|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-240 |
7.64e-158 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 437.12 E-value: 7.64e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskDKKSQI-EVRKQ 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDInKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLNV 239
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSK 238
|
.
gi 581794297 240 I 240
Cdd:COG1126 239 V 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
1.13e-132 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 374.14 E-value: 1.13e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKS-------- 72
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 73 -QIE-VRKQSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIAR 150
Cdd:COG4598 88 rQLQrIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 151 ALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
....*..
gi 581794297 231 EELRRFL 237
Cdd:COG4598 248 ERLRQFL 254
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
3.31e-124 |
|
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: 351.06 E-value: 3.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTsKDKKSQIEVRKQSG 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-237 |
1.69e-111 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 320.12 E-value: 1.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGktYTSKDKKSQI-EVRKQ 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDErLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-238 |
4.20e-100 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 291.65 E-value: 4.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYV-----NGKTYTSKDKKSQIE 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 VRKQSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRR 235
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
...
gi 581794297 236 FLN 238
Cdd:PRK11264 243 FLE 245
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
5.66e-93 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 276.57 E-value: 5.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLaNE--GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELR 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDI-NRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238
|
....
gi 581794297 235 RFLN 238
Cdd:COG1135 239 RFLP 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
4.47e-90 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 269.66 E-value: 4.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSkdkksqIEVRK-Q 79
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------LPPEKrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLN 238
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG 237
|
...
gi 581794297 239 VIN 241
Cdd:COG3842 238 EAN 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
9.55e-88 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 259.21 E-value: 9.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQS-GMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:COG1136 84 RRRHiGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAkEVSNNIVFIHEGMIGEQ 218
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-238 |
1.96e-87 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 259.52 E-value: 1.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYT-SKDKKSQIEV---- 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlVRDKDGQLKVadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 -----RKQSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTH-VKDQRPHALSGGQQQRVAIAR 150
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 151 ALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 581794297 231 EELRRFLN 238
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
2.33e-87 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 258.76 E-value: 2.33e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKtEELRRFL 237
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD-PWVRQFL 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
1.19e-86 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 257.25 E-value: 1.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDK---KSQIEVRK 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpseKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGApEEMFNRPKTEELRRFLN 238
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.46e-85 |
|
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: 253.18 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFND----VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVR 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQS-GMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:cd03255 81 RRHiGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSnNIVFIHEGMI 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-240 |
2.71e-85 |
|
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: 253.98 E-value: 2.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKT-YTSKDKKSQI------ 74
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQlYHMPGRNGPLvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 ---EVRKQSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARA 151
Cdd:TIGR03005 81 hlrQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|
gi 581794297 231 EELRRFLNVI 240
Cdd:TIGR03005 241 ERTREFLSKV 250
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-229 |
3.86e-85 |
|
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: 252.89 E-value: 3.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-238 |
8.88e-84 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 249.93 E-value: 8.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTY---TSKDKKSQIEVRK 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGApEEMFNRPKTEELRRFLN 238
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-230 |
4.48e-81 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 246.52 E-value: 4.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKD-KKSQIevrkq 79
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPpKDRNI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 sGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG3839 78 -AMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHE----MRFAkevsNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-195 |
1.39e-80 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 242.30 E-value: 1.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkksqiEV 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT--------GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 581794297 157 KVMLFDEPTSALDP----ELVNDVLKVikdLANEGMTMVIVTH 195
Cdd:COG1116 158 EVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTH 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
2.00e-80 |
|
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: 249.82 E-value: 2.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF-----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIE 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 VRKQSGMVFQSYN--LFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL-THVKDQRPHALSGGQQQRVAIARAL 152
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK-- 229
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQhp 499
|
....*
gi 581794297 230 -TEEL 233
Cdd:COG1123 500 yTRAL 504
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-235 |
1.36e-79 |
|
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: 238.77 E-value: 1.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQS 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR---ELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYN--LFpHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:COG1122 78 GLVFQNPDdqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPktEELRR 235
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY--ELLEE 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
3.00e-79 |
|
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: 237.03 E-value: 3.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSkdkksqIEVRKQS- 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPERRNi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-237 |
3.64e-79 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 241.63 E-value: 3.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRR 235
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
..
gi 581794297 236 FL 237
Cdd:PRK11153 240 FI 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
1.87e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 236.49 E-value: 1.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQ 79
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLI--------TVKKLKKDEaRGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARA 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrsLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-237 |
1.08e-77 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 237.74 E-value: 1.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSkdkksQIEVRK-QS 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-----NLPPRErRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
9.23e-77 |
|
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: 229.77 E-value: 9.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEvRKQSG 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-RRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGlitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-226 |
3.52e-75 |
|
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: 227.77 E-value: 3.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFN 226
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
3.54e-75 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 227.24 E-value: 3.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKKSQI-EVRK 78
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLKRREIpYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-224 |
3.52e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 224.94 E-value: 3.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkKSQIEVRKQSG 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENV--MEGLitvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG1131 77 YVPQEPALYPDLTVRENLrfFARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
4.69e-74 |
|
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: 225.07 E-value: 4.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQiev 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSY--NLFPHKTALENVMEGLitvKKLKKDEARGKSLELLEKVGLT-HVKDQRPHALSGGQQQRVAIARALA 153
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAEPL---RIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEE 232
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*.
gi 581794297 233 LRRFLN 238
Cdd:COG1124 235 TRELLA 240
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-237 |
5.89e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 226.90 E-value: 5.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqIEVRKQ 79
Cdd:COG1125 1 MIEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDP---VELRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMegliTVKKLK---KDEARGKSLELLEKVGL--THVKDQRPHALSGGQQQRVAIARALAM 154
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIA----TVPRLLgwdKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 155 NPKVMLFDEPTSALDP----ELVNDVLKVIKDLaneGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:COG1125 154 DPPILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPAN 230
|
....*..
gi 581794297 231 EELRRFL 237
Cdd:COG1125 231 DFVADFV 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
9.10e-74 |
|
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: 224.37 E-value: 9.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS 80
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVK-------KLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-208 |
7.39e-73 |
|
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: 221.19 E-value: 7.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskdkkSQIEVR 77
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--------PVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 158 VMLFDEPTSALDP----ELVNDVLKVIKDlanEGMTMVIVTHEMRFAKEVSNNIV 208
Cdd:cd03293 152 VLLLDEPFSALDAltreQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVV 203
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-237 |
1.28e-71 |
|
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: 218.65 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSG 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
4.20e-71 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 217.05 E-value: 4.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL-----EIPTEGTVYVNGKTYTSKDKkSQIEV 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV-DVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPhKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLT-HVKDQ-RPHALSGGQQQRVAIARALAM 154
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEgMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-237 |
3.44e-70 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 215.24 E-value: 3.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL-----EIPTEGTVYVNGKTYTSKdKKSQIEV 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDK-KIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPhKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL-THVKD---QRPHALSGGQQQRVAIARAL 152
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwDEVKDrlhDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEE 232
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*
gi 581794297 233 LRRFL 237
Cdd:TIGR00972 239 TEDYI 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-219 |
4.04e-70 |
|
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: 214.68 E-value: 4.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQ-SYN-LFPHKTALENVMEGLITVKKLKKDEARGK-SLELLEKVGL-THVKDQRPHALSGGQQQRVAIARAL 152
Cdd:cd03257 81 RKEIQMVFQdPMSsLNPRMTIGEQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
5.39e-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: 213.48 E-value: 5.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVE--VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQS 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK---ELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNL-FPHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-230 |
1.28e-68 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 214.90 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSG 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-----KRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKN-RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 162 DEPTSALDPeLVNDVLKV-IKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:TIGR03265 159 DEPLSALDA-RVREHLRTeIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPAT 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-237 |
2.43e-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: 210.62 E-value: 2.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVE-VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksQIEVRKQS 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVmeGLI-TVKKLKKDEARGKSLELLEKVGL--THVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENI--ALVpKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 158 VMLFDEPTSALDP----ELVNDVLKVIKDLaneGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEEL 233
Cdd:cd03295 156 LLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFV 232
|
....
gi 581794297 234 RRFL 237
Cdd:cd03295 233 AEFV 236
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
2.48e-68 |
|
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: 210.62 E-value: 2.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQ 79
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLITVKK-------LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARAL 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
1.62e-66 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 205.37 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVevIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksqIEVRKQS 80
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----PAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 gMVFQSYNLFPHKTALENVMEGLITVKKLKKDEaRGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:COG3840 75 -MLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-236 |
1.67e-66 |
|
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: 206.73 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 5 NNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS-GMV 83
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKiSMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 84 FQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 164 PTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRF 236
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-243 |
4.61e-66 |
|
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: 204.71 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqiEVRKQS 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR----EARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVmEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:COG4555 77 GVLPDERGLYDRLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRR-FLNV 239
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDaFVAL 235
|
....
gi 581794297 240 INEE 243
Cdd:COG4555 236 IGSE 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-237 |
1.08e-65 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 203.72 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSG 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLiTVKKLK----KDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGL-RVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRF 236
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
.
gi 581794297 237 L 237
Cdd:cd03296 237 L 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-236 |
7.84e-65 |
|
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: 202.68 E-value: 7.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFN-----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQ--SYNLFpHKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTH-VKDQRPHALSGGQQQRVAIARALA 153
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLG-LSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPktEE 232
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV--DE 236
|
....
gi 581794297 233 LRRF 236
Cdd:TIGR04521 237 LEKI 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-238 |
5.02e-64 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 199.88 E-value: 5.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL--EIP---TEGTVYVNGK-TYTskDKKSQIE 75
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEdIYD--PDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 VRKQSGMVFQSYNLFPhKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL-THVKD---QRPHALSGGQQQRVAIARA 151
Cdd:COG1117 90 LRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDrlkKSALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDP-------ELvndvlkvIKDLANEgMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|....
gi 581794297 225 FNRPKTEELRRFLN 238
Cdd:COG1117 241 FTNPKDKRTEDYIT 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
7.50e-64 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 203.26 E-value: 7.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSG 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLNVI 240
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEI 248
|
.
gi 581794297 241 N 241
Cdd:PRK09452 249 N 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
2.52e-62 |
|
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: 197.58 E-value: 2.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFN----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMI-NALEIP--TEGTVYVNGKTYTSKDKKSQ 73
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 74 IEVR-KQSGMVFQ----SYNlfPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLT---HVKDQRPHALSGGQQQR 145
Cdd:COG0444 81 RKIRgREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 146 VAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 581794297 225 FNRPK 229
Cdd:COG0444 239 FENPR 243
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-236 |
6.23e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 198.79 E-value: 6.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 7 IHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS-GMVFQ 85
Cdd:COG4175 33 ILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKKmSMVFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 86 SYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPT 165
Cdd:COG4175 113 HFALLPHRTVLENVAFGL-EIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 166 SALDP----ELVNDVLKVIKDLaneGMTMVIVTHE----MRFAkevsNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRF 236
Cdd:COG4175 192 SALDPlirrEMQDELLELQAKL---KKTIVFITHDldeaLRLG----DRIAIMKDGRIVQIGTPEEILTNPANDYVADF 263
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-201 |
8.54e-62 |
|
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: 193.42 E-value: 8.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND----VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQS-GMVFQSYNLFPHKTALENVMEGLitvkKLK-KDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAM 154
Cdd:COG4181 88 RARHvGFVFQSFQLLPTLTALENVMLPL----ELAgRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAK 201
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-229 |
5.49e-61 |
|
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: 191.50 E-value: 5.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkKSQIEVRKQSG 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL--PPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLITVKKL---------KKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARAL 152
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-237 |
2.17e-60 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 193.78 E-value: 2.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkKSQIEVRKQSg 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQRDIC- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
5.89e-60 |
|
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: 197.05 E-value: 5.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF--NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIP----TEGTVYVNGKTYTskdKKSQI 74
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPhggrISGEVLLDGRDLL---ELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 EVRKQSGMVFQS--YNLFPHkTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARAL 152
Cdd:COG1123 80 LRGRRIGMVFQDpmTQLNPV-TVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-234 |
7.67e-60 |
|
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: 189.56 E-value: 7.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF--NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGktYTSKDKKSQIEVRKQ 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQS-YNLFPHKTALENV---MEGLitvkKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVEDDVafgLENL----GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFNRPktEELR 234
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQV--ELLK 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-241 |
1.11e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 191.84 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYtskdkkSQIEVR-KQS 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV------SRLHARdRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLiTV----KKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGL-TVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRR 235
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLE 235
|
....*.
gi 581794297 236 FLNVIN 241
Cdd:PRK10851 236 FMGEVN 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.50e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.95 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqIEVRKQSG 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP---PEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPhktalENVMEGLITVKKLKKDEA-RGKSLELLEKVGLTH-VKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG4619 78 YVPQEPALWG-----GTVRDNLPFPFQLRERKFdRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-233 |
3.13e-59 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 187.56 E-value: 3.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQS 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR---ELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKKL-----KKDEArgKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYPHLGLfgrpsAEDRE--AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFnrpkTEEL 233
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL----TPEL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
4.26e-59 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 184.52 E-value: 4.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYtskdKKSQIEVRKQSG 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMeglitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
2.58e-58 |
|
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: 185.24 E-value: 2.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdKKSQIeVRKqs 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-PPHRI-ARL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMV--FQSYNLFPHKTALENVM------------EGLITVKKLKKDE--ARGKSLELLEKVGLTHVKDQRPHALSGGQQQ 144
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLvaaharlgrgllAALLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 145 RVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*.
gi 581794297 224 MFNRPK 229
Cdd:COG0411 240 VRADPR 245
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-210 |
2.67e-58 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 183.59 E-value: 2.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 4 LNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTY-TSKDKKSQIEVRKQSGM 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETpPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VFQSYNLFPHKTALENVMEGLITVKKLKKDEaRGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEK-REKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKeVSNNIVFI 210
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-215 |
4.61e-58 |
|
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: 183.22 E-value: 4.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
4.62e-58 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 183.22 E-value: 4.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFN-DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQ 79
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLE-VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGM 214
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
4.46e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 181.83 E-value: 4.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkksqiEVRKQS 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNL---FPhKTALENVMEGLIT----VKKLKKdEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA 153
Cdd:COG1121 78 GYVPQRAEVdwdFP-ITVRDVVLMGRYGrrglFRRPSR-ADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEqGAPEEMFNRPKTEEL 233
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLSRA 234
|
..
gi 581794297 234 RR 235
Cdd:COG1121 235 YG 236
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-237 |
4.75e-56 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 182.74 E-value: 4.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV-RKQSGMVFQSYNLFPHKTA 95
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 176 VLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:TIGR01186 168 MQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
3.30e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 177.96 E-value: 3.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKKSQIEVRKQ 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-IKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYN--LFPhKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:PRK13639 80 VGIVFQNPDdqLFA-PTVEEDVAFGPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-166 |
2.12e-54 |
|
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: 171.68 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFPHKTAL 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS---LRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 97 ENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQR----PHALSGGQQQRVAIARALAMNPKVMLFDEPTS 166
Cdd:pfam00005 78 ENLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-237 |
6.54e-54 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 173.29 E-value: 6.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEViKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTS-KDKKSQIevrkqs 80
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlPPEKRDI------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVI-VTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-228 |
1.26e-52 |
|
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: 173.75 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS-GMVFQSYNLFPHKTALEN 98
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRiGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 99 VMEGLitvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLK 178
Cdd:COG4148 98 LLYGR---KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 179 VIKDLANE-GMTMVIVTHEMRfakEV---SNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:COG4148 175 YLERLRDElDIPILYVSHSLD---EVarlADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
2.28e-52 |
|
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: 169.15 E-value: 2.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkKSQIEVRKQSG 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKvgLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
2.39e-52 |
|
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: 166.65 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQSGM 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE---ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VFQsynlfphktalenvmeglitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
2.79e-52 |
|
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: 168.74 E-value: 2.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKKSQIE-VRKQ 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGRAIPyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLITVKKlKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-200 |
2.58e-51 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 165.29 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKKSQIEVRKQSGMVFQSYN--L 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP-LDYSRKGLLERRQRVGLVFQDPDdqL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FpHKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALD 169
Cdd:TIGR01166 82 F-AADVDQDVAFGPLNLG-LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 581794297 170 PELVNDVLKVIKDLANEGMTMVIVTHEMRFA 200
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-229 |
1.15e-50 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 167.99 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 19 GIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQ----SYNlfPHKT 94
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQdpyaSLN--PRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENVMEGLITVKKLKKDEARGKSLELLEKVGL--THVkDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:COG4608 114 VGDIIAEPLRIHGLASKAERRERVAELLELVGLrpEHA-DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 173 VNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:COG4608 193 QAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-241 |
2.91e-50 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 166.90 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 32 LIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSGMVFQSYNLFPHKTALENVMEGLiTVKKLKK 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQSYALFPHMTVEENVAFGL-KMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 112 DEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTM 190
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 581794297 191 VIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLNVIN 241
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEIN 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-197 |
5.17e-50 |
|
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: 162.70 E-value: 5.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskdkkSQIEVRKQSGM 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK--------PLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VFQSYNL---FPhKTALENVMEGLIT----VKKLKKDEARgKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:cd03235 73 VPQRRSIdrdFP-ISVRDVVLMGLYGhkglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDL 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-241 |
6.11e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 167.32 E-value: 6.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskDKKSQIEVRKQS 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-----DLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 161 FDEPTSALDPELVNDV-LKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLNV 239
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
..
gi 581794297 240 IN 241
Cdd:PRK11607 253 VN 254
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-229 |
9.46e-50 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 166.74 E-value: 9.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskdKKSQIEVRKQS- 80
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK------RMNDVPPAERGv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGL-KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 161 FDEPTSALDPEL-VN---DVLKVIKDLaneGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:PRK11000 157 LDEPLSNLDAALrVQmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-219 |
1.09e-49 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 162.08 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEqGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS-GMVFQSYNLFPHKTALEN 98
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKiGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 99 VMEGLitvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLK 178
Cdd:cd03297 96 LAFGL---KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 581794297 179 VIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03297 173 ELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-216 |
3.59e-49 |
|
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: 160.12 E-value: 3.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 6 NIHKSFNDV-EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqievRKQSGMVF 84
Cdd:cd03226 4 NISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 85 QS--YNLFpHKTALENVMEGLitvkKLKkDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:cd03226 78 QDvdYQLF-TDSVREELLLGL----KEL-DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIG 216
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-237 |
4.66e-49 |
|
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: 168.32 E-value: 4.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQ----SYNl 89
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQdpfgSLS- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 fPHKTALENVMEGLITVK-KLKKDEARGKSLELLEKVGLTHVKDQR-PHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:COG4172 377 -PRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 168 LDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALL 526
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
5.07e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 162.50 E-value: 5.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIE-VRKQSGMVFQsynlFPHKTA 95
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKpLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENvmegliTVKK----------LKKDEARGKSLELLEKVGLTH-VKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEP 164
Cdd:PRK13634 99 FEE------TVEKdicfgpmnfgVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 165 TSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
5.31e-49 |
|
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: 170.79 E-value: 5.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhkSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVR 77
Cdd:COG2274 474 IELENV--SFrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFpHKTALENVMEG--LITVKKLkkdeargksLELLEKVGLTHVKDQRPH-----------ALSGGQQQ 144
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENITLGdpDATDEEI---------IEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 145 RVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANeGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEEM 224
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEEL 696
|
...
gi 581794297 225 FNR 227
Cdd:COG2274 697 LAR 699
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-219 |
7.23e-49 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 158.75 E-value: 7.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQSGM 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK---ELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VFQSynlfphktalenvmeglitvkklkkdeargkslelLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:cd03214 78 VPQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-237 |
7.95e-49 |
|
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: 160.53 E-value: 7.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksqIEVRKQS 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP----PHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVF--QSYNLFPHKTALENVMEGLITVKKLKKDEARgksLE--------LLEKvglthvKDQRPHALSGGQQQRVAIAR 150
Cdd:COG0410 79 GIGYvpEGRRIFPSLTVEENLLLGAYARRDRAEVRAD---LErvyelfprLKER------RRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 151 ALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPkt 230
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP-- 227
|
....*..
gi 581794297 231 EELRRFL 237
Cdd:COG0410 228 EVREAYL 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-235 |
5.11e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 159.87 E-value: 5.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVE------VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGktYTSKDKKSQI 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 EVRKQSGMVFQSynlfPHKTALENVMEGLITVKK----LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIAR 150
Cdd:PRK13633 82 DIRNKAGMVFQN----PDNQIVATIVEEDVAFGPenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 151 ALAMNPKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFnrPK 229
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KE 234
|
....*.
gi 581794297 230 TEELRR 235
Cdd:PRK13633 235 VEMMKK 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-239 |
6.75e-48 |
|
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: 157.69 E-value: 6.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkKSQIEVRKQSGM 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VFQSYNLFPHKTALENVMEGLITVKKLKK---DEArgksLELLEKvgLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRkipDEI----YELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMfnrpKTEELRRFLN 238
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
.
gi 581794297 239 V 239
Cdd:TIGR03410 230 V 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-224 |
8.33e-48 |
|
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: 157.15 E-value: 8.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkKSQIEVRKQSG 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENV-MEGLItvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:cd03265 77 IVFQDLSVDDELTGWENLyIHARL--YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.11e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 158.62 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVE--VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRK 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK---EIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMVFQSY-NLFPHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVEDDIAFGLEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVI-VTHEMRFAKEVSNNIVFIHEGMIgEQGAPEEMFN 226
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAILADKVIVFSEGKLI-AQGKPKEILN 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-219 |
3.39e-47 |
|
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: 155.34 E-value: 3.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 21 DLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSGMVFQSYNLFPHKTALENVM 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 101 EGLITVKKLKkDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVI 180
Cdd:cd03298 93 LGLSPGLKLT-AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 581794297 181 KDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-227 |
3.65e-47 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 158.32 E-value: 3.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 9 KSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqieVRKQSGMVFQSYN 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK----VRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 89 LFPHKTALENvMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSAL 168
Cdd:TIGR01188 77 VDEDLTGREN-LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 169 DPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRR 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
4.02e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 156.61 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL-----EIPTEGTVYVNGKTYTSKDkksQIEV 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD---VIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVMEGLITVKKLK-KDEARGKSLELLEKVGL-THVKDQ--RPHA-LSGGQQQRVAIARA 151
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKsKKELQERVRWALEKAQLwDEVKDRldAPAGkLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEgMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTE 231
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*.
gi 581794297 232 ELRRFL 237
Cdd:PRK14247 240 LTEKYV 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-232 |
4.20e-47 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 156.47 E-value: 4.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL-----EIPTEGTVYVNGKTYTSKdKKSQIE 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSP-RTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 VRKQSGMVFQSYNLFPHkTALENVMEGL-ITVKKLKK--DEARGKSLellekVGLT---HVKDqRPH----ALSGGQQQR 145
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPM-SIYENVVYGLrLKGIKDKQvlDEAVEKSL-----KGASiwdEVKD-RLHdsalGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 146 VAIARALAMNPKVMLFDEPTSALDP---ELVNDVLKVIKDlaneGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPE 222
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPisaGKIEETLLGLKD----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
250
....*....|
gi 581794297 223 EMFNRPKTEE 232
Cdd:PRK14239 233 QMFMNPKHKE 242
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-196 |
4.44e-47 |
|
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: 154.94 E-value: 4.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytsKDKKSQIEVRKQS 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE----PIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENvmegLITVKKLKKDEARGKSL-ELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG4133 78 AYLGHADGLKPELTVREN----LRFWAALYGLRADREAIdEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHE 196
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
5.53e-47 |
|
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: 153.69 E-value: 5.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFND--VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQ 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFpHKTALENVmeglitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVM 159
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVsNNIVFIHEG 213
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-195 |
2.08e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.02 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYT--SKDKksqi 74
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 evrkqsGMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAM 154
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 155 NPKVMLFDEPTSALDP-------ELVNDVlkvikdLANEGMTMVIVTH 195
Cdd:COG4525 152 DPRFLLMDEPFGALDAltreqmqELLLDV------WQRTGKGVFLITH 193
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-230 |
2.09e-46 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 157.70 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkksQIEVRKQ 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN------ELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 S-GMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK11650 77 DiAMVFQNYALYPHMSVRENMAYGL-KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIgEQ-GAPEEMFNRPKT 230
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQiGTPVEVYEKPAS 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-242 |
2.23e-46 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 155.17 E-value: 2.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL---EIPTEGTVYVNGKTYTSKDKKSQiEVR 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLAR-DIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 K---QSGMVFQSYNLFPHKTALENVMEGLI-------TVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVA 147
Cdd:PRK09984 83 KsraNTGYIFQQFNLVNRLSVLENVLIGALgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 148 IARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEmFN 226
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
|
250
....*....|....*.
gi 581794297 227 RPKTEELRRFLNVINE 242
Cdd:PRK09984 242 NERFDHLYRSINRVEE 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
4.20e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 155.63 E-value: 4.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFN-----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTV---YVN------------ 61
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 62 -------GKTYTSKDKKSQiEVRKQSGMVFQ--SYNLFpHKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKD 132
Cdd:PRK13651 83 vleklviQKTRFKKIKKIK-EIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMG-VSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 133 QR-PHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIH 211
Cdd:PRK13651 160 QRsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*
gi 581794297 212 EGMIGEQGAPEEMFN 226
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-197 |
4.22e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.80 E-value: 4.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKD-KKSQievrkQ 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQ-----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SG--MVFQSYNLFPHKTALENVM-------EGLITVKKLKKdEARgkslELLEKVGL-----THVKDqrphaLSGGQQQR 145
Cdd:COG1129 79 AGiaIIHQELNLVPNLSVAENIFlgreprrGGLIDWRAMRR-RAR----ELLARLGLdidpdTPVGD-----LSVAQQQL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 581794297 146 VAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRL 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-213 |
5.11e-46 |
|
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: 152.66 E-value: 5.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVE--VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTytskDKKSQIEVRKQ 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS----IRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMegLIT-VKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLR--FYArLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
5.60e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 154.88 E-value: 5.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsQI----EV 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR-RIgylpEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RkqsGmvfqsynLFPHKTalenVMEGLI---TVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA 153
Cdd:COG4152 80 R---G-------LYPKMK----VGEQLVylaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-233 |
6.86e-46 |
|
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: 152.70 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 6 NIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkKSQIEVRKQSGMVF- 84
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT----KLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 85 -QSYNLFPHKTALENVMEGLITVKKLKKdEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKK-EREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 164 PTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEEL 233
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKV 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
6.93e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 153.46 E-value: 6.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL-----EIPTEGTVYVNGKTYTSKDKKSqIEV 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP-IEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLE-LLEKVGL-THVKDQ---RPHALSGGQQQRVAIARA 151
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEgMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTE 231
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
....*.
gi 581794297 232 ELRRFL 237
Cdd:PRK14267 243 LTEKYV 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-232 |
7.38e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 154.44 E-value: 7.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQiEVRKQSGMVFQ--SYNLFpHKT 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS-DIRKKVGLVFQypEYQLF-EET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENVMEGLITVKkLKKDEARGKSLELLEKVGLTH--VKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:PRK13637 101 IEKDIAFGPINLG-LSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 173 VNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEE 232
Cdd:PRK13637 180 RDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
7.41e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 152.88 E-value: 7.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksqIEVRKQS 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMvfqSY-----NLFPHKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:COG1137 79 GI---GYlpqeaSIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-238 |
1.38e-45 |
|
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: 159.08 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKT----TLLRMINALEIPTEGTVYVNGKTYTSKDKKS 72
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 73 QIEVR-KQSGMVFQ----SYNlfPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVK---DQRPHALSGGQQQ 144
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 145 RVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250
....*....|....*
gi 581794297 224 MFNRPKTEELRRFLN 238
Cdd:COG4172 244 LFAAPQHPYTRKLLA 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-215 |
1.81e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 160.66 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQS-GMVFQSYNLFPHKTALENVmEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:PRK10535 84 RREHfGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMI 215
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-232 |
1.83e-45 |
|
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: 151.46 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIevrkqsgmVFQSYNLFPHKTAL 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV--------VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 97 ENVMEGLITV-KKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP----E 171
Cdd:TIGR01184 73 ENIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 172 LVNDVLKVIKDlanEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM-FNRPKTEE 232
Cdd:TIGR01184 153 LQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDRL 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
2.67e-45 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 150.51 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskdkKSQIEVRKQSG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-------PLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEgLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVY-LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-208 |
3.61e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 157.50 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkkSQIEVRKQS 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS--PRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVK--KLKKDEARGKSLELLEKVGLtHVK-DQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKggRLDRKAARARIRELSERYGL-DVDpDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIV 208
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVT 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
1.13e-44 |
|
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: 149.06 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND----VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKksqIEV 76
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEP---AEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHKTALENVmEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-229 |
1.23e-44 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 152.43 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQS-Y-NLFP 91
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYgSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL-THVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 170
Cdd:PRK11308 108 RKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 171 ELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:PRK11308 188 SVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.78e-44 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 146.80 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQS- 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR---DARRAGi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQsynlfphktalenvmeglitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVML 160
Cdd:cd03216 78 AMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-217 |
2.45e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 149.84 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQ----SYNlfP 91
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQdsisAVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLT-HVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 170
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 171 ELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGE 217
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-228 |
2.62e-44 |
|
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: 152.19 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS-GMVFQSYNLFPHKTALEN 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRiGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 99 VMEGLitvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLK 178
Cdd:TIGR02142 96 LRYGM---KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 581794297 179 VIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:TIGR02142 173 YLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-204 |
4.85e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 148.04 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND----VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQS-GMVFQSYNLFPHKTALENVMEGLITVKKlKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:PRK11629 85 RNQKlGFIYQFHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVS 204
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-235 |
4.94e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 149.40 E-value: 4.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdKKSQIEVRKQSGMVFQSY-NLFPHKTA 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWDVRRQVGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:PRK13635 100 QDDVAFGLEN-IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 176 VLKVIKDLANEGMTMVI-VTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFNRpkTEELRR 235
Cdd:PRK13635 179 VLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS--GHMLQE 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-219 |
5.77e-44 |
|
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: 146.98 E-value: 5.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSkdkksQIEVRKQSG 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVmegLITVKKLKKDEARGKslELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03268 76 ALIEAPGFYPNLTARENL---RLLARLLGIRKKRID--EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
1.30e-43 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 147.52 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 4 LNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVyVNGKTYTSkdkksqiEVRKQSGMV 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLA-------EAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 84 FQSYNLFPHKTALENVMEGLitvkklkKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 164 PTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIG 216
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
4.75e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 146.80 E-value: 4.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQS 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYN--LFPhKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK13647 82 GLVFQDPDdqVFS-STVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEE 232
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
5.13e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 146.92 E-value: 5.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKKSQIEVRKQ 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-IDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQS--YNLFPhKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:PRK13636 84 VGMVFQDpdNQLFS-ASVYQDVSFGAVNLK-LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFnrPKTEELR 234
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF--AEKEMLR 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
2.23e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 151.06 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQS 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFpHKTALENVMEGlitvkklkKDEARGKSL-ELLEKVGLTHVKDQRPH-----------ALSGGQQQRVAI 148
Cdd:COG4988 414 AWVPQNPYLF-AGTIRENLRLG--------RPDASDEELeAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 149 ARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEE 223
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-229 |
2.80e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 144.92 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIE-VRKQSGMVFQsynlFPHK 93
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 94 TALENVMEGLITVK----KLKKDEARGKSLELLEKVGLT-HVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSAL 168
Cdd:PRK13646 97 QLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 169 DPELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-226 |
3.16e-42 |
|
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: 143.69 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEG-TVYVNGKTYTSKDkksqI-EVRK 78
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED----VwELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMV---FQSYnLFPHKTALENVMEGL---ITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARAL 152
Cdd:COG1119 79 RIGLVspaLQLR-FPRDETVLDVVLSGFfdsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEG-MTMVIVTHemrFAKEVS---NNIVFIHEGMIGEQGAPEEMFN 226
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH---HVEEIPpgiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-223 |
7.31e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.99 E-value: 7.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAlEI-PTEGTVYVNGKTYTSkdkKSQIEVRKQ 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG-ELsPDSGEVRLNGRPLAD---WSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNL-FPHkTALENVMEGLITvkkLKKDEARGKSL--ELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA--- 153
Cdd:PRK13548 78 RAVLPQHSSLsFPF-TVEEVVAMGRAP---HGLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 154 ---MNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-219 |
1.67e-41 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 140.77 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhkSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievRKQSG 81
Cdd:TIGR01277 1 LALDKV--RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY-----QRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVMEGLITVKKLKKDEARgKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:TIGR01277 74 MLFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-242 |
4.11e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 143.07 E-value: 4.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 9 KSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYV-------------NGKTYTSKDKKSQIE 75
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheLITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 VRKQSGMVFQ--SYNLFphKTALE-NVMEGLITVKkLKKDEARGKSLELLEKVGLTH-VKDQRPHALSGGQQQRVAIARA 151
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLF--KDTIEkDIMFGPVALG-VKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK-- 229
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHii 270
|
250
....*....|....*.
gi 581794297 230 ---TEELRRFLNVINE 242
Cdd:PRK13631 271 nstSIQVPRVIQVIND 286
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-195 |
4.76e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 139.54 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLR-MINALE--IPTEGTVYVNGKTYTSKdkksQIEvR 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSpaFSASGEVLLNGRRLTAL----PAE-Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFPHKTALENVMEGLitVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 581794297 158 VMLFDEPTSALDPELVNDVLK-VIKDLANEGMTMVIVTH 195
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
5.75e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.62 E-value: 5.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhkSF---NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTSKDkksqie 75
Cdd:COG1132 340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLES------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 VRKQSGMVFQSYNLFpHKTALENVmeglitvkKLKKDEArgkSLELLEKV---------------GL-THVkDQRPHALS 139
Cdd:COG1132 412 LRRQIGVVPQDTFLF-SGTIRENI--------RYGRPDA---TDEEVEEAakaaqahefiealpdGYdTVV-GERGVNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 140 GGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEM---RFAkevsNNIVFIHEGMIG 216
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLstiRNA----DRILVLDDGRIV 553
|
....*..
gi 581794297 217 EQGAPEE 223
Cdd:COG1132 554 EQGTHEE 560
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
9.66e-41 |
|
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: 138.87 E-value: 9.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGeVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGktytSKDKKSQIEVRKQSG 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG----QDVLKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALEnVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03264 76 YLPQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-213 |
9.98e-41 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 139.08 E-value: 9.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFN----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEV 76
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQ-SGMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:NF038007 81 RRElIGYIFQSFNLIPHLSIFDNVALPLK-YRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEmRFAKEVSNNIVFIHEG 213
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-227 |
1.45e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 140.65 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 19 GIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIE-VRKQSGMVFQsynlFPH----- 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqIRKKVGLVFQ----FPEsqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTH-VKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 171
Cdd:PRK13649 101 ETVLKDVAFGPQNFG-VSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 172 LVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
2.09e-40 |
|
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: 145.68 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF--NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQ 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED---DLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFpHKTALENVmegLITVKKLKKDEARgkslELLEKVGLTHVKDQRPH-----------ALSGGQQQRVAI 148
Cdd:COG4987 411 IAVVPQRPHLF-DTTLRENL---RLARPDATDEELW----AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 149 ARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEE 223
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-226 |
3.20e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 138.18 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNI-------HKSFndvevikgiDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkKSQ 73
Cdd:PRK10771 1 MLKLTDItwlyhhlPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT----TTP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 74 IEVRKQSgMVFQSYNLFPHKTALENVMEGLITVKKLKkDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA 153
Cdd:PRK10771 68 PSRRPVS-MLFQENNLFSHLTVAQNIGLGLNPGLKLN-AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFN 226
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-237 |
3.52e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 139.46 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 6 NIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSK---DKKSQIEVRKQSGM 82
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRsifNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VFQSYNLFPhKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL-THVKDQ---RPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEgMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-241 |
3.80e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 142.48 E-value: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVR-KQSGMVFQSYNLFPHKTA 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:PRK10070 124 LDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 176 VL-KVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLNVIN 241
Cdd:PRK10070 203 MQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVD 269
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-223 |
5.97e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 138.32 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMInALEI-PTEGTVYVNGKTYTSKDKKsqiEVRKQ 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLL-TGELtPSSGEVRLNGRPLAAWSPW---ELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNL-FPHkTALENVMEGLI---TVKKLKKDEARgkslELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA-- 153
Cdd:COG4559 77 RAVLPQHSSLaFPF-TVEEVVALGRAphgSSAAQDRQIVR----EALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 154 -----MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-243 |
6.77e-40 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 143.79 E-value: 6.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEI--PTEGTV-----------YVN------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 62 -----GKTYTSK-------DKKSQIEVRKQSGMVFQ-SYNLFPHKTALENVMEGLITVkKLKKDEARGKSLELLEKVGLT 128
Cdd:TIGR03269 81 pcpvcGGTLEPEevdfwnlSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEI-GYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 129 HVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAKEVSNNI 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 581794297 208 VFIHEGMIGEQGAPEEMFNR--PKTEELRRFLNVINEE 243
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVfmEGVSEVEKECEVEVGE 277
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-237 |
1.10e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 137.49 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKT-YTSKD--KKSQIEVR 77
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlYFGKDifQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL---THVKDQRPHA-LSGGQQQRVAIARALA 153
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkeVYDRLNSPASqLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEgMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEEL 233
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....
gi 581794297 234 RRFL 237
Cdd:PRK14246 249 EKYV 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-237 |
1.36e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 137.61 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALE--IPT---EGTVYVNGKTYTSKDKKSqIEVRKQSGMVFQSYNLFP 91
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKNLYAPDVDP-VEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 hKTALENVMEGL-ITVKKLKKDEARGKSLEllEKVGLTHVKD---QRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:PRK14243 105 -KSIYDNIAYGArINGYKGDMDELVERSLR--QAALWDEVKDklkQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 168 LDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVSNNIVF---------IHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK14243 182 LDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTAFfnvelteggGRYGYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-229 |
2.69e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 137.27 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSK-DKKSQIEVRKQSGMVFQsynlFPH-----K 93
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKKLRKKVSLVFQ----FPEaqlfeN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 94 TALENVMEGLITVKkLKKDEARGKSLELLEKVGL-THVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:PRK13641 102 TVLKDVEFGPKNFG-FSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 173 VNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-208 |
1.81e-38 |
|
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: 133.33 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFN-------DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYV---NGKTYTSKDK 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 71 KSQI-EVRKQS-GMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLthvkDQR-----PHALSGGQQ 143
Cdd:COG4778 84 PREIlALRRRTiGYVSQFLRVIPRVSALDVVAEPLL-ERGVDREEARARARELLARLNL----PERlwdlpPATFSGGEQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 144 QRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIV 208
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-227 |
1.88e-38 |
|
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: 133.77 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFpHKT 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENV--------MEGLITVKKLKkdEARGKSLELLEkvGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTS 166
Cdd:cd03252 92 IRDNIaladpgmsMERVIEAAKLA--GAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 167 ALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:cd03252 168 ALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-225 |
2.59e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 134.86 E-value: 2.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIE-VRKQSGMVFQ--SYNLFpHKTAL 96
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQfpESQLF-EETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 97 ENVMEGLITVKkLKKDEARGKSLELLEKVGLT-HVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:PRK13643 104 KDVAFGPQNFG-IPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 581794297 176 VLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMF 225
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-228 |
6.13e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.77 E-value: 6.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 8 HKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQSGMVFQSY 87
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR---EVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 88 N--LFPhKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPT 165
Cdd:PRK13652 88 DdqIFS-PTVEQDIAFGPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 166 SALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-238 |
1.87e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 131.88 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFND---------VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKs 72
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 73 qieVRKQS-GMVFQSYN--LFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL--THVkDQRPHALSGGQQQRVA 147
Cdd:COG4167 84 ---YRCKHiRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlpEHA-NFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 148 IARALAMNPKVMLFDEPTSALDP----ELVNDVLKVIKDLaneGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMsvrsQIINLMLELQEKL---GISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*
gi 581794297 224 MFNRPKTEELRRFLN 238
Cdd:COG4167 237 VFANPQHEVTKRLIE 251
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-229 |
2.03e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 133.68 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQ----SYNlfPH 92
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQdplaSLN--PR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEGLITVK-KLKKDEARGKSLELLEKVGL-THVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 170
Cdd:PRK15079 115 MTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 171 ELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:PRK15079 195 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
7.99e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 129.22 E-value: 7.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTyTSKDKKSQIE-VRK 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD-ITRLKNREVPfLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMVFQSYNLFPHKTALENVMEGLItVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG-MIGEQG 219
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGhLHGGVG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
9.08e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 130.62 E-value: 9.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVE---VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdKKSQIEVR 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSY-NLFPHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMrfaKEV--SNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL---DEValSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
12-200 |
1.47e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 128.74 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS-GMVFQSYNLF 90
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHvGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 91 PHKTALENV-MEGLItvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALD 169
Cdd:PRK10584 101 PTLNALENVeLPALL--RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|..
gi 581794297 170 PELVNDVLKVIKDLANE-GMTMVIVTHEMRFA 200
Cdd:PRK10584 179 RQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
2.26e-36 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 132.27 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQS 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR---AASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNL---F-----------PHKTALEnvmeglitvkklKKDEARGKSLE-LLEKVGLTHVKDQRPHALSGGQQQR 145
Cdd:PRK09536 80 ASVPQDTSLsfeFdvrqvvemgrtPHRSRFD------------TWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 146 VAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMF 225
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
...
gi 581794297 226 NRP 228
Cdd:PRK09536 228 TAD 230
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-219 |
3.59e-36 |
|
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: 127.52 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqievrkqSG 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK-------IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVmegLITVKKLKKDEARgkSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:TIGR03740 74 SLIESPPLYENLTARENL---KVHTTLLGLPDSR--IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
5.65e-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: 133.00 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVE--VIK---GIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVN-GKTYTSKDKKSQI 74
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 E---VRKQSGMVFQSYNLFPHKTALENVMEGLITvkKLKKDEARGKSLELLEKVGLTHVK-----DQRPHALSGGQQQRV 146
Cdd:TIGR03269 359 GrgrAKRYIGILHQEYDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 147 AIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-235 |
7.30e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 128.38 E-value: 7.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 8 HKSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIP---TEGTVYVNGKTYTSKdkkSQIEVRKQS 80
Cdd:PRK13640 10 HVSFtypdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAK---TVWDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSY-NLFPHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:PRK13640 87 GIVFQNPdNQFVGATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAkEVSNNIVFIHEGMIGEQGAPEEMFnrPKTEELRR 235
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF--SKVEMLKE 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-227 |
2.08e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 125.81 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQS 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFpHKTALENVMEGLITVKKLKKDEARgKSLELLEKV-----GLTHVKDQRPHALSGGQQQRVAIARALAMN 155
Cdd:cd03253 78 GVVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAA-KAAQIHDKImrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANeGMTMVIVTHEMRfakEVSN--NIVFIHEGMIGEQGAPEEMFNR 227
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS---TIVNadKIIVLKDGRIVERGTHEELLAK 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
3.06e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 125.97 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK---TYTSKDKKSQIEVR 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvaTTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQsgmvfqsynlfphktalENVMEGLITVKKL--------------KKDEAR-GKSLELLEkvgLTHVKDQRPHALSGGQ 142
Cdd:COG4604 81 RQ-----------------ENHINSRLTVRELvafgrfpyskgrltAEDREIiDEAIAYLD---LEDLADRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 143 QQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAP 221
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
....*..
gi 581794297 222 EEMFNRP 228
Cdd:COG4604 221 EEIITPE 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
3.97e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 125.92 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL-----EIPTEGTV-YVNGKTYTSKDKKSQIe 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVeFFNQNIYERRVNLNRL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 76 vRKQSGMVFQSYNLFPhKTALENVMEGLITV---KKLKKD---EARGKSLELLEKVglTHVKDQRPHALSGGQQQRVAIA 149
Cdd:PRK14258 87 -RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEIDdivESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 150 RALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAKEVSNNIVFIH--EGMIG---EQGAPEE 223
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRIGqlvEFGLTKK 242
|
250
....*....|....
gi 581794297 224 MFNRPKTEELRRFL 237
Cdd:PRK14258 243 IFNSPHDSRTREYV 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-209 |
4.80e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 124.24 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVE--VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqIEVRKQ 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP---ADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFpHKTALENvmeglITVKKLKKDEARgkSLELLEKVGLTHVKDQRPH-----------ALSGGQQQRVAI 148
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDN-----ITLGAPLADDER--ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 149 ARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVSNNIVF 209
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVM 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-195 |
1.06e-34 |
|
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: 129.71 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFPhKT 94
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQIAWVPQHPFLFA-GT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENVMEGlitvkklKKDEARGKSLELLEKVGLTHVKDQRP-----------HALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:TIGR02857 412 IAENIRLA-------RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190
....*....|....*....|....*....|..
gi 581794297 164 PTSALDPELVNDVLKVIKDLAnEGMTMVIVTH 195
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALA-QGRTVLLVTH 515
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
1.12e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.81 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFN-----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK--TYTSKDKKSq 73
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvTKLPEYKRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 74 ievrKQSGMVFQ--SYNLFPHKTALENVM--------EGL-ITVKKLKKDEARG--KSLEL-LE-----KVGLthvkdqr 134
Cdd:COG1101 80 ----KYIGRVFQdpMMGTAPSMTIEENLAlayrrgkrRGLrRGLTKKRRELFREllATLGLgLEnrldtKVGL------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 135 phaLSGGQQQrvaiARALAM----NPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVF 209
Cdd:COG1101 149 ---LSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIM 221
|
....*.
gi 581794297 210 IHEGMI 215
Cdd:COG1101 222 MHEGRI 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-233 |
1.61e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 124.71 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND-VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGktYTSKDKKSQIEVRKQ 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQS-YNLFPHKTALENVMEGLITVKkLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLC-LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRfAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEEL 233
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
2.18e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.09 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQSGMVFQS-YNLFPHKTA 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE---KLRKHIGIVFQNpDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:PRK13648 102 KYDVAFGLEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 581794297 176 VLKVIKDL-ANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFN 226
Cdd:PRK13648 181 LLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-169 |
3.97e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 122.89 E-value: 3.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqievrkQS 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA--------ER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLiTVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
....*....
gi 581794297 161 FDEPTSALD 169
Cdd:PRK11248 152 LDEPFGALD 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-195 |
7.21e-34 |
|
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: 120.73 E-value: 7.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIP--TEGTVYVNGKtytskdKKSQIEVRKQSGMVFQSYNLFPH 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGR------PLDKRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMeglITVKklkkdeARGkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:cd03213 97 LTVRETLM---FAAK------LRG---------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180
....*....|....*....|...
gi 581794297 173 VNDVLKVIKDLANEGMTMVIVTH 195
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
7.27e-34 |
|
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: 121.56 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFN-DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQS 80
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPhKTALENVMEG--LITVKKLKKDEARGKSLELLEKV--GLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:cd03254 80 GVVLQDTFLFS-GTIMENIRLGrpNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLaNEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMF 225
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
1.62e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 126.33 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 4 LNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVyvngktytSKDKKSQIevrkqsGMV 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLRI------GYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 84 FQSYNLFPHKTALENVMEGLITVKKLKK--------------------------DEARGKSLE-----LLEKVGLTHVKD 132
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLDGDAELRALEAeleeleaklaepdedlerlaelqeefEALGGWEAEaraeeILSGLGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 133 QRP-HALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVN---DVLKvikdlaNEGMTMVIVTHEMRFAKEVSNNIV 208
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFLK------NYPGTVLVVSHDRYFLDRVATRIL 220
|
....*..
gi 581794297 209 FIHEGMI 215
Cdd:COG0488 221 ELDRGKL 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-209 |
2.09e-33 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 127.29 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhkSFN----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkksQI--- 74
Cdd:TIGR03375 464 IEFRNV--SFAypgqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR------QIdpa 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 EVRKQSGMVFQSYNLFpHKTALENvmeglITVKKLKKDEARgkSLELLEKVGLTHVKDQRPH-----------ALSGGQQ 143
Cdd:TIGR03375 536 DLRRNIGYVPQDPRLF-YGTLRDN-----IALGAPYADDEE--ILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQR 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 144 QRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEVSNNIVF 209
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLVDRIIVM 672
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-235 |
3.69e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 120.38 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 6 NIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQieVRKQSGMVFQ 85
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR--ARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 86 SYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPT 165
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 166 SALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNrpkTEELRR 235
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ---DEHVKR 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-237 |
4.59e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 125.20 E-value: 4.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTT----LLRMINAleiptEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQSYN--L 89
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNssL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALENVMEGL-ITVKKLKKDEARGKSLELLEKVGLTHVKDQR-PHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:PRK15134 376 NPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 168 LDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
5.55e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 121.45 E-value: 5.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqievRKQSG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALENVmegLITVK--KLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENL---LVFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-223 |
1.16e-32 |
|
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: 118.80 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHksFN-----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTSKDKKSQ 73
Cdd:cd03249 1 IEFKNVS--FRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 74 IevrkqsGMVFQSYNLFPhKTALENVMEGLITVKKLKKDEARGKS-----LELLEKVGLTHVKDqRPHALSGGQQQRVAI 148
Cdd:cd03249 79 I------GLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKAnihdfIMSLPDGYDTLVGE-RGSQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 149 ARALAMNPKVMLFDEPTSALDPE---LVNDVLkvikDLANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEE 223
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAEsekLVQEAL----DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-240 |
1.20e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 119.48 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKtEELRRFLNV 239
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFLDG 245
|
.
gi 581794297 240 I 240
Cdd:PRK11831 246 I 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-215 |
3.83e-32 |
|
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: 116.99 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLL----RMINALEIpTEGTVYVNGKtytskdKKSQIEVRKQSGMVFQSY 87
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisGRVEGGGT-TSGQILFNGQ------PRKPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 88 NLFPHKTALENV-MEGLITVKKLKKDEARGKSLE--LLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEP 164
Cdd:cd03234 91 ILLPGLTVRETLtYTAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 165 TSALDPELVNDVLKVIKDLANEGMTMVIVTHEMR---FakEVSNNIVFIHEGMI 215
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEI 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-197 |
4.08e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.79 E-value: 4.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 10 SFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTY-------TSKDKKSQIEVRKQSGM 82
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqrSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 vfqsyNLFPHKTALenvmeglitvKKLKKDeARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:NF040873 81 -----GRWARRGLW----------RRLTRD-DRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-238 |
4.12e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.51 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKT-TLLRMINALEIP----TEGTVYVNGKTYTSKDKKSQIEVR-KQSGMVFQS-- 86
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 YNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKdQR----PHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAA-KRltdyPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFLN 238
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-237 |
1.19e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.31 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIPTEGTVYVNGKTYTSKD--KKSQIEVRKQSG----MVFQS--YNLFP 91
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKLEFNGQDlqRISEKERRNLVGaevaMIFQDpmTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVK---DQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSAL 168
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 169 DPELVNDVLKVIKDLAN-EGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK---TEELRRFL 237
Cdd:PRK11022 185 DVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRhpyTQALLRAL 257
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
1.24e-31 |
|
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: 114.24 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhkSF----NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVR 77
Cdd:cd03246 1 LEVENV--SFrypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN---ELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFPhKTALENVmeglitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPK 157
Cdd:cd03246 76 DHVGYLPQDDELFS-GSIAENI--------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVsNNIVFIHEGMI 215
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-235 |
1.61e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.27 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYtskdkkSQIEVRKQS 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI------SMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 gmvfQSYNLFP--HKTAlenvmEGlITVKKL----------------KKDEARGKSLelLEKVGLTHVKDQRPHALSGGQ 142
Cdd:PRK11231 76 ----RRLALLPqhHLTP-----EG-ITVRELvaygrspwlslwgrlsAEDNARVNQA--MEQTRINHLADRRLTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 143 QQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPE 222
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
250
....*....|...
gi 581794297 223 EMFnrpkTEELRR 235
Cdd:PRK11231 224 EVM----TPGLLR 232
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-228 |
1.71e-31 |
|
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: 121.60 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFPhKTA 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA---VRRQLGVVLQNGRLMS-GSI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEG-LITVkklkkDEArgksLELLEKVGLTHVKDQRP---H--------ALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:TIGR03797 544 FENIAGGaPLTL-----DEA----WEAARMAGLAEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDE 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 164 PTSALD---PELVNDVLKVIKdlanegMTMVIVTHEMRFAKEVSNNIVFiHEGMIGEQGAPEEMFNRP 228
Cdd:TIGR03797 615 ATSALDnrtQAIVSESLERLK------VTRIVIAHRLSTIRNADRIYVL-DAGRVVQQGTYDELMARE 675
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-227 |
2.23e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.56 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF----------------------NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 59 YVNGKTytskdkKSQIEVrkqsGMVFQsynlfPHKTALENV-MEGLITvkKLKKDEARgkslELLEKV----GLTHVKDQ 133
Cdd:COG1134 84 EVNGRV------SALLEL----GAGFH-----PELTGRENIyLNGRLL--GLSRKEID----EKFDEIvefaELGDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 134 RPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|....
gi 581794297 214 MIGEQGAPEEMFNR 227
Cdd:COG1134 223 RLVMDGDPEEVIAA 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-195 |
2.78e-31 |
|
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: 120.16 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksQIEVRKQSGMVFQSYNLFpHKT 94
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD---QDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENVMEGlitvkklKKDEARGKSLELLEKVGLTHVKDQRPH-----------ALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:TIGR02868 425 VRENLRLA-------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....*.
gi 581794297 164 PTSALDP----ELVNDVLKvikdlANEGMTMVIVTH 195
Cdd:TIGR02868 498 PTEHLDAetadELLEDLLA-----ALSGRTVVLITH 528
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-228 |
1.32e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.93 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkKSQIEVRKqs 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIARM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMV--FQSYNLFPHKTALEN------------VMEGLITVKKLKK--DEARGKSLELLEKVGLTHVKDQRPHALSGGQQQ 144
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENllvaqhqqlktgLFSGLLKTPAFRRaeSEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 145 RVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*
gi 581794297 224 MFNRP 228
Cdd:PRK11300 241 IRNNP 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-224 |
1.70e-30 |
|
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: 113.09 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 10 SFNDV---------EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTSKDkksqieVR 77
Cdd:cd03251 2 EFKNVtfrypgdgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLAS------LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFpHKTALENVMEGlitvkklKKDEARGKSLELLEKVGLTHVKDQRPHA-----------LSGGQQQRV 146
Cdd:cd03251 76 RQIGLVSQDVFLF-NDTVAENIAYG-------RPGATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 147 AIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEM 224
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-232 |
6.46e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 112.41 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYtSKDKKSQIEVRKQS 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEE 232
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-237 |
6.81e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 6.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTY-TSKDKKSQiEVRKQSGMVFQS--YNL 89
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQ-ALRRDIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQR-PHALSGGQQQRVAIARALAMNPKVMLFDEPTSAL 168
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 169 DPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-224 |
8.70e-30 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 116.77 E-value: 8.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFpHKT 94
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW---LRRQMGVVLQENVLF-SRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENV--------MEGLITVKKLKKDEA------RGKSLELLEKVGlthvkdqrphALSGGQQQRVAIARALAMNPKVML 160
Cdd:TIGR01846 547 IRDNIalcnpgapFEHVIHAAKLAGAHDfiselpQGYNTEVGEKGA----------NLSGGQRQRIAIARALVGNPRILI 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEM 224
Cdd:TIGR01846 617 FDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-226 |
9.47e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.41 E-value: 9.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFN-----DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQ--I 74
Cdd:PRK13645 7 IILDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKevK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 EVRKQSGMVFQ--SYNLFpHKTALENVMEGLITVKKlKKDEARGKSLELLEKVGLTHVKDQR-PHALSGGQQQRVAIARA 151
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLF-QETIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFN 226
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-225 |
1.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.72 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSY-NLF 90
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN---LRRKIGMVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 91 PHKTALENVMEGLITvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 170
Cdd:PRK13642 95 VGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 171 ELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMF 225
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
2.27e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 114.76 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYT--SKDKKSQIEVRk 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArlTPAKAHQLGIY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 qsgMVFQSYNLFPHKTALENVMEGLItvkklKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK15439 90 ---LVPQEPLLFPNLSVKENILFGLP-----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-228 |
2.49e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.59 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFpH 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LHRQVALVGQEPVLF-S 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEGLitvKKLKKDEARGKSLEL--------LEKVGLTHVkDQRPHALSGGQQQRVAIARALAMNPKVMLFDEP 164
Cdd:TIGR00958 569 GSVRENIAYGL---TDTPDEEIMAAAKAAnahdfimeFPNGYDTEV-GEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 165 TSALDPElVNDVLKVIKDLAneGMTMVIVTHEMRFAkEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:TIGR00958 645 TSALDAE-CEQLLQESRSRA--SRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-224 |
3.08e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTSKdkksqiEVRKQSGMVFQSYNLFPH 92
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiQHYASK------EVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEG------LITVKKLKKDEARGKSLElleKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTS 166
Cdd:PRK10253 96 ITVQELVARGryphqpLFTRWRKEDEEAVTKAMQ---ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 167 ALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
3.48e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 114.50 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVrkQS 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--GI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKK------LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAM 154
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-215 |
4.74e-29 |
|
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: 107.52 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGmvfqsy 87
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragiayvpEDRKREG------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 88 nLFPHKTALENVmeglitvkklkkdeargkSLELLekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:cd03215 89 -LVLDLSVAENI------------------ALSSL---------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 168 LDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-219 |
5.21e-29 |
|
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: 107.40 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF--NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqiEVRKQ 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFphktalenvmeglitvkklkkdeargkSLELLEKVGLThvkdqrphaLSGGQQQRVAIARALAMNPKVM 159
Cdd:cd03247 77 ISVLNQRPYLF---------------------------DTTLRNNLGRR---------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRfAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
1.06e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.38 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVE--VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK---TYTSKDKKSQIEV 76
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiaDYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 rkqsgmVFQSYNLFPHkTALENvmegLITVKKLKKDEargKSLELLEKVGLTHVKDQ------------RPhaLSGGQQQ 144
Cdd:PRK11160 419 ------VSQRVHLFSA-TLRDN----LLLAAPNASDE---ALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 145 RVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRfAKEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQE 559
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-197 |
1.24e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 112.70 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEvrkqSG- 81
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA----AGv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 -MVFQSYNLFPHKTALENVMEGLITVKK--LKKDEARGKSLELLEKVGLthvkDQRPHA----LSGGQQQRVAIARALAM 154
Cdd:PRK11288 82 aIIYQELHLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGV----DIDPDTplkyLSIGQRQMVEIAKALAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-223 |
1.95e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.83 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLL-----RMINALEIptEGTVYVNGKTYTSKdkksqiEVRKQSGMVFQSYNL 89
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAK------EMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALE--NVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKD------QRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:TIGR00955 111 IPTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMR---FakEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
2.98e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.56 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIPT---EGTVYVNGKTYtskdKKSQIEVR 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL----QASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMV--FQSYNLFPHKTALENVMEG--LITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA 153
Cdd:PRK13549 80 ERAGIAiiHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-215 |
5.33e-28 |
|
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: 106.65 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 8 HKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTytskDKKSQIEVRKQSGMVFQSy 87
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKKFLRRIGVVFGQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 88 nlfphKTALE---NVMEGLITVK---KLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03267 103 -----KTQLWwdlPVIDSFYLLAaiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.12e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.99 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqievRKQSG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA----RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSYNLFPHKTALEN-VMEGLITVKKLKKDEARGKSLelLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSL--LEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-193 |
1.76e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.35 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskDKKSQIEVRKQS 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKvgLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190
....*....|....*....|....*....|...
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIV 193
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-215 |
1.92e-27 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 104.86 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFPh 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY---LHSKVSLVGQEPVLFA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEGLITVKKLKKDEARGKS-----LELLEKVGLTHVkDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:cd03248 102 RSLQDNIAYGLQSCSFECVKEAAQKAhahsfISELASGYDTEV-GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 168 LDPELVNDVLKVIKDlANEGMTMVIVTHEMRFAkEVSNNIVFIHEGMI 215
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-219 |
2.83e-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: 104.15 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTytskdkKSQIEVrkqsGMVFQsynlfPH 92
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLGL----GGGFN-----PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENV-MEGLItvKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 171
Cdd:cd03220 99 LTGRENIyLNGRL--LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 172 LVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-217 |
3.91e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGmvfqs 86
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIragiayvpEDRKGEG----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 ynLFPHKTALENVMegLITVKKLKK----DEARGKSL--ELLEKVGL-THVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:COG1129 341 --LVLDLSIRENIT--LASLDRLSRggllDRRRERALaeEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 160 LFDEPTSALDpelV---NDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG-MIGE 217
Cdd:COG1129 417 ILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGrIVGE 475
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
6.28e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVnGKTytskdkksqievrkqs 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET---------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 gmVFQSY------NLFPHKTALENVMEGLitvKKLKKDEARGksleLLEKVGLTHVKDQRP-HALSGGQQQRVAIARALA 153
Cdd:COG0488 378 --VKIGYfdqhqeELDPDKTVLDELRDGA---PGGTEQEVRG----YLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 154 MNPKVMLFDEPTSALDP---ELVNDVLKvikdlANEGmTMVIVTHEMRFAKEVSNNIVFIHEGMIGE 217
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIetlEALEEALD-----DFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-228 |
7.11e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.11 E-value: 7.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNnIHKSFNDVEVikGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS 80
Cdd:PRK11144 1 MLELN-FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 -GMVFQSYNLFPHKTALENVMEGLItvkklKKDEARGKSL-ELLekvGLTHVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK11144 78 iGYVFQDARLFPHYKVRGNLRYGMA-----KSMVAQFDKIvALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEM----RFAkevsNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLdeilRLA----DRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
1.47e-26 |
|
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: 106.83 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEiPT---EGTVYVNGktytSKDKKSQIEVR 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSG----SPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVF--QSYNLFPHKTALENVMEG-LITVK--KLKKDEARGKSLELLEKVGLTHVKDQRP-HALSGGQQQRVAIARA 151
Cdd:TIGR02633 76 ERAGIVIihQELTLVPELSVAENIFLGnEITLPggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-195 |
1.54e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.87 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIE-VRKQSGMvfqsynlf 90
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLGHRNAM-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 91 phKTALeNVMEGLITVKKLkKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 170
Cdd:PRK13539 85 --KPAL-TVAENLEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*
gi 581794297 171 ELVNDVLKVIKDLANEGMTMVIVTH 195
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATH 185
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-227 |
2.16e-26 |
|
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: 106.72 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTSKDkksqieVRKQSGMVFQSYNL 89
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLAS------LRRQVALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FpHKTALENVMEGlitvkklKKDEA-RGKSLELLEKVGLTHVKDQRPHA-----------LSGGQQQRVAIARALAMNPK 157
Cdd:TIGR02203 418 F-NDTIANNIAYG-------RTEQAdRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 158 VMLFDEPTSALDPE---LVNDVLkvikDLANEGMTMVIVTHEMRfAKEVSNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:TIGR02203 490 ILILDEATSALDNEserLVQAAL----ERLMQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-222 |
2.69e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.07 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMI--NALEIPTEGTVYVNGKTYTSKDkksqIEVRKQS 80
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELS----PDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 G--MVFQS---------YNLFphKTALENVMEGLITVKKLKKdEARgkslELLEKVGLTHVKDQRP--HALSGGQQQRVA 147
Cdd:COG0396 78 GifLAFQYpveipgvsvSNFL--RTALNARRGEELSAREFLK-LLK----EKMKELGLDEDFLDRYvnEGFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 148 IARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFI-HEGMIGEQGAPE 222
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVHVlVDGRIVKSGGKE 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-227 |
5.37e-26 |
|
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: 105.60 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKksqiEVRKQS-GMVFQSYNLFPhKT 94
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR----EELGRHiGYLPQDVELFD-GT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALENVmeglitvkklkkdeAR------GKSLELLEKVGL------------THVkDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:COG4618 422 IAENI--------------ARfgdadpEKVVAAAKLAGVhemilrlpdgydTRI-GEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-233 |
1.29e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.02 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKS---QIEVRKQ 79
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 S-----GMVFQ---SYNLFPHKTALenvmeGLITVkklkkdEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARA 151
Cdd:PRK10575 93 QlpaaeGMTVRelvAIGRYPWHGAL-----GRFGA------ADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKT 230
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
...
gi 581794297 231 EEL 233
Cdd:PRK10575 242 EQI 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-213 |
1.35e-25 |
|
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: 99.47 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLrmiNAL--EIP-TEGTVYVNGKT-YTSKdkKSQIevrkQSGmvfqsynlfp 91
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLL---SALlgELEkLSGSVSVPGSIaYVSQ--EPWI----QNG---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 hkTALENVMEGL----------ITVKKLKKDeargksLELLEKVGLTHVKDqRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03250 81 --TIRENILFGKpfdeeryekvIKACALEPD------LEILPDGDLTEIGE-KGINLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 581794297 162 DEPTSALDPELVNDVL-KVIKDLANEGMTMVIVTHEMRFAKEVsNNIVFIHEG 213
Cdd:cd03250 152 DDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
1.74e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.39 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVyvngkTYTSKDKK-------SQ 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-----HYRMRDGQlrdlyalSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 74 IE----VRKQSGMVFQS--YNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVK-DQRPHALSGGQQQRV 146
Cdd:PRK11701 81 AErrrlLRTEWGFVHQHprDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 147 AIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-229 |
1.88e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 100.29 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKT------YTSKDKKSQI 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 EVRKQSGMVFQSY--NLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVK-DQRPHALSGGQQQRVAIARA 151
Cdd:TIGR02323 83 LMRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQ 241
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-223 |
2.59e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLrmiNALE--IPTEGTVYVNGKTYTSKDKKSQievRKQSGMVFQSYNLFpHKTALE 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELRELDPESW---RKHLSWVGQNPQLP-HGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 98 NVMEG--LITVKKLKKDEARGKSLELLEKV--GLTH-VKDQRPhALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:PRK11174 442 NVLLGnpDASDEQLQQALENAWVSEFLPLLpqGLDTpIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 581794297 173 VNDVLKVIKDlANEGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEE 223
Cdd:PRK11174 521 EQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-229 |
2.79e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.78 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKT-TLLRMINALEipTEGTVYVNGKTYTSKDKKSQIEVRKQS------------ 80
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLE--QAGGLVQCDKMLLRRRSRQVIELSEQSaaqmrhvrgadm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQS--YNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVK---DQRPHALSGGQQQRVAIARALAMN 155
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPK 229
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-238 |
4.34e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.48 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSF---------NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK--TYTSKD 69
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 70 KKSQiEVRkqsgMVFQ--SYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGL--THVkDQRPHALSGGQQQR 145
Cdd:PRK15112 84 YRSQ-RIR----MIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlpDHA-SYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 146 VAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
250
....*....|....
gi 581794297 225 FNRPKTEELRRFLN 238
Cdd:PRK15112 238 LASPLHELTKRLIA 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-195 |
5.19e-25 |
|
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: 97.81 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskdkksqiEVRKQSGMVFQSYNLFPHKT 94
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-----------PLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 95 ALEN---VMEGLITVKKLKKDEARgKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 171
Cdd:TIGR01189 83 GLKPelsALENLHFWAAIHGGAQR-TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 581794297 172 LVNDVLKVIKDLANEGMTMVIVTH 195
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-221 |
5.73e-25 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 103.17 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskDKKSQIEVRKQS-GMVFQSYNLFPHKTALEN 98
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK-----DIETNLDAVRQSlGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 99 VMeGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLK 178
Cdd:TIGR01257 1024 IL-FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 581794297 179 VIKDLaNEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAP 221
Cdd:TIGR01257 1103 LLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-222 |
8.32e-25 |
|
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: 97.21 E-value: 8.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALE--IPTEGTVYVNGKTYTSKDkksqIEVRKQ 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLP----PEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SG--MVFQSYNLFP---HKTALENVMEGLitvkklkkdeargkslellekvglthvkdqrphalSGGQQQRVAIARALAM 154
Cdd:cd03217 77 LGifLAFQYPPEIPgvkNADFLRYVNEGF-----------------------------------SGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFI-HEGMIGEQGAPE 222
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVlYDGRIVKSGDKE 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-203 |
1.96e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkkSQIEVRKQS 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL---KPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPhktalENVMEGLITVKKLKKDEARGKSL-ELLEKVGL-THVKDQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK10247 84 SYCAQTPTLFG-----DTVYDNLIFPWQIRNQQPDPAIFlDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVI-VTH---EMRFAKEV 203
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHdkdEINHADKV 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-218 |
2.43e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.46 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVrkQS 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA--GI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVME--------GLITVKKLKKDEARgksleLLEKVGLTHVKDQRPHALSGGQQQRVAIARAL 152
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLgrefvnrfGRIDWKKMYAEADK-----LLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG-MIGEQ 218
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGqFIAER 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-195 |
2.67e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 10 SFNDVEV--------IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTvyvngktytskdkksqIEVRKQSG 81
Cdd:COG4178 364 ALEDLTLrtpdgrplLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR----------------IARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVF---QSYnlFPhktaLENVMEGLI---TVKKLKKDEARgkslELLEKVGLTHVKDQ------RPHALSGGQQQRVAIA 149
Cdd:COG4178 428 VLFlpqRPY--LP----LGTLREALLypaTAEAFSDAELR----EALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 581794297 150 RALAMNPKVMLFDEPTSALDPELVNDVLKVIKDlANEGMTMVIVTH 195
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
2.84e-24 |
|
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: 94.05 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSkdkksqievrkqsg 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 mvfqsynLFPHktalenvmeglitvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLF 161
Cdd:cd03221 67 -------YFEQ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 581794297 162 DEPTSALDPElvnDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:cd03221 95 DEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-228 |
4.46e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.26 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKT----TLLRMINALEIpTEGTVYVNGKTYTSKDKKSQIEVR-KQSGMVFQS- 86
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPEKELNKLRaEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 -YNLFPHKTALENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKdQR----PHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEAR-KRmkmyPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVI-VTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-195 |
1.25e-23 |
|
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: 94.10 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTytskdkksqieVRKQSGMVFQSYNLFPHKTA 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-----------LDFQRDSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 581794297 176 VLKVIKDLANEGMTMVIVTH 195
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-224 |
2.81e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 97.80 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQSGMVFQSYNLFPhKTA 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRET---FGKHIGYLPQDVELFP-GTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENV--MEGLITVKKLKKDEARGKSLELLEKV--GLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 171
Cdd:TIGR01842 409 AENIarFGENADPEKIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 581794297 172 LVNDVLKVIKDLANEGMTMVIVTHEMRfAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:TIGR01842 489 GEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-226 |
4.54e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.50 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLR-MINALEIPTEGTVYVNGKT-YTSkdkksqievrkQSGMVFQSynlfphkTALE 97
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVaYVP-----------QVSWIFNA-------TVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 98 NVMEGL----------ITVKKLKKDeargksLELLEKVGLTHVkDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:PLN03130 698 NILFGSpfdperyeraIDVTALQHD------LDLLPGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 168 LDPELVNDVL-KVIKDlANEGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEEMFN 226
Cdd:PLN03130 771 LDAHVGRQVFdKCIKD-ELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-200 |
2.43e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.63 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 19 GIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKtytskdkksqiEVRKQSGMVFQSYNLFPHK----- 93
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-----------PIRRQRDEYHQDLLYLGHQpgikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 94 --TALENV-----MEGLITvkklkkDEARgksLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTS 166
Cdd:PRK13538 88 elTALENLrfyqrLHGPGD------DEAL---WEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 581794297 167 ALDPELVNDVLKVIKDLANEGmTMVIVT--HEMRFA 200
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQG-GMVILTthQDLPVA 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-220 |
5.61e-22 |
|
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: 94.08 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 25 EQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTvyvngktYTSKDKKSQIeVRKQSGMVFQSYnlfphktaLENVMEGLI 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-------YDEEPSWDEV-LKRFRGTELQDY--------FKKLANGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 105 ------------------TVKKL--KKDEaRGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEP 164
Cdd:COG1245 161 kvahkpqyvdlipkvfkgTVRELleKVDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 165 TSALD-PELVNdVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHegmiGEQGA 220
Cdd:COG1245 240 SSYLDiYQRLN-VARLIRELAEEGKYVLVVEHDLAILDYLADYVHILY----GEPGV 291
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 |
1.34e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.30 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFN---------------------DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVY 59
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 60 VNGKTyTSKDKKsqiEVRKQSGMVF-QSYNLFPHKTALEnvmegliTVKKLKK-----DEARGKSL-ELLEKVGLTHVKD 132
Cdd:COG4586 81 VLGYV-PFKRRK---EFARRIGVVFgQRSQLWWDLPAID-------SFRLLKAiyripDAEYKKRLdELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 133 QRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIH 211
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVID 229
|
250
....*....|....*.
gi 581794297 212 EGMIGEQGAPEEMFNR 227
Cdd:COG4586 230 HGRIIYDGSLEELKER 245
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-237 |
2.08e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 89.37 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTtlLRMINALEI-P-----TEGTVYVNGKTYTSKDKKSqievrKQSGMVFQ- 85
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGIlPagvrqTAGRVLLDGKPVAPCALRG-----RKIATIMQn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 86 ---SYNlfPHKTALENVMEgliTVKKLKKDEARGKSLELLEKVGLTHVK---DQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:PRK10418 88 prsAFN--PLHTMHTHARE---TCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRPKTEELRRFL 237
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-227 |
2.43e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqieVRKQS 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFpHKTALENVMEGL--ITVKKLKKDEARGKSLELLEK--VGLTHVKDQRPHALSGGQQQRVAIARALAMNP 156
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIRVGRpdATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 157 KVMLFDEPTSALDPEL---VNDVLkvikDLANEGMTMVIVTHEM---RFAKEvsnnIVFIHEGMIGEQGAPEEMFNR 227
Cdd:PRK13657 491 PILILDEATSALDVETeakVKAAL----DELMKGRTTFIIAHRLstvRNADR----ILVFDNGRVVESGSFDELVAR 559
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-197 |
8.76e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.64 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 24 VEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTvyvngktYTSKDKKSQIeVRKQSGMVFQSYnlfphktaLENVMEGL 103
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-------YEEEPSWDEV-LKRFRGTELQNY--------FKKLYNGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 104 ITV-KK------------------LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEP 164
Cdd:PRK13409 160 IKVvHKpqyvdlipkvfkgkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 581794297 165 TSALD-PELVNdVLKVIKDLAnEGMTMVIVTHEM 197
Cdd:PRK13409 240 TSYLDiRQRLN-VARLIRELA-EGKYVLVVEHDL 271
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-227 |
3.13e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 89.03 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKS--FNDvEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQ 79
Cdd:TIGR01193 474 IVINDVSYSygYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH---TLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPhKTALENVMEGliTVKKLKKDEARgKSLEL------LEKVGLTHVKDQRPHA--LSGGQQQRVAIARA 151
Cdd:TIGR01193 550 INYLPQEPYIFS-GSILENLLLG--AKENVSQDEIW-AACEIaeikddIENMPLGYQTELSEEGssISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNdvlKVIKDLAN-EGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEK---KIVNNLLNlQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-210 |
5.01e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFN---DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNgKTYTSKDK-----KSQ 73
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-DSHNLKDInlkwwRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 74 IEVRKQSGMVFQS-------YNLFPHK--TALENVME----------------------------------GLITVKK-- 108
Cdd:PTZ00265 462 IGVVSQDPLLFSNsiknnikYSLYSLKdlEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsnELIEMRKny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 109 --LKKDEARGKSLELLEKVGLTHVKDQ-------RPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKV 179
Cdd:PTZ00265 542 qtIKDSEVVDVSKKVLIHDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|....*
gi 581794297 180 IKDL-ANEGMTMVIVTHEM---RFAkevsnNIVFI 210
Cdd:PTZ00265 622 INNLkGNENRITIIIAHRLstiRYA-----NTIFV 651
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-219 |
6.95e-20 |
|
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: 87.95 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 11 FNDV--------EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTskdkksQIEVRKQ 79
Cdd:COG5265 360 FENVsfgydperPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVT------QASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFpHKTALENVMEGLITVKKlkkDE----ARGKSL----ELLEK-----VGLTHVKdqrphaLSGGQQQRV 146
Cdd:COG5265 434 IGIVPQDTVLF-NDTIAYNIAYGRPDASE---EEveaaARAAQIhdfiESLPDgydtrVGERGLK------LSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 147 AIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHemRFAKEV-SNNIVFIHEGMIGEQG 219
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH--RLSTIVdADEILVLEAGRIVERG 574
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-227 |
9.20e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 9.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNG---KTYTSKDkksqieVRKQSGMVFQSYNLFpHK 93
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLAS------LRNQVALVSQNVHLF-ND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 94 TALENVM---EGLITVKKLKKDEARGKSLELLEKV--GLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSAL 168
Cdd:PRK11176 432 TIANNIAyarTEQYSREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 169 DPELVNDVLKVIKDLANEGMTMVIvTHEMRfAKEVSNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:PRK11176 512 DTESERAIQAALDELQKNRTSLVI-AHRLS-TIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-196 |
9.90e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 87.63 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 9 KSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLrmiNALEipteGTVYVNGKTYT--SKDKKSQIEVRKQSGMVFQS 86
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLL---NALA----GRIQGNNFTGTilANNRKPTKQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 YNLFPHKTALEN-VMEGLITV-KKLKKDEARGKSLELLEKVGLTH-----VKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:PLN03211 149 DILYPHLTVRETlVFCSLLRLpKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*..
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHE 196
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-197 |
1.25e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVyvngktytSKDKKSQIevrkqs 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRI------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVfqsynlfPHKTALENVMEglITVKK---LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:PRK09544 70 GYV-------PQKLYLDTTLP--LTVNRflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 581794297 158 VMLFDEPTSALDpelVNDVL---KVIKDLANE-GMTMVIVTHEM 197
Cdd:PRK09544 141 LLVLDEPTQGVD---VNGQValyDLIDQLRRElDCAVLMVSHDL 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-215 |
2.11e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksqIEVRKQSGMVF-----QSYN 88
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----PRERRRLGVAYipedrLGRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 89 LFPHKTALENVMEGLITVKK------LKKDEARGKSLELLEKVGlthVKDQRPHA----LSGGQQQRVAIARALAMNPKV 158
Cdd:COG3845 347 LVPDMSVAENLILGRYRRPPfsrggfLDRKAIRAFAEELIEEFD---VRTPGPDTparsLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-213 |
4.50e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEiptegtvyvngktytsKDKKSQIEVRkqsgmvFQSYNLFPHKTA 95
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL----------------KGTPVAGCVD------VPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVmeglitVKKLKKDEArgksLELLEKVGLTHVKD--QRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 173
Cdd:COG2401 103 IDAI------GRKGDFKDA----VELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 581794297 174 NDVLKVIKDLANE-GMTMVIVTHEMRFAKEVS-NNIVFIHEG 213
Cdd:COG2401 173 KRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-225 |
9.86e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.03 E-value: 9.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLlrmINAL--EIPTEGTvyvngktyTSKDKKSQIEVRKQSGMVFQSynlfphkTALE 97
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSL---ISAMlgELSHAET--------SSVVIRGSVAYVPQVSWIFNA-------TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 98 NVMEG----------LITVKKLKKDeargksLELLEKVGLTHVkDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:PLN03232 698 NILFGsdfeserywrAIDVTALQHD------LDLLPGRDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 168 LDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEEMF 225
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-217 |
1.27e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGMVfqsynlfP 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragimlcpEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HKTALENV---------MEGLITVKKLKKDEARgkslellEKVGLTHVK----DQRPHALSGGQQQRVAIARALAMNPKV 158
Cdd:PRK11288 345 VHSVADNInisarrhhlRAGCLINNRWEAENAD-------RFIRSLNIKtpsrEQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 159 MLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI-GE 217
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIaGE 477
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-213 |
1.92e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.63 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 4 LNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEvrKQSGMV 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 84 FQSYNLFPHKTALENVMEGLITVKKLKKDEAR--GKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-223 |
1.96e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksqIEVRKQSGMVFQSYNLFphktalenv 99
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD----IATRRRVGYMSQAFSLY--------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 100 meGLITVKK----------LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALD 169
Cdd:NF033858 352 --GELTVRQnlelharlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 170 PELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAkEVSNNIVFIHEGMIGEQGAPEE 223
Cdd:NF033858 430 PVARDMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-240 |
2.07e-18 |
|
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: 81.30 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 22 LSVEQG-----EVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIevrKQSGMVFQsynlfphktAL 96
Cdd:cd03237 15 LEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA---DYEGTVRD---------LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 97 ENVMEGLITVKKLKKdeargkslELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDV 176
Cdd:cd03237 83 SSITKDFYTHPYFKT--------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 177 LKVIKDLA-NEGMTMVIVTHEMRFAKEVSNN-IVFihEGMIGEQG---APEEMfnrpkTEELRRFLNVI 240
Cdd:cd03237 155 SKVIRRFAeNNEKTAFVVEHDIIMIDYLADRlIVF--EGEPSVNGvanPPQSL-----RSGMNRFLKNL 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-228 |
2.22e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.26 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMI-NALE---IPTEGTVYVNGKTYT--SKDKKSQIeVRKQSGMVFQ-- 85
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKdnwHVTADRFRWNGIDLLklSPRERRKI-IGREIAMIFQep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 86 SYNLFPHKTALENVMEGL--ITVK-------KLKKDEArgksLELLEKVGlthVKDQR------PHALSGGQQQRVAIAR 150
Cdd:COG4170 99 SSCLDPSAKIGDQLIEAIpsWTFKgkwwqrfKWRKKRA----IELLHRVG---IKDHKdimnsyPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 151 ALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-233 |
2.96e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 19 GIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIPTEGTVYVNGKTYTSKDKKSQIEVR-----KQS---GM-VFQSYNL 89
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSppfAMpVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALENVMEGLItvkklkkdeargksLELLEKVGLTHvKDQRP-HALSGGQQQRVAIARAL-----AMNP--KVMLF 161
Cdd:COG4138 93 HQPAGASSEAVEQLL--------------AQLAEALGLED-KLSRPlTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 162 DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM----RFAKEVsnniVFIHEGMIGEQGAPEEMFnrpkTEEL 233
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLnhtlRHADRV----WLLKQGKLVASGETAEVM----TPEN 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-214 |
6.48e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIPT---EGTVYVNGKTYTSKDkksqIEVR 77
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKD----IRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVF--QSYNLFPHKTALENVMEGLITVKK--LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALA 153
Cdd:NF040905 76 EALGIVIihQELALIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 154 MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGM 214
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-192 |
7.44e-18 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 78.84 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 4 LNNIH----KSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeipTEGTVYVNGK-TYTSKDKKSQIEV-R 77
Cdd:cd03233 6 WRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYNGIPYKEFAEKyP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQSYNLFPHKTalenVMEGLITVKKLKKDE-ARGkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNP 156
Cdd:cd03233 83 GEIIYVSEEDVHFPTLT----VRETLDFALRCKGNEfVRG---------------------ISGGERKRVSIAEALVSRA 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 581794297 157 KVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVI 192
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFV 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
1.36e-17 |
|
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: 79.33 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 23 SVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGtvyvngkTYTSKDKKSQIeVRKQSGMVFQSYnlfphktaLENVMEG 102
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFDDPPDWDEI-LDEFRGSELQNY--------FTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 103 LITVKK-------------------LKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:cd03236 86 DVKVIVkpqyvdlipkavkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 581794297 164 PTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNI 207
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-221 |
2.64e-17 |
|
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: 77.53 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTT----LLRMINaleiPTEGTVYVNG---KTYTSKDKKSQIEVRKQSGMVFQS-- 86
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGvdiSKIGLHDLRSRISIIPQDPVLFSGti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 -YNLFPHKT--------ALENVMEGLITVKKLKKDEARgkslelLEKVGLThvkdqrphaLSGGQQQRVAIARALAMNPK 157
Cdd:cd03244 95 rSNLDPFGEysdeelwqALERVGLKEFVESLPGGLDTV------VEEGGEN---------LSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDlANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAP 221
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-224 |
3.41e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.39 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSG--KTTLLRMINAleiPTEGTVYVNGKTYTSKDKKSQIEVRKQ 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALENVMEGLitvkKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVM 159
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*L----DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-224 |
3.53e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.33 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMInALEIP---------TEGTVYVNGKTYTSKDKKSQIEVRK------QS 80
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL-AGDLTgggaprgarVTGDVTLNGEPLAAIDAPRLARLRAvlpqaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNL-----FPHKTAlenvmEGLITVkklkkdEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAM- 154
Cdd:PRK13547 95 AFAFSAREIvllgrYPHARR-----AGALTH------RDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 155 --------NPKVMLFDEPTSALDPELVNDVLKVIKDLANE-GMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-224 |
8.00e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSqievRKQSGMVF-----QSYNL 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALENVMEGLITVKKLKKDEARGKSLelLEK------VGLTHVkDQRPHALSGGQQQRVAIARALAMNPKVMLFDE 163
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRRGFWIKPARENAV--LERyrralnIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 164 PTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-217 |
9.78e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGMVF---- 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangivyisEDRKRDGLVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 85 -QSYNLfphkTALENVMEGLITVKKLKKDEARGKSLELLE-KvglTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:PRK10762 348 kENMSL----TALRYFSRAGGSLKHADEQQAVSDFIRLFNiK---TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 163 EPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI-GE 217
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsGE 476
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-227 |
1.02e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFND--VEVIKGidlSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK-TYtskdkKSQIEVR 77
Cdd:PRK13409 340 LVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKiSY-----KPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSGMVFQsyNLFPHKTALENVMEglitvkklkkdeargKSlELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPK 157
Cdd:PRK13409 412 DYDGTVED--LLRSITDDLGSSYY---------------KS-EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 158 VMLFDEPTSALDPELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAKEVSNN-IVFIHE-GMIGEQGAPEEM---FNR 227
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDIYMIDYISDRlMVFEGEpGKHGHASGPMDMregMNR 549
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-195 |
1.80e-16 |
|
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: 74.11 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 10 SFNDVEV--------IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL--------EIPT-EGTVYVNGKTYtskdkks 72
Cdd:cd03223 2 ELENLSLatpdgrvlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEgEDLLFLPQRPY------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 73 qievrkqsgmvfqsynlFPhktalenvmeglitvkklkkdeaRGkSLellekvglthvKDQ--RP--HALSGGQQQRVAI 148
Cdd:cd03223 75 -----------------LP-----------------------LG-TL-----------REQliYPwdDVLSGGEQQRLAF 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 581794297 149 ARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDlanEGMTMVIVTH 195
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-208 |
1.84e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.07 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAlEIP------------------------TEG 56
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlddgriiyeqdlivarlqqdpprnVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 57 TVYvngkTYTSKDKKSQIEVRKQ----SGMVFQSY---NLfphkTALENVMEGLitvkklkkDEARGKSLE-----LLEK 124
Cdd:PRK11147 82 TVY----DFVAEGIEEQAEYLKRyhdiSHLVETDPsekNL----NELAKLQEQL--------DHHNLWQLEnrineVLAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 125 VGLThvKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANegmTMVIVTHEMRFAKEVS 204
Cdd:PRK11147 146 LGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMA 220
|
....
gi 581794297 205 NNIV 208
Cdd:PRK11147 221 TRIV 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
10-219 |
2.67e-16 |
|
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: 73.90 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 10 SFNDVEV--IKGIDLSVEQGEVVTLIGRSGSGKTTLLrminaLEIptegtVYVNGKTYTSKDKKsqievrkqsgmvfqsy 87
Cdd:cd03238 2 TVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEG-----LYASGKARLISFLP---------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 88 nLFPHKTalenvmegLITVKKLKkdeargksleLLEKVGLTHVKDQRPHA-LSGGQQQRVAIARALAMNPK--VMLFDEP 164
Cdd:cd03238 56 -KFSRNK--------LIFIDQLQ----------FLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 165 TSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMiGEQG 219
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS-GKSG 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-195 |
2.70e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.53 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKG-----IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksQIEV 76
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN---REAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 77 RKQSGMVFQSYNLFPHktalenvmegLITVKKLKKDE-ARgkslELLEKVGLTH---VKDQR--PHALSGGQQQRVAIAR 150
Cdd:COG4615 405 RQLFSAVFSDFHLFDR----------LLGLDGEADPArAR----ELLERLELDHkvsVEDGRfsTTDLSQGQRKRLALLV 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 581794297 151 ALAMNPKVMLFDEPTSALDP--------ELvndvlkvIKDLANEGMTMVIVTH 195
Cdd:COG4615 471 ALLEDRPILVFDEWAADQDPefrrvfytEL-------LPELKARGKTVIAISH 516
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-225 |
3.32e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 22 LSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQSynlFPhkTALENVME 101
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWS---FP--VLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 102 ----GLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVL 177
Cdd:PRK15056 103 mgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 581794297 178 KVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIhEGMIGEQGAPEEMF 225
Cdd:PRK15056 183 SLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTF 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-217 |
4.80e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 13 DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkkSQIEVRKQsGMVFQSYN---- 88
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR---SPLDAVKK-GMAYITESrrdn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 89 -LFPHKTALENV-------------MEGLITVKKLKKDEARGKSLELLEkvglTHVKDQRPHALSGGQQQRVAIARALAM 154
Cdd:PRK09700 351 gFFPNFSIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLALK----CHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGE 217
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-227 |
6.20e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK-TYTSKdkksQIEVRKQSgmvFQSYNLFPHKTA 95
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvAYVPQ----QAWIQNDS---LRENILFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 lENVMEGLITVKKLKKDeargksLELLEKVGLTHVKDQRPHaLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVND 175
Cdd:TIGR00957 727 -EKYYQQVLEACALLPD------LEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 176 VLKVIkdLANEGM----TMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:TIGR00957 799 IFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-213 |
6.61e-16 |
|
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: 76.40 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMI-NALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGMVfqsynlf 90
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIragiamvpEDRKRHGIV------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 91 PHKTALENvmeglITVKKLKKDEARGKSLE------LLEKVGLTHVKDQRPH----ALSGGQQQRVAIARALAMNPKVML 160
Cdd:TIGR02633 352 PILGVGKN-----ITLSVLKSFCFKMRIDAaaelqiIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-199 |
6.97e-16 |
|
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: 73.90 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQS 80
Cdd:cd03290 1 VQVTNGYFSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITVKKLKKDEARGKSLEllEKVGLTHVKDQ-----RPHALSGGQQQRVAIARALAMN 155
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQ--PDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLK--VIKDLANEGMTMVIVTHEMRF 199
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-227 |
8.77e-16 |
|
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: 75.98 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 6 NIHKSFND--VEVIKGidlSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGK-TYtskdkKSQIEVRKQSGM 82
Cdd:COG1245 346 DLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKiSY-----KPQYISPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 83 VfqsynlfphKTALENVMEGLITVKKLKkdeargksLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFD 162
Cdd:COG1245 418 V---------EEFLRSANTDDFGSSYYK--------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581794297 163 EPTSALDPELVNDVLKVIKDLA-NEGMTMVIVTHEMRFAKEVSNNI-VFihEGMIGEQG---APEEM---FNR 227
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLIDYISDRLmVF--EGEPGVHGhasGPMDMregMNR 551
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-207 |
1.81e-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: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVnGKTYtskdkksqievrkQSG 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSY-NLFPHKTALENVMEGLITVKKLKKD-EARGkslelleKVGLTHVK--DQ--RPHALSGGQQQRVAIARALAMN 155
Cdd:TIGR03719 389 YVDQSRdALDPNKTVWEEISGGLDIIKLGKREiPSRA-------YVGRFNFKgsDQqkKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 581794297 156 PKVMLFDEPTSALDPELVNDVLKVIKDLAneGMTMVIvTHEMRFAKEVSNNI 207
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVVI-SHDRWFLDRIATHI 510
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-211 |
2.10e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.14 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMIN---ALEIpTEGTVYVNGKTYTSKDKksqiEVR 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpAYKI-LEGDILFKGESILDLEP----EER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 KQSG--MVFQsynlFPHKTALENVMEGLITV-----KKLKKDEARGKSL-----ELLEKVGLTHVKDQR--PHALSGGQQ 143
Cdd:CHL00131 82 AHLGifLAFQ----YPIEIPGVSNADFLRLAynskrKFQGLPELDPLEFleiinEKLKLVGMDPSFLSRnvNEGFSGGEK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 144 QRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNivFIH 211
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPD--YVH 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-228 |
3.92e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.30 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeipTEGTVYVNGKTYTSKD----KKSQIEVRKQSG----MVFQ 85
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDidllRLSPRERRKLVGhnvsMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 86 SYN--LFPHKTALENVMEGL--ITVK-------KLKKDEArgksLELLEKVGLTHVKD---QRPHALSGGQQQRVAIARA 151
Cdd:PRK15093 97 EPQscLDPSERVGRQLMQNIpgWTYKgrwwqrfGWRKRRA----IELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDL-ANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFNRP 228
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-197 |
3.96e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 23 SVEQGEVVTLIGRSGSGKTTLLRMINALeIPTEGTVYVNGKTYTSKDKKSQIEVR----KQS----GM-VFQSYNLFPHK 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRaylsQQQtppfAMpVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 94 TALENVMEGLITvkklkkdeargkslELLEKVGLTHvKDQRP-HALSGGQQQRVAIARAL-----AMNP--KVMLFDEPT 165
Cdd:PRK03695 97 KTRTEAVASALN--------------EVAEALGLDD-KLGRSvNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|..
gi 581794297 166 SALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-225 |
4.59e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSF-NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSkdkKSQIEVRKQS 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS---LSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSynlfphKTALENVMEGLITvkkLKKDEARGKSLELLEKVGL------------THVKDQrPHALSGGQQQRVAI 148
Cdd:PRK10790 418 AMVQQD------PVVLADTFLANVT---LGRDISEEQVWQALETVQLaelarslpdglyTPLGEQ-GNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 149 ARALAMNPKVMLFDEPTSALDP---ELVNDVLKVIKdlanEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMF 225
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSgteQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-196 |
5.36e-15 |
|
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: 70.74 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIP--TEGTVYVNGktytskdKKSQIEVRKQSGMVFQSYNLFPH 92
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILING-------RPLDKNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTalenVMEGLITVKKLkkdeaRGKSLEllekvglthvkdqrphalsggQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:cd03232 94 LT----VREALRFSALL-----RGLSVE---------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|....
gi 581794297 173 VNDVLKVIKDLANEGMTMVIVTHE 196
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-213 |
9.18e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.41 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkksqievrkqsgmvfQSYNLFPhKTA 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSP----------------QTSWIMP-GTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGlitvkkLKKDEARGKSL----ELLEKVGLTHVKDQRPH-----ALSGGQQQRVAIARALAMNPKVMLFDEPTS 166
Cdd:TIGR01271 504 KDNIIFG------LSYDEYRYTSVikacQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 581794297 167 ALDPELVNDVLK--VIKDLANEgmTMVIVTHEMRFAKEvSNNIVFIHEG 213
Cdd:TIGR01271 578 HLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-219 |
2.35e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMI----NALEIPTEGTVYVNGKTytskdkKSQIEVRKQSGMVFQSYN- 88
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGIT------PEEIKKHYRGDVVYNAETd 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 89 -LFPHKTalenVMEGLITVKKLKKDEARGKSLELLEKV-----------GLTHVKDQRP-----HALSGGQQQRVAIARA 151
Cdd:TIGR00956 148 vHFPHLT----VGETLDFAARCKTPQNRPDGVSREEYAkhiadvymatyGLSHTRNTKVgndfvRGVSGGERKRVSIAEA 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVT--HEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-215 |
2.35e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 14 VEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMI-NALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGMVF 84
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAIaqgiamvpEDRKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 85 Q----------SYNLFPHKTALENVMEGLITVKKLKKDEARGKSLELleKVGlthvkdqrphALSGGQQQRVAIARALAM 154
Cdd:PRK13549 355 VmgvgknitlaALDRFTGGSRIDDAAELKTILESIQRLKVKTASPEL--AIA----------RLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-195 |
2.41e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 10 SFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVRKQSGmvfqsyNL 89
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP------GL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALENvmegLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALD 169
Cdd:PRK13543 94 KADLSTLEN----LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*.
gi 581794297 170 PELVNDVLKVIKDLANEGMTMVIVTH 195
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-171 |
2.79e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVnGKTYtskdkksqievrkQSG 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSY-NLFPHKTALENVMEGLITVkKLKKDE--ARG-------KSLELLEKVGLthvkdqrphaLSGGQQQRVAIARA 151
Cdd:PRK11819 391 YVDQSRdALDPNKTVWEEISGGLDII-KVGNREipSRAyvgrfnfKGGDQQKKVGV----------LSGGERNRLHLAKT 459
|
170 180
....*....|....*....|
gi 581794297 152 LAMNPKVMLFDEPTSALDPE 171
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-196 |
3.36e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDkksQIEVRKQSGMVFQSYNLFPHktalenv 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ---PEDYRKLFSAVFTDFHLFDQ------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 100 megLITVKKLKKDEARGKS-LELLEKVGLTHVKDQR--PHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP----EL 172
Cdd:PRK10522 412 ---LLGPEGKPANPALVEKwLERLKMAHKLELEDGRisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrrEF 488
|
170 180
....*....|....*....|....
gi 581794297 173 VNDVLKVIKDLaneGMTMVIVTHE 196
Cdd:PRK10522 489 YQVLLPLLQEM---GKTIFAISHD 509
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-207 |
4.71e-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: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFN-DVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeiptegtvyvngktytskDKKSQIEVRKQS- 80
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------------------DKDFNGEARPQPg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 ---GMVFQSYNLFPHKTALENVMEGLITVKKLKKD-------------------EARGKSLELLEKVGLTHV-------- 130
Cdd:TIGR03719 68 ikvGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRfneisakyaepdadfdklaAEQAELQEIIDAADAWDLdsqleiam 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 131 -------KDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANegmTMVIVTHEMRFAKEV 203
Cdd:TIGR03719 148 dalrcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNV 224
|
....
gi 581794297 204 SNNI 207
Cdd:TIGR03719 225 AGWI 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-221 |
4.92e-14 |
|
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: 68.59 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqiEVRKQSGMVFQSYNLFPH-- 92
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE---DLRSSLTIIPQDPTLFSGti 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEglitvkklKKDEARGKSLELLEKvGLThvkdqrphaLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 172
Cdd:cd03369 99 RSNLDPFDE--------YSDEEIYGALRVSEG-GLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 581794297 173 VNDVLKVIKDLANeGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAP 221
Cdd:cd03369 161 DALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-197 |
7.58e-14 |
|
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: 70.81 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 22 LSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKsqievrkqsgmVFQSYNLFPHKTALENVME 101
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-----------VHQNMGYCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 102 G---LITVKKLkkdeaRGKSLELLEKV--------GLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 170
Cdd:TIGR01257 2029 GrehLYLYARL-----RGVPAEEIEKVanwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180
....*....|....*....|....*..
gi 581794297 171 ELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-196 |
2.57e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLrmiNALE------IPTEGTVYVNGKTYTSKDKKSqievrkqSGMVFQSYNL 89
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAervttgVITGGDRLVNGRPLDSSFQRS-------IGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTalenVMEGLI---------TVKKLKKDEARGKSLELLEkvgLTHVKDqrphALSG--------GQQQRVAIARAL 152
Cdd:TIGR00956 848 LPTST----VRESLRfsaylrqpkSVSKSEKMEYVEEVIKLLE---MESYAD----AVVGvpgeglnvEQRKRLTIGVEL 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 581794297 153 AMNPKVMLF-DEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHE 196
Cdd:TIGR00956 917 VAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-213 |
3.67e-13 |
|
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: 67.19 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKdkksqievrkqsgmvfQSYNLFPhKTA 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS----------------QFSWIMP-GTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 LENVMEGlitvkkLKKDEARGKSL----ELLEKVGLTHVKDQRPHA-----LSGGQQQRVAIARALAMNPKVMLFDEPTS 166
Cdd:cd03291 115 KENIIFG------VSYDEYRYKSVvkacQLEEDITKFPEKDNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 581794297 167 ALDPELVNDVLK--VIKDLANEgmTMVIVTHEMRFAKEvSNNIVFIHEG 213
Cdd:cd03291 189 YLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
4.56e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYtskdKKSQIEVRKQS 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTALENVMEGLITvkklkKDEARGKSlELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDIHF-----SPGAVGIT-ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHE 196
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-228 |
1.73e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.27 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTskdkKSQIEV-RKQS 80
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSwRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 GMVFQSYNLFPHKTAlENVmeglitvkKLKKDEARGKSLEllEKVGLTHVKD--------------QRPHALSGGQQQRV 146
Cdd:PRK10789 392 AVVSQTPFLFSDTVA-NNI--------ALGRPDATQQEIE--HVARLASVHDdilrlpqgydtevgERGVMLSGGQKQRI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 147 AIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLAnEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEMFN 226
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQ 538
|
..
gi 581794297 227 RP 228
Cdd:PRK10789 539 QS 540
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-197 |
2.04e-12 |
|
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: 65.26 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTL----LRMINaleipTEGTVYVNGktyTSKDKKSQIEVRKQSGMVFQSYNLFP 91
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDG---VSWNSVPLQKWRKAFGVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HktaleNVMEGLITVKKLKKDEArgksLELLEKVGLTHVKDQRP-----------HALSGGQQQRVAIARALAMNPKVML 160
Cdd:cd03289 91 G-----TFRKNLDPYGKWSDEEI----WKVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDlANEGMTMVIVTHEM 197
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-217 |
2.05e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 3 QLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLR-MINALEiPTEGTVYVNGKtytskdkksqIEVrkqsg 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHCGTK----------LEV----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 MVFQSY--NLFPHKTALENVMEGlitvkklKKD-EARGKSLELL---------EKVGLTHVKdqrphALSGGQQQRVAIA 149
Cdd:PRK11147 385 AYFDQHraELDPEKTVMDNLAEG-------KQEvMVNGRPRHVLgylqdflfhPKRAMTPVK-----ALSGGERNRLLLA 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 150 RALAMNPKVMLFDEPTSALDPElvndVLKVIKDL-ANEGMTMVIVTHEMRFA-KEVSNNIVFIHEGMIGE 217
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVE----TLELLEELlDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGR 518
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-236 |
2.55e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGktytskdkksqievrkQSGMVFQSYNLFPHKTALENV 99
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------------SAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 100 -MEGLITvkKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLK 178
Cdd:PRK13545 107 eLKGLMM--GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581794297 179 VIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEM----------FNRPKTEELRRF 236
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVvdhydeflkkYNQMSVEERKDF 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-181 |
3.88e-12 |
|
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: 65.70 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALeIPTEGTVYVNGKTYTSKDKKSQievRKQSGMVFQSYNLFPHkta 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTW---RKAFGVIPQKVFIFSG--- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 96 lenvmegliTVKKLKKDEARGKSLEL---LEKVGLTHVKDQRP-----------HALSGGQQQRVAIARALAMNPKVMLF 161
Cdd:TIGR01271 1307 ---------TFRKNLDPYEQWSDEEIwkvAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180
....*....|....*....|
gi 581794297 162 DEPTSALDPELVNDVLKVIK 181
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLK 1397
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-195 |
4.91e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAlEIPtEGtvYVNGKTYTSKDKKS--QI-EVRK 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHP-QG--YSNDLTLFGRRRGSgeTIwDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSGMVFQSYNL-FPHKTALENV-MEGL---ITVKKLKKDEARGKSLELLEKVGLTHVKDQRP-HALSGGQQQRVAIARAL 152
Cdd:PRK10938 337 HIGYVSSSLHLdYRVSTSVRNViLSGFfdsIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRAL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 581794297 153 AMNPKVMLFDEPTSALDPelVND--VLKVIKDLANEGMTMVI-VTH 195
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDP--LNRqlVRRFVDVLISEGETQLLfVSH 460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-224 |
5.41e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTS---KDKKSQIEVRKQSGMVFQS---YNL 89
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiglHDLRFKITIIPQDPVLFSGslrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 90 FPHKTALEnvmEGLITVKKLkkdeARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALD 169
Cdd:TIGR00957 1381 DPFSQYSD---EEVWWALEL----AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 170 PELVNDVLKVIKDlANEGMTMVIVTHEMRFAKEVSNNIVfIHEGMIGEQGAPEEM 224
Cdd:TIGR00957 1454 LETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIV-LDKGEVAEFGAPSNL 1506
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-196 |
2.84e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEipTEGtvYVNGKTYTSKDKKSQIEVRKQSGMVFQSYNLFP 91
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HKTalenVMEGLI------TVKKLKKDEARGKSLELLEKVGLTHVKDQ---RP--HALSGGQQQRVAIARALAMNPKVML 160
Cdd:PLN03140 967 QVT----VRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190
....*....|....*....|....*....|....*.
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHE 196
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-226 |
4.25e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 137 ALSGGQQQRVAIARALAMNPKVMLFDEPTSALDP---ELVNDVLKVIKDLANEgmTMVIVTHEMRFAKEVSNNIVFIHEG 213
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIASIKRSDKIVVFNNPD 1435
|
90
....*....|....*..
gi 581794297 214 MIGE----QGAPEEMFN 226
Cdd:PTZ00265 1436 RTGSfvqaHGTHEELLS 1452
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
8.48e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 21 DLSVEQGEVVTLIGRSGSGKTTLLRminALEipTEGTVYvNGKTYTSKDKKSQIEVRKQSGMV---FQSYN---LFPH-- 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAR---ALA--GELPLL-SGERQSQFSHITRLSFEQLQKLVsdeWQRNNtdmLSPGed 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 ---KTALENVMEGLitvkklkKDEARgkSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALD 169
Cdd:PRK10938 97 dtgRTTAEIIQDEV-------KDPAR--CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190
....*....|....*....|....*....|
gi 581794297 170 PELVNDVLKVIKDLANEGMTMVIVTHemRF 199
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLN--RF 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-240 |
8.68e-11 |
|
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: 59.12 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 24 VEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQievrkqsgmvfqsynlfphktalenvmegl 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID------------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 104 itvkklkkdeargkslellekvglthvkdqrphaLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDL 183
Cdd:cd03222 72 ----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 184 ANEGM-TMVIVTHEMRFAKEVSnNIVFIHEGMIGEQGapeeMFNRPKT--EELRRFLNVI 240
Cdd:cd03222 118 SEEGKkTALVVEHDLAVLDYLS-DRIHVFEGEPGVYG----IASQPKGtrEGINRFLRGY 172
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-223 |
9.21e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLR-MINALEiPTEGTVYVNGKT---YTSKDKKSQIEVR 77
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELE-PDSGTVKWSENAnigYYAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 kqsgmvfqsynlfphktalENVMEGLITVKKLKKDE--ARGKSLELLekVGLTHVKdQRPHALSGGQQQRVAIARALAMN 155
Cdd:PRK15064 399 -------------------LTLFDWMSQWRQEGDDEqaVRGTLGRLL--FSQDDIK-KSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 156 PKVMLFDEPTSALDPELV---NDVLKVIkdlanEGmTMVIVTHEMRFAKEVSNNIVFI-HEGMIGEQGAPEE 223
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIeslNMALEKY-----EG-TLIFVSHDREFVSSLATRIIEItPDGVVDFSGTYEE 522
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-219 |
9.46e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALE--IPTEGTVYVNGKTYTSKDKksqiEVRK 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSP----EDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 79 QSG--MVFQ-------SYNLFPHKTALEnvmegliTVKKLKKDEA--RGKSLELLE-KVGLTHVKD---QRP--HALSGG 141
Cdd:PRK09580 77 GEGifMAFQypveipgVSNQFFLQTALN-------AVRSYRGQEPldRFDFQDLMEeKIALLKMPEdllTRSvnVGFSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 142 QQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFI-HEGMIGEQG 219
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVlYQGRIVKSG 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-199 |
9.90e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKsfNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGtvyvngktytskdkksqiEVRKQS 80
Cdd:PRK11819 9 MNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------------EARPAP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 ----GMVFQSYNLFPHKTALENVMEGLITVKKLKKD---------EARGKSLELLEKVG-------------LTHVKDQR 134
Cdd:PRK11819 69 gikvGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRfneiyaayaEPDADFDALAAEQGelqeiidaadawdLDSQLEIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 135 PHAL------------SGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANegmTMVIVTHEMRF 199
Cdd:PRK11819 149 MDALrcppwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTHDRYF 222
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-223 |
3.58e-10 |
|
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: 59.64 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 119 LELLEKVGLTHVKDQRP-HALSGGQQQRVAIARAL---AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVT 194
Cdd:TIGR00630 810 LQTLCDVGLGYIRLGQPaTTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
|
90 100 110
....*....|....*....|....*....|....*
gi 581794297 195 HEMRFAKeVSNNIVFI------HEGMIGEQGAPEE 223
Cdd:TIGR00630 890 HNLDVIK-TADYIIDLgpeggdGGGTVVASGTPEE 923
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-234 |
5.02e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLR--MINALE-IPTEGTVY-----VNGKTYT------S 67
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDgIPKNCQILhveqeVVGDDTTalqcvlN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 68 KDKKSQIEVRKQSGMVFQSYNLFPHKTALENVMEGLITVKK---LKKDEARGKSLELLEK-----------VGLTHVKD- 132
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKdavSQRLEEIYKRLELIDAytaearaasilAGLSFTPEm 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 133 --QRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFI 210
Cdd:PLN03073 338 qvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
250 260
....*....|....*....|....
gi 581794297 211 HEGMIGEQGAPEEMFNRPKTEELR 234
Cdd:PLN03073 415 HGQKLVTYKGDYDTFERTREEQLK 438
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-227 |
6.97e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTllrMINALEIPTE---GTVYVNGKTYTskdKKSQIEVRKQSGMVFQSYNLFph 92
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSS---MLNALFRIVElekGRIMIDDCDVA---KFGLTDLRRVLSIIPQSPVLF-- 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 ktalenvmEGLITVKKLKKDEARGKSL-ELLEKVGLTHVKDQRPHAL-----------SGGQQQRVAIARALAMNPKVML 160
Cdd:PLN03232 1323 --------SGTVRFNIDPFSEHNDADLwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581794297 161 FDEPTSALDPELVNDVLKVIKDlANEGMTMVIVTHEMRFAKEVsNNIVFIHEGMIGEQGAPEEMFNR 227
Cdd:PLN03232 1395 LDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-195 |
7.02e-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: 55.84 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 26 QGEVVTLIGRSGSGKTTLLRMI-NALEIPTEGTVYVNGktytskdkksqievrkqsgmvfqsynlfphktalenvmegli 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 105 tvkklkkdearGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE-----LVNDVLKV 179
Cdd:smart00382 39 -----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRL 107
|
170
....*....|....*.
gi 581794297 180 IKDLANEGMTMVIVTH 195
Cdd:smart00382 108 LLLLKSEKNLTVILTT 123
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-240 |
8.41e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTLL----RMINAleipTEGTVYVNGKTYTSKDKKsqiEVRKQSGMVFQSYNLFp 91
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMVEV----CGGEIRVNGREIGAYGLR---ELRRQFSMIPQDPVLF- 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 92 HKTALENVMEGLitvkklkkdEArgKSLEL---LEKVGL-THVK------DQRphALSG------GQQQRVAIARA-LAM 154
Cdd:PTZ00243 1397 DGTVRQNVDPFL---------EA--SSAEVwaaLELVGLrERVAsesegiDSR--VLEGgsnysvGQRQLMCMARAlLKK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDlANEGMTMVIVTHEMRFAKEVSNNIVFIHeGMIGEQGAPEEMFNRPK----- 229
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQYDKIIVMDH-GAVAEMGSPRELVMNRQsifhs 1541
|
250
....*....|....*..
gi 581794297 230 ------TEELRRFLNVI 240
Cdd:PTZ00243 1542 mvealgRSEAKRFLQLV 1558
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-197 |
1.21e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 8 HKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLlrminALEI-------PTEGTVYVNGKTYTSKDKKSQI------ 74
Cdd:NF040905 267 HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL-----AMSVfgrsygrNISGTVFKDGKEVDVSTVSDAIdaglay 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 75 --EVRKQSGMVfqsynlfphktaLENVMEGLITVKKLKKDEARG--------------------KSLELLEKVGlthvkd 132
Cdd:NF040905 342 vtEDRKGYGLN------------LIDDIKRNITLANLGKVSRRGvideneeikvaeeyrkkmniKTPSVFQKVG------ 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581794297 133 qrphALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:NF040905 404 ----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-197 |
1.48e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 15 EVIKGIDLSVEQGEVVTLIGRSGSGKTTLLR-MINALEIpTEGTVYVngktytskdKKSQIEVRKQSGMV---FQSYNLF 90
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGRVWA---------ERSIAYVPQQAWIMnatVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 91 --PHKTA-LENVmeglITVKKLKKDEAR---GKSLELLEKvGLThvkdqrphaLSGGQQQRVAIARALAMNPKVMLFDEP 164
Cdd:PTZ00243 744 fdEEDAArLADA----VRVSQLEADLAQlggGLETEIGEK-GVN---------LSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190
....*....|....*....|....*....|...
gi 581794297 165 TSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:PTZ00243 810 LSALDAHVGERVVEECFLGALAGKTRVLATHQV 842
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-197 |
1.85e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQI--------EVRKQSGMV----- 83
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvtEERRSTGIYayldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 84 -FQSY--NLFPHKTALenvmeGLITVKKLKKD------EARGKSLELLEKVGlthvkdqrphALSGGQQQRVAIARALAM 154
Cdd:PRK10982 344 gFNSLisNIRNYKNKV-----GLLDNSRMKSDtqwvidSMRVKTPGHRTQIG----------SLSGGNQQKVIIGRWLLT 408
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 581794297 155 NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEM 197
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEM 451
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-238 |
9.52e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 20 IDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTytskdkkSQIEVrkqsgmvfqSYNLFPHKTALENV 99
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-------SVIAI---------SAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 100 mEGLITVKKLKKDEARGKSLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVNDVLKV 179
Cdd:PRK13546 107 -EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDK 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 180 IKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQGAPEEMFnrPKTEElrrFLN 238
Cdd:PRK13546 186 IYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYEA---FLN 239
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-201 |
2.20e-08 |
|
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: 53.39 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 119 LELLEKVGLTHVKDQRP-HALSGGQQQRVAIARALAM---NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVT 194
Cdd:cd03271 150 LQTLCDVGLGYIKLGQPaTTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIE 229
|
....*..
gi 581794297 195 HEMRFAK 201
Cdd:cd03271 230 HNLDVIK 236
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
71-198 |
6.83e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 71 KSQIEVRKQSGMVFQSY--NLFPHKTALENVMEGLitvkklkkdEARgksLELLEKVGLTHVKDQRPHA-LSGGQQQRVA 147
Cdd:PRK00635 419 KTFAEFQQMSLQELFIFlsQLPSKSLSIEEVLQGL---------KSR---LSILIDLGLPYLTPERALAtLSGGEQERTA 486
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 581794297 148 IARALA--MNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMR 198
Cdd:PRK00635 487 LAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ 539
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-210 |
1.04e-07 |
|
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: 50.68 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhKSFNDVEVIkgidlsvEQGEVVTLI-GRSGSGKTTLlrmINALEIPTEGTVYVNGKTYTSKDKKSQI-EVRKQ 79
Cdd:cd03240 4 LSIRNI-RSFHERSEI-------EFFSPLTLIvGQNGAGKTTI---IEALKYALTGELPPNSKGGAHDPKLIREgEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 80 SGMVFQSYNLFPHKTALE-NVMEGLITVKKlkkdearGKSLELLEkvglthvkdQRPHALSGGQQQ------RVAIARAL 152
Cdd:cd03240 73 VKLAFENANGKKYTITRSlAILENVIFCHQ-------GESNWPLL---------DMRGRCSGGEKVlasliiRLALAETF 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 153 AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANE--GMTMVIVTHEMRFaKEVSNNIVFI 210
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIEESLAEIIEERKSqkNFQLIVITHDEEL-VDAADHIYRV 195
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-237 |
1.50e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 119 LELLEKVGLTHVKDQRP-HALSGGQQQRVAIARAL---AMNPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVT 194
Cdd:PRK00635 790 IHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 581794297 195 HEMRFAKEVSNNIVFIHEGmiGEQG-------APEEMF--NRPKTEELRRFL 237
Cdd:PRK00635 870 HNMHVVKVADYVLELGPEG--GNLGgyllascSPEELIhlHTPTAKALRPYL 919
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-225 |
6.02e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.14 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTL----LRMINALEipteGTVYVNGKTYTS---KDKKSQIEVRKQSGMVFQS-- 86
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKlplHTLRSRLSIILQDPILFSGsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 -YNLFPHKTALENVMEGLITVKKLKKdeaRGKSLelleKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPT 165
Cdd:cd03288 112 rFNLDPECKCTDDRLWEALEIAQLKN---MVKSL----PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 166 SALDPELVNDVLKVIKDlANEGMTMVIVTHemRFAKEVSNNIVFI-HEGMIGEQGAPEEMF 225
Cdd:cd03288 185 ASIDMATENILQKVVMT-AFADRTVVTIAH--RVSTILDADLVLVlSRGILVECDTPENLL 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-195 |
6.97e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 34 GRSGSGKTTLLRMINALEIPTEGTVYVngktytskdKKSQIEVRKQSGMVFQSYNLfphKTALE-NVMEGLITVKKLKKd 112
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY---------KNCNINNIAKPYCTYIGHNL---GLKLEmTVFENLKFWSEIYN- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 113 eargkSLELLEKV----GLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVNDvLKVIKdlAN 185
Cdd:PRK13541 100 -----SAETLYAAihyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEnrdLLNN-LIVMK--AN 171
|
170
....*....|
gi 581794297 186 EGMTMVIVTH 195
Cdd:PRK13541 172 SGGIVLLSSH 181
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-195 |
7.92e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIhKSFNDVEVIkgiDLSveqGEVVTLIGRSGSGKTTLLR-------------------MINALEIPTEGTVY--V 60
Cdd:COG0419 5 LRLENF-RSYRDTETI---DFD---DGLNLIVGPNGAGKSTILEairyalygkarsrsklrsdLINVGSEEASVELEfeH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 61 NGKTYT-SKDKKSQIEVRKQSGmvfqsynlfphkTALENVMEGLITVKKLKKDEARGKSLE------LLEKVGLTHVKDQ 133
Cdd:COG0419 78 GGKRYRiERRQGEFAEFLEAKP------------SERKEALKRLLGLEIYEELKERLKELEealesaLEELAELQKLKQE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581794297 134 R---------PHALSGGQQQRVAIARALAmnpkvMLFDepTSALDPELVNDVLKVIKDLAnegmtmvIVTH 195
Cdd:COG0419 146 IlaqlsgldpIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-194 |
8.54e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 8.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 119 LELLEKVGLTHVK-DQRPHALSGGQQQRVAIARALAMNPK--VMLFDEPTSALDPELVNDVLKVIKDLANEGMTmVIVT 194
Cdd:PRK00635 1368 LTFIDKVGLSYITlGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNT-VIAT 1445
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-173 |
1.13e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 19 GIDLSVEqgevVTLIGRSGSGKTTLLRMINALEIPTEGTVYvngktytsKDKKSQIEVRKQ---SGMVFQSYNLFPHKTA 95
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVRMAVFSQhhvDGLDLSSNPLLYMMRC 598
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581794297 96 LENVMEglitvKKLKKDeargkslelLEKVGLT-HVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 173
Cdd:PLN03073 599 FPGVPE-----QKLRAH---------LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-193 |
1.26e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVR---- 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRiaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 78 -----KqsgmvfqsyNLFPHKTALENV-----MEGLitvkklKKDEARGKSLELLEKVGLTHVKDqRPHA-LSGGQQQRV 146
Cdd:NF033858 82 pqglgK---------NLYPTLSVFENLdffgrLFGQ------DAAERRRRIDELLRATGLAPFAD-RPAGkLSGGMKQKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 147 AIARALAMNPKVMLFDEPTSALDP-------ELVNDVLKvikdlANEGMTmVIV 193
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMS-VLV 193
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-196 |
1.45e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 17 IKGIDLSVEQGEVVTLIGRSGSGKTTL----------LRMINAL---------EIPT------EG---TVYVNGKTyTSK 68
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLsayarqflgQMDKpdvdsiEGlspAIAIDQKT-TSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 69 DKKSQIevrkqsGMVFQSYNLFphktALENVMEGLITvkklkkdeargkSLELLEKVGLTHVK-DQRPHALSGGQQQRVA 147
Cdd:cd03270 90 NPRSTV------GTVTEIYDYL----RLLFARVGIRE------------RLGFLVDVGLGYLTlSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 148 IARALAMNPKVML--FDEPTSAL---DPELVNDVLKVIKDLANegmTMVIVTHE 196
Cdd:cd03270 148 LATQIGSGLTGVLyvLDEPSIGLhprDNDRLIETLKRLRDLGN---TVLVVEHD 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-217 |
2.78e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 23 SVEQGEVVTLIGRSGSGKTTLLRMInaleiptEGTVYVNGKTYTSKDKKSQIEVRKQSGMVFQSynlfphktALENVMEG 102
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQLAWVNQETPALPQP--------ALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 103 LITVKKLKKDEA--------------------------RGKSLELLEKVGLTHVKDQRP-HALSGGQQQRVAIARALAMN 155
Cdd:PRK10636 88 DREYRQLEAQLHdanerndghaiatihgkldaidawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581794297 156 PKVMLFDEPTSALDpelVNDVLKVIKDLANEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGE 217
Cdd:PRK10636 168 SDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-240 |
3.05e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.30 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 2 IQLNNiHKSFNDVEvikgIDLSveqGEVVTLIGRSGSGKTTLLRminALEIPTEGTvyvNGKTYTSKD---------KKS 72
Cdd:COG3593 6 IKIKN-FRSIKDLS----IELS---DDLTVLVGENNSGKSSILE---ALRLLLGPS---SSRKFDEEDfylgddpdlPEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 73 QIEVRKQS--GMVFQSYNLFPHKTALENVMEGLIT------------VKKLKKDEARGKSLEL---------LEKVGLTH 129
Cdd:COG3593 72 EIELTFGSllSRLLRLLLKEEDKEELEEALEELNEelkealkalnelLSEYLKELLDGLDLELelsldeledLLKSLSLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 130 VKDQRP---HALSGGQQQRVAIARALAM-------NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRF 199
Cdd:COG3593 152 IEDGKElplDRLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 581794297 200 AKEVS-NNIVFIHEgmiGEQGAPEEMFNRPKTEELRRFLNVI 240
Cdd:COG3593 232 LSEVPlENIRRLRR---DSGGTTSTKLIDLDDEDLRKLLRYL 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-224 |
4.60e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 16 VIKGIDLSVEQGEVVTLIGRSGSGKTTllrMINAL-EI--PTEGTVYVNGktyTSKDKKSQIEVRKQSGMVFQS------ 86
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSS---MLNALfRIveLERGRILIDG---CDISKFGLMDLRKVLGIIPQApvlfsg 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 87 ---YNLFP---HKTAleNVMEGLitVKKLKKDEARGKSLELLEKVGlthvkdQRPHALSGGQQQRVAIARALAMNPKVML 160
Cdd:PLN03130 1328 tvrFNLDPfneHNDA--DLWESL--ERAHLKDVIRRNSLGLDAEVS------EAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 161 FDEPTSALDpeLVNDVL--KVIKDlANEGMTMVIVTHEMRFAKEvSNNIVFIHEGMIGEQGAPEEM 224
Cdd:PLN03130 1398 LDEATAAVD--VRTDALiqKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-201 |
6.21e-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: 45.04 E-value: 6.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 136 HALSGGQQQRVAIARALAMNPK----VMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTHEMRFAK 201
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-195 |
6.84e-06 |
|
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: 46.67 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 12 NDVeVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINAL--------EIPTEGTV-YVNGKTYTSKDK-KSQIevrkqsg 81
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLfYVPQRPYMTLGTlRDQI------- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 82 mvfqsynLFPHktalenvmegliTVKKLKKDEARGKSLE-LLEKVGLTH----------VKDQRpHALSGGQQQRVAIAR 150
Cdd:TIGR00954 536 -------IYPD------------SSEDMKRRGLSDKDLEqILDNVQLTHilereggwsaVQDWM-DVLSGGEKQRIAMAR 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 581794297 151 ALAMNPKVMLFDEPTSALDPELVNDVLKVIKDLaneGMTMVIVTH 195
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
103-195 |
1.70e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 103 LITVKKLKKDEARGKSLELLEKVGLTHVKDQRP---HALSGGQQQ---RVAIARALAMNPKVMLFDEPTSALDPELVNDV 176
Cdd:pfam13304 199 LSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpaFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRL 278
|
90
....*....|....*....
gi 581794297 177 LKVIKDLANEGMTMVIVTH 195
Cdd:pfam13304 279 LELLKELSRNGAQLILTTH 297
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
119-197 |
2.69e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 119 LELLEKVGLTHVK-DQrpHA--LSGGQQQRVAIARALAM---NPKVMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVI 192
Cdd:COG0178 807 LQTLQDVGLGYIKlGQ--PAttLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVV 884
|
....*
gi 581794297 193 VTHEM 197
Cdd:COG0178 885 IEHNL 889
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
93-201 |
1.57e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 93 KTALENVMEGLITVKKLKKdeargkSLELLEKVGLTHVK-DQRPHALSGGQQQRVAIARALAMNPK---VMLFDEPTSAL 168
Cdd:PRK00635 1660 QTPIEEVAETFPFLKKIQK------PLQALIDNGLGYLPlGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSL 1733
|
90 100 110
....*....|....*....|....*....|...
gi 581794297 169 DPELVNDVLKVIKDLANEGMTMVIVTHEMRFAK 201
Cdd:PRK00635 1734 DNQQKSALLVQLRTLVSLGHSVIYIDHDPALLK 1766
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-215 |
1.93e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 1 MIQLNNIHKSFNDVEVIKGIDLSVEQGEVVTLIGRSGSGKTTLLRMINALEIPTEGTVYVNGKTYTSKDKKSQIEVrkqs 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEF---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 81 gmvfqsynLFPHKTALENVMeglitvkKLKKDEARGKSLELLEKVGLTHVKDQRPHA-LSGGQQQRVAIARALAMNPKVM 159
Cdd:PRK10636 388 --------LRADESPLQHLA-------RLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581794297 160 LFDEPTSALDPELVNDVLKVIKDLanEGmTMVIVTHEMRFAKEVSNNIVFIHEGMI 215
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
119-195 |
2.76e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 119 LELLEKVGLTHVK-DQRPHALSGGQQQRVAIARALAMNPK---VMLFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVT 194
Cdd:PRK00349 811 LQTLVDVGLGYIKlGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIE 890
|
.
gi 581794297 195 H 195
Cdd:PRK00349 891 H 891
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
145-203 |
3.84e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 145 RVAIARALAMNPKVMLFDEPTSALDPelvnDVLKVIKDLANE-GMTMVIVTHEMRFAKEV 203
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDI----NTIRWLEDVLNErNSTMIIISHDRHFLNSV 218
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
103-194 |
1.06e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.17 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 103 LITVKKLKKDE--------ARGKSLELLEKVG-----------------LTHVKD---QRPHALSGGQQQRVAIARALAM 154
Cdd:cd03272 96 LRRTIGLKKDEyfldkknvTKNDVMNLLESAGfsrsnpyyivpqgkinsLTNMKQdeqQEMQQLSGGQKSLVALALIFAI 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 581794297 155 N---PKVM-LFDEPTSALDPELVNDVLKVIKDLANEgmTMVIVT 194
Cdd:cd03272 176 QkcdPAPFyLFDEIDAALDAQYRTAVANMIKELSDG--AQFITT 217
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-50 |
1.87e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 581794297 2 IQLNNIhKSFNDVEvikgIDLSvEQGEVVTLIGRSGSGKTTLLRMINAL 50
Cdd:COG3950 6 LTIENF-RGFEDLE----IDFD-NPPRLTVLVGENGSGKTTLLEAIALA 48
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
6-56 |
2.04e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 581794297 6 NIHKSFNDVEVIKGIDLsveQGEVVTLIGRSGSGKTTLLRMInALEIPTEG 56
Cdd:COG5635 162 NLLERIESLKRLELLEA---KKKRLLILGEPGSGKTTLLRYL-ALELAERY 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
88-219 |
2.17e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 88 NLFPHKTALENVMEGLITVKKLKkdeargksLELLEKVGLTHVKDQRPHALSGGQQQRVAIARALAMNPKVMLFDEPTSA 167
Cdd:PLN03140 295 DLFMKATAMEGVKSSLITDYTLK--------ILGLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTG 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 581794297 168 LDPELVNDVLKVIKDLA--NEGMTMVIVTHEMRFAKEVSNNIVFIHEGMIGEQG 219
Cdd:PLN03140 367 LDSSTTYQIVKCLQQIVhlTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQG 420
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-230 |
2.70e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581794297 119 LELLEKVGLTHVKDQRPHA-LSGGQQQRVAIARALAMN-PKVM-LFDEPTSALDPELVNDVLKVIKDLANEGMTMVIVTH 195
Cdd:TIGR00630 469 LGFLIDVGLDYLSLSRAAGtLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 581794297 196 E---MRFAkevsNNIVFI------HEGMIGEQGAPEEMFNRPKT 230
Cdd:TIGR00630 549 DedtIRAA----DYVIDIgpgageHGGEVVASGTPEEILANPDS 588
|
|
| |
