAEYLKRYHDishlvetdpseknlnelaklqeqldhhnlwqleNRINEVLAQLGLdPDAAL---SS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 139 LSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQklnlTIVLITHE 198
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHD 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-200 |
5.12e-11 |
|
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: 60.81 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 13 GTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnLLERPTAGRIIVNGNDITRMDKSALREYRLRTGMIF--QHFN 90
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 91 LLHArSVADNVAV--PLEIAKVPKAARQARVAELLELVGLADKAAAFPS--QLSGGQKQRVGIARALAARPDVLLCDEAT 166
Cdd:cd03290 90 LLNA-TVEENITFgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1610668340 167 SALDPETT-----ASVLNLLADINQklnlTIVLITHELE 200
Cdd:cd03290 169 SALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKLQ 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-217 |
5.48e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 17 PALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL-NLLERpTAGRIIVNGNDI-TRMDKSALR-------EYRLRTGMIFq 87
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVvTRSPQDGLAngivyisEDRKRDGLVL- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 88 hfnllhARSVADNVAVPlEIAKVPKAARQARVAELLELVGlaDKAAAF----PSQ------LSGGQKQRVGIARALAARP 157
Cdd:PRK10762 344 ------GMSVKENMSLT-ALRYFSRAGGSLKHADEQQAVS--DFIRLFniktPSMeqaiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 158 DVLLCDEATSALDPETTASVLNLladINQ--KLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-207 |
8.50e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 29 GAVYGILGRSGAGKSTLIRCLnllerptAGRIIVN-GNDITRMDKSA-LREYRlRTGMiFQHFNLLHARSVadNVAV-PL 105
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-------SGELIPNlGDYEEEPSWDEvLKRFR-GTEL-QNYFKKLYNGEI--KVVHkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 106 EIAKVPKAARqARVAELLELVglaDKAAAFP----------------SQLSGGQKQRVGIARALAARPDVLLCDEATSAL 169
Cdd:PRK13409 168 YVDLIPKVFK-GKVRELLKKV---DERGKLDevverlglenildrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|....*...
gi 1610668340 170 DPETTASVLNLLADINQklNLTIVLITHELEVVKTLCD 207
Cdd:PRK13409 244 DIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLAD 279
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-230 |
9.60e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 22 VSLHVPGGAVYGILGRSGAGKSTLIRCL-NLLerPTAGRIIVNGNDITRMDKSALREYRlrtGMIFQHFNLLHARSVADN 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 101 VAVPLEiAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARAL-----AARPD--VLLCDEATSALDPET 173
Cdd:PRK03695 90 LTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 174 TASVLNLLADINQkLNLTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLLVAP 230
Cdd:PRK03695 169 QAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-198 |
9.68e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL--NLLERPTAGRIIVNGNDITrmdKSALReyrlRTGMIFQHfNLLH 93
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPT---KQILK----RTGFVTQD-DILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAVPLEIAKVPKA-ARQ--ARVAE-LLELVGLAD-----KAAAFPSQLSGGQKQRVGIARALAARPDVLLCDE 164
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSlTKQekILVAEsVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....
gi 1610668340 165 ATSALDPETTASVLNLLADINQKlNLTIVLITHE 198
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-208 |
1.20e-10 |
|
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: 60.11 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGA-----VYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDK--SALREYRLRtgmifqhfNL 91
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQyiKADYEGTVR--------DL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 LHarSVADNVAVpleiakvpKAARQARVAELLELVGLADKAAafpSQLSGGQKQRVGIARALAARPDVLLCDEATSALDP 171
Cdd:cd03237 82 LS--SITKDFYT--------HPYFKTEIAKPLQIEQILDREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1610668340 172 ET---TASVLNLLADINQKlnlTIVLITHELEVVKTLCDH 208
Cdd:cd03237 149 EQrlmASKVIRRFAENNEK---TAFVVEHDIIMIDYLADR 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-183 |
1.33e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALReyrlrtgmifqhfNLL-- 92
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ-------------DLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 93 -HARSVADnVAVPLE----IAKVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATS 167
Cdd:PRK13538 80 gHQPGIKT-ELTALEnlrfYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170
....*....|....*.
gi 1610668340 168 ALDPETTASVLNLLAD 183
Cdd:PRK13538 159 AIDKQGVARLEALLAQ 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-192 |
2.12e-10 |
|
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: 58.41 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 12 AGTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNllERPTAGRIivnGNDITrMDKSALREYRLRTGMIFQHFNL 91
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVI---TGEIL-INGRPLDKNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 LHArsvadnvavpleiakvpkaarQARVAELLELvgladkaAAFPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDP 171
Cdd:cd03232 90 HSP---------------------NLTVREALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....
gi 1610668340 172 ETTASVLNL---LADINQKLNLTI 192
Cdd:cd03232 142 QAAYNIVRFlkkLADSGQAILCTI 165
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-201 |
5.29e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 29 GAVYGILGRSGAGKSTLIRCL-NLLERPTAGRIIVNGNDITRMDKSALREYRLRTGmifqhfnllharsvadnvavplei 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 108 akvpkaarqarvaellelvgladkaaafPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVL-----NLLA 182
Cdd:smart00382 58 ----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLL 109
|
170
....*....|....*....
gi 1610668340 183 DINQKLNLTIVLITHELEV 201
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKD 128
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-173 |
6.02e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGtgRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVnGN--DITRMDKSalREyr 79
Cdd:PRK11819 325 IEAENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDQS--RD-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 80 lrtgmifqhfNLLHARSVADNVAVPLEIAKVPKAARQARV---------AELLELVGladkaaafpsQLSGGQKQRVGIA 150
Cdd:PRK11819 398 ----------ALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVG----------VLSGGERNRLHLA 457
|
170 180
....*....|....*....|...
gi 1610668340 151 RALAARPDVLLCDEATSALDPET 173
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-198 |
1.37e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYAGTGRpALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmdKSALREYRLR 81
Cdd:PRK10522 323 LELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 TGMIFQHFNLLHARSVADNvavpleiakvpKAARQARVAELLELVGLADKAA-----AFPSQLSGGQKQRVGIARALAAR 156
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPEG-----------KPANPALVEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1610668340 157 PDVLLCDEATSALDP----ETTASVLNLLadinQKLNLTIVLITHE 198
Cdd:PRK10522 468 RDILLLDEWAADQDPhfrrEFYQVLLPLL----QEMGKTIFAISHD 509
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
2.30e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRmDKSALREYRL 80
Cdd:PRK13540 1 MLDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 81 RTGmifqhfnllHARSVADNVAVPLE-IAKVPKAARQARVAELLELVGLaDKAAAFP-SQLSGGQKQRVGIARALAARPD 158
Cdd:PRK13540 78 FVG---------HRSGINPYLTLRENcLYDIHFSPGAVGITELCRLFSL-EHLIDYPcGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1610668340 159 VLLCDEATSALDPETTASVLNLLADiNQKLNLTIVLITHE 198
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-217 |
2.60e-09 |
|
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: 57.14 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL-NLLERPTAGRIIVNGNDI-TRMDKSALR-------EYRLRTGMIF 86
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVdIRNPAQAIRagiamvpEDRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 87 QhfnllhaRSVADNVAVPL-----EIAKVPKAARQARVAELLELVGLADKAAAFP-SQLSGGQKQRVGIARALAARPDVL 160
Cdd:TIGR02633 353 I-------LGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-221 |
2.92e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLE--RPTAGRIIVNGNDITRMDKsalrEYRLRTG--MIFQHfn 90
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSP----EDRAGEGifMAFQY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 91 llharsvadnvavPLEIAKVP---------KAARQARVAELLELVGLAD------KAAAFPSQL---------SGGQKQR 146
Cdd:PRK09580 87 -------------PVEIPGVSnqfflqtalNAVRSYRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 147 VGIARALAARPDVLLCDEATSALDPETTASV---LNLLADINQklnlTIVLITHE---LEVVKTlcDHAALLEHGEIIES 220
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRDGKR----SFIIVTHYqriLDYIKP--DYVHVLYQGRIVKS 227
|
.
gi 1610668340 221 G 221
Cdd:PRK09580 228 G 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-217 |
9.73e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 20 NDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDIT-RMDKSALR-------EYRLRTGMIfqhfnl 91
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRagimlcpEDRKAEGII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 92 lHARSVADNVAVPLEIAKVP-----KAARQARVAELLelvgLADKAAAFPS------QLSGGQKQRVGIARALAARPDVL 160
Cdd:PRK11288 344 -PVHSVADNINISARRHHLRagcliNNRWEAENADRF----IRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610668340 161 LCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-204 |
1.07e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.48 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAVYGILGRSGAGKSTLirCLNLLERPTAGRIIvngnditrmdKSALREYRLRTGMIFQHFNLlharsv 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLI----------SFLPKFSRNKLIFIDQLQFL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 98 adnVAVPLEIAKVPKAArqarvaellelvgladkaaafpSQLSGGQKQRVGIARALAARPD--VLLCDEATSALDPETTA 175
Cdd:cd03238 72 ---IDVGLGYLTLGQKL----------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*....
gi 1610668340 176 SVLNLLADINQKLNlTIVLITHELEVVKT 204
Cdd:cd03238 127 QLLEVIKGLIDLGN-TVILIEHNLDVLSS 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-217 |
1.40e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 7 LSKTYAGTG-RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRI-IVNGnditrmdksalreyrLRTGM 84
Cdd:PRK10636 315 MEKVSAGYGdRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKG---------------IKLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 IFQHfNLLHARsvADNVAVPLEIAKVPKAARQaRVAELLELVGL-ADKAAAFPSQLSGGQKQRVGIARALAARPDVLLCD 163
Cdd:PRK10636 380 FAQH-QLEFLR--ADESPLQHLARLAPQELEQ-KLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610668340 164 EATSALDPETTASVLNLLADINQKLnltiVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-170 |
2.59e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLE---RPTAGRII-----VNGNDITRMdKSALREYRLRTGMIF 86
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQILhveqeVVGDDTTAL-QCVLNTDIERTQLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 87 QHFNLLHARSVADNVAVPL-----EIAKVPKAARQARVAELLELVGLADKAAA------------FPSQL--------SG 141
Cdd:PLN03073 268 EEAQLVAQQRELEFETETGkgkgaNKDGVDKDAVSQRLEEIYKRLELIDAYTAearaasilaglsFTPEMqvkatktfSG 347
|
170 180
....*....|....*....|....*....
gi 1610668340 142 GQKQRVGIARALAARPDVLLCDEATSALD 170
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-205 |
8.15e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYagTGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLnllerptAGRIIVNGNDITRMDKSALreyrlr 81
Cdd:PRK15064 320 LEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVKWSENANI------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 82 tGMIFQHfnllHARSVADNVAVPLEIA--KVPKAARQARVAELLELVGLADKAAAFPSQLSGGQKQRVGIARALAARPDV 159
Cdd:PRK15064 385 -GYYAQD----HAYDFENDLTLFDWMSqwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1610668340 160 LLCDEATSALDPETTASvLNLLADinqKLNLTIVLITHELEVVKTL 205
Cdd:PRK15064 460 LVMDEPTNHMDMESIES-LNMALE---KYEGTLIFVSHDREFVSSL 501
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-203 |
9.14e-08 |
|
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: 51.07 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 34 ILGRSGAGKSTLIRCLNLL---ERPTAGRIIVNGNDITRmDKSALREYRLRtgmiFQHFN--LLHAR---SVADNVAVpl 105
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIR-EGEVRAQVKLA----FENANgkKYTITrslAILENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 106 eiakvpkaARQARVAELLELVgladkaaafPSQLSGGQKQ------RVGIARALAARPDVLLCDEATSALDPETTASVL- 178
Cdd:cd03240 100 --------CHQGESNWPLLDM---------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLa 162
|
170 180
....*....|....*....|....*
gi 1610668340 179 NLLADINQKLNLTIVLITHELEVVK 203
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVD 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-197 |
1.23e-07 |
|
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: 52.06 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIivngnditrmdksalreYRLRTGMIF-----QHFNLlh 93
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----------------TKPAKGKLFyvpqrPYMTL-- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 aRSVADNVAVPLEIAKV-PKAARQARVAELLELVGLA---------DKAAAFPSQLSGGQKQRVGIARALAARPDVLLCD 163
Cdd:TIGR00954 529 -GTLRDQIIYPDSSEDMkRRGLSDKDLEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 1610668340 164 EATSALDPETTASVLNLLadinQKLNLTIVLITH 197
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
110-227 |
1.31e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 110 VPKAARQARVAELLELVGLADKAaaFpSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlN 189
Cdd:PRK10938 110 VKDPARCEQLAQQFGITALLDRR--F-KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-G 185
|
90 100 110
....*....|....*....|....*....|....*...
gi 1610668340 190 LTIVLITHELEVVKTLCDHAALLEHGEIIESGRIADLL 227
Cdd:PRK10938 186 ITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-182 |
2.35e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALreyrlrtGMIFQHFNLLHARSVA 98
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-------TYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 99 DNVAVPLEI----AKVPKAARQARVAELLelvglaDKAAAfpsQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETT 174
Cdd:PRK13541 89 ENLKFWSEIynsaETLYAAIHYFKLHDLL------DEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
....*...
gi 1610668340 175 ASVLNLLA 182
Cdd:PRK13541 160 DLLNNLIV 167
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-199 |
2.54e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 1 MIEIVGLSKTYagtgrpalNDVSLHVPGGAVY-----GILGRSGAGKSTLIRCLNLLERPTAGRI------------IVN 63
Cdd:PRK13409 340 LVEYPDLTKKL--------GDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqyIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 64 GNDITRMDksalreyrlrtgmifqhfnLLhaRSVADNVAVPL---EIAKvPkaarqarvaelLELVGLADKAAafpSQLS 140
Cdd:PRK13409 412 DYDGTVED-------------------LL--RSITDDLGSSYyksEIIK-P-----------LQLERLLDKNV---KDLS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610668340 141 GGQKQRVGIARALAARPDVLLCDEATSALDPE---TTASVLNLLADINQKlnlTIVLITHEL 199
Cdd:PRK13409 456 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIAEEREA---TALVVDHDI 514
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-226 |
6.05e-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: 50.29 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITRMDKSALREYRLRTGMIFQ-HFNLLH 93
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGlSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 94 ARSVADNVAVPLEIAKVPKAARQArvaellelvgLADKAAAfpsqLSGGQKQRVGIARALAARPDVLLCDEATSALDPET 173
Cdd:TIGR01271 518 YTSVIKACQLEEDIALFPEKDKTV----------LGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 174 TASVL-----NLLAdinqklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADL 226
Cdd:TIGR01271 584 EKEIFesclcKLMS------NKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-217 |
1.60e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 14 TGRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCL-NLLERPTAGRIIVNGNDIT-RMDKSALR-------EYRLRTGM 84
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKiRNPQQAIAqgiamvpEDRKRDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 85 IFQhfnllhaRSVADNVAVPLeIAKVPKAARQARVAELL----ELVGLADKAAAfP----SQLSGGQKQRVGIARALAAR 156
Cdd:PRK13549 353 VPV-------MGVGKNITLAA-LDRFTGGSRIDDAAELKtileSIQRLKVKTAS-PelaiARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610668340 157 PDVLLCDEATSALDPETTASVLNLladINQ--KLNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKL---INQlvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-207 |
2.27e-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: 48.24 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 2 IEIVGLSKTYagtgrpalNDVSLHVPGGAVY-----GILGRSGAGKSTLIRCLNLLERPTAGRI------------IVNG 64
Cdd:COG1245 342 VEYPDLTKSY--------GGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqyISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 65 NDITrmdksaLREYrLRTgmifqhfnllharSVADNVAVPLEiakvpkaarQARVAELLELVGLADKAAafpSQLSGGQK 144
Cdd:COG1245 414 YDGT------VEEF-LRS-------------ANTDDFGSSYY---------KTEIIKPLGLEKLLDKNV---KDLSGGEL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610668340 145 QRVGIARALAARPDVLLCDEATSALDPE---TTASVLNLLADINQKlnlTIVLITHELEVVKTLCD 207
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRFAENRGK---TAMVVDHDIYLIDYISD 524
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-226 |
2.97e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.54 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 15 GRPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGnditRMDKSAlreyrlrtgmifqHFNLLHA 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----RISFSS-------------QFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 95 RSVADNVavpleIAKVpkAARQARVAELLELVGLADKAAAFPSQ-----------LSGGQKQRVGIARALAARPDVLLCD 163
Cdd:cd03291 112 GTIKENI-----IFGV--SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 164 EATSALDPETT-----ASVLNLLAdinqklNLTIVLITHELEVVKTlCDHAALLEHGEIIESGRIADL 226
Cdd:cd03291 185 SPFGYLDVFTEkeifeSCVCKLMA------NKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-205 |
4.81e-06 |
|
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: 45.43 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 20 NDVSLhvPGGAVYGILGRSGAGKSTLIRCLNLLerptagriivngnditrmdksalreyrlrTGMIFQHFNLLHARSVAD 99
Cdd:cd03227 14 NDVTF--GEGSLTIITGPNGSGKSTILDAIGLA-----------------------------LGGAQSATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 100 NVAvpleiakvpkaarqARVAELLELVgladkaaafpSQLSGGQKQRVGIARALA-----ARPDVLLcDEATSALDPETT 174
Cdd:cd03227 63 IVA--------------AVSAELIFTR----------LQLSGGEKELSALALILAlaslkPRPLYIL-DEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|.
gi 1610668340 175 ASVLNLLADINQKLNLTIVlITHELEVVKTL 205
Cdd:cd03227 118 QALAEAILEHLVKGAQVIV-ITHLPELAELA 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-171 |
5.21e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLircLNLL--ERPTA--------GRIIVNGNDITRMDK------SALR-EY 78
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTL---LSLItgDHPQGysndltlfGRRRGSGETIWDIKKhigyvsSSLHlDY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 79 RLRTGmifqhfnllhARSVA-----DNVAVpleIAKVPKAARQaRVAELLELVGLADKAAAFPSQ-LSGGQKQRVGIARA 152
Cdd:PRK10938 350 RVSTS----------VRNVIlsgffDSIGI---YQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRA 415
|
170
....*....|....*....
gi 1610668340 153 LAARPDVLLCDEATSALDP 171
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDP 434
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-208 |
7.35e-06 |
|
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: 46.07 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 19 LNDVSLHVPGGAVYGILGRSGAGKSTLI--------RCLNLLERPTAGR-------------IIVNGNDITRMDKSALRE 77
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalARRLHLKKEQPGNhdrieglehidkvIVIDQSPIGRTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 78 YrlrTGmIFQH-------------FN------LLHARSVADNVAVPLEIA-----KVPKAARQARvaeLLELVGLADKAA 133
Cdd:cd03271 91 Y---TG-VFDEirelfcevckgkrYNretlevRYKGKSIADVLDMTVEEAleffeNIPKIARKLQ---TLCDVGLGYIKL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 134 AFPS-QLSGGQKQRVGIARALAAR---PDVLLCDEATSALDPETTASVLNLLADINQKLNlTIVLITHELEVVKTlCDH 208
Cdd:cd03271 164 GQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKC-ADW 240
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-204 |
4.80e-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: 44.23 E-value: 4.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610668340 139 LSGGQKQRVGIARALAAR---PDVLLCDEATSALDPETTASVLNLLADINQKLNlTIVLITHELEVVKT 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKT 897
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-196 |
7.11e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 34 ILGRSGAGKSTLIRCLNL----LERPTAGRIIVNGNDITRMDKsalreyRLRTGMIFQ-----HFNLLHARSVADNVA-- 102
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKK------HYRGDVVYNaetdvHFPHLTVGETLDFAArc 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 103 --VPLEIAKVPKAARQARVAEL-LELVGLADKAAA-----FPSQLSGGQKQRVGIARALAARPDVLLCDEATSALDPETT 174
Cdd:TIGR00956 166 ktPQNRPDGVSREEYAKHIADVyMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATA 245
|
170 180
....*....|....*....|..
gi 1610668340 175 ASVLNLLADINQKLNLTiVLIT 196
Cdd:TIGR00956 246 LEFIRALKTSANILDTT-PLVA 266
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-252 |
1.30e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 137 SQLSGGQKQRVGIARALAA---RPDVLLCDEATSALDPETTASVLNLLADINQkLNLTIVLITHELEVVKTlCDHaaLLE 213
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVKV-ADY--VLE 883
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1610668340 214 HGEiiESGRIADLLVAPWSRLRQSLLHDPQAE--RDFLARH 252
Cdd:PRK00635 884 LGP--EGGNLGGYLLASCSPEELIHLHTPTAKalRPYLSSP 922
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-217 |
2.36e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 16 RPALNDVSLHVPGGAVYGILGRSGAGKSTLIRCLNLLERPTAGRIIVNGNDITrmDKSALR----------EYRLRTGmI 85
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN--NHNANEainhgfalvtEERRSTG-I 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 86 F------------------QHFNLLHARSVADNVAVPLEIAKVPKAARQARVaellelvgladkaaafpSQLSGGQKQRV 147
Cdd:PRK10982 338 YayldigfnslisnirnykNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI-----------------GSLSGGNQQKV 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 148 GIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKlNLTIVLITHELEVVKTLCDHAALLEHGEI 217
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-208 |
3.42e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 3.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610668340 139 LSGGQKQRVGIARALAARPD-----VLlcDEATSALDPETTA---SVLNLLADinqKLNlTIVLITHELEVVKTlCDH 208
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktlyIL--DEPTTGLHFEDIRkllEVLHRLVD---KGN-TVVVIEHNLDVIKT-ADW 901
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-197 |
3.68e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 31 VYGILGRSGAGKSTLIRCLNLL-----ERPTAGR--IIVNGND----------------ITRMDKSALREYRL----RTG 83
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRYAlygkaRSRSKLRsdLINVGSEeasvelefehggkryrIERRQGEFAEFLEAkpseRKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 84 MIFQHFNLLHARSVADNVA---VPLEIAKVPKAARQARVAELL-ELVGLADkaaafPSQLSGGQKQRVGIARALAarpdv 159
Cdd:COG0419 105 ALKRLLGLEIYEELKERLKeleEALESALEELAELQKLKQEILaQLSGLDP-----IETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1610668340 160 LLCDeaTSALDPETTASVLNLLADinqklnltIVLITH 197
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE--------LAIITH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-182 |
4.56e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 18 ALNDVSLHVPGGAV------YGI--------LGRSGAGKSTLIRCLNLLERPTAGRIivngnditrmdksaLREYRLRTG 83
Cdd:PLN03073 510 SFSDASFGYPGGPLlfknlnFGIdldsriamVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 84 MIFQHfnllHARSVADNVAVPLEIAKVPKAARQARVAELLELVGLADKAAAFPS-QLSGGQKQRVGIARALAARPDVLLC 162
Cdd:PLN03073 576 VFSQH----HVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180
....*....|....*....|
gi 1610668340 163 DEATSALDPETTASVLNLLA 182
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLV 671
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
139-213 |
8.04e-04 |
|
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: 39.48 E-value: 8.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610668340 139 LSGGQKQRVGIARALAARPDVLLCDEATSALDPETTASVLNLLADINQKLNLTIVLITHELEVVKTLCDHAALLE 213
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
137-183 |
9.08e-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: 37.60 E-value: 9.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610668340 137 SQLSGGQKQRVG---IARALAA----------RPDVLLCDEATSALDPETTASVLNLLAD 183
Cdd:pfam13558 31 GGLSGGEKQLLAylpLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| |
